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1. Escherichia coli RIC is able to donate iron to iron-sulfur clusters.

Author

Lígia S Nobre, Ricardo Garcia-Serres, Smilja Todorovic, Peter Hildebrandt, Miguel Teixeira, Jean-Marc Latour, and Lígia M Saraiva

Subjects
Medicine, Science
Abstract

Escherichia coli RIC (Repair of Iron Centers) is a diiron protein previously reported to be involved in the repair of iron-sulfur proteins damaged by oxidative or nitrosative stresses, and proposed to act as an iron donor. This possible role of RIC was now examined specifically by evaluating its ability to donate iron ions to apo-iron-sulfur proteins, determining the iron binding constants and assessing the lability of its iron ions. We show, by UV-visible, EPR and resonance Raman spectroscopies that RIC may participate in the synthesis of an iron-sulfur cluster in the apo-forms of the spinach ferredoxin and IscU when in the presence of the sulfide donating system IscS and L-cysteine. Iron binding assays allowed determining the as-isolated and fully reduced RIC dissociation constants for the ferric and ferrous iron of 10-27 M and 10-13 M, respectively. Mössbauer studies revealed that the RIC iron ions are labile, namely when the center is in the mixed-valence redox form as compared with the (μ-oxo) diferric one. Altogether, these results suggest that RIC is capable of delivering iron for the formation of iron-sulfur clusters.

Published
2014
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2. The role of CyaY in iron sulfur cluster assembly on the E. coli IscU scaffold protein.

Author

Clara Iannuzzi, Salvatore Adinolfi, Barry D Howes, Ricardo Garcia-Serres, Martin Clémancey, Jean-Marc Latour, Giulietta Smulevich, and Annalisa Pastore

Subjects
Medicine, Science
Abstract

Progress in understanding the mechanism underlying the enzymatic formation of iron-sulfur clusters is difficult since it involves a complex reaction and a multi-component system. By exploiting different spectroscopies, we characterize the effect on the enzymatic kinetics of cluster formation of CyaY, the bacterial ortholog of frataxin, on cluster formation on the scaffold protein IscU. Frataxin/CyaY is a highly conserved protein implicated in an incurable ataxia in humans. Previous studies had suggested a role of CyaY as an inhibitor of iron sulfur cluster formation. Similar studies on the eukaryotic proteins have however suggested for frataxin a role as an activator. Our studies independently confirm that CyaY slows down the reaction and shed new light onto the mechanism by which CyaY works. We observe that the presence of CyaY does not alter the relative ratio between [2Fe2S](2+) and [4Fe4S](2+) but directly affects enzymatic activity.

Published
2011
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3. Catalytic Nitrene Transfer by an Fe IV ‐Imido Complex Generated by a Comproportionation Process

Author

Jordan Donat, Patrick Dubourdeaux, Martin Clémancey, Julia Rendon, Clara Gervasoni, Morgan Barbier, Jessica Barilone, Jacques Pécaut, Serge Gambarelli, Pascale Maldivi, Jean‐Marc Latour, Physiochimie des Métaux (PMB), Laboratoire de Chimie et Biologie des Métaux (LCBM - UMR 5249), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes (UGA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes (UGA), Conception d’Architectures Moléculaires et Processus Electroniques (CAMPE ), SYstèmes Moléculaires et nanoMatériaux pour l’Energie et la Santé (SYMMES), Institut des Sciences Moléculaires (ISM), Université Montesquieu - Bordeaux 4-Université Sciences et Technologies - Bordeaux 1 (UB)-École Nationale Supérieure de Chimie et de Physique de Bordeaux (ENSCPB)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Chimie Interface Biologie pour l’Environnement, la Santé et la Toxicologie (CIBEST ), and ANR-17-EURE-0003,CBH-EUR-GS,CBH-EUR-GS(2017)

Subjects
[CHIM.THEO]Chemical Sciences/Theoretical and/or physical chemistry, spectroscopy, iron, nitrene transfer, density functional calculations, tetracarbene macrocycles, Organic Chemistry, [CHIM.COOR]Chemical Sciences/Coordination chemistry, [INFO]Computer Science [cs], [CHIM.CATA]Chemical Sciences/Catalysis, General Chemistry, Catalysis
Abstract

International audience; Nitrene transfer reactions have emerged as one of the most powerful and versatile ways to insert an amine function to various kinds of hydrocarbon substrates. However, the mechanisms of nitrene generation have not been studied in depth albeit their formation is taken for granted in most cases without definitive evidence of their occurrence. In the present work, we compare the generation of tosylimido iron species and NTs transfer from Fe-II and Fe-III precursors where the metal is embedded in a tetracarbene macrocycle. Catalytic nitrene transfer to reference substrates (thioanisole, styrene, ethylbenzene and cyclohexane) revealed that the same active species was at play, irrespective of the ferrous versus ferric nature of the precursor. Through combination of spectroscopic (UV-visible, Mossbauer), ESI-MS and DFT studies, an Fe-IV tosylimido species was identified as the catalytically active species and was characterized spectroscopically and computationally. Whereas its formation from the Fe-II precursor was expected by a two-electron oxidative addition, its formation from an Fe-III precursor was unprecedented. Thanks to a combination of spectroscopic (UV-visible, EPR, Hyscore and Mossbauer), ESI-MS and DFT studies, we found that, when starting from the Fe-III precursor, an Fe-III tosyliodinane adduct was formed and decomposed into an Fe-V tosylimido species which generated the catalytically active Fe-IV tosylimide through a comproportionation process with the Fe-III precursor.

Published
2022
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4. Mixed Valence (μ‐Phenoxido) Fe II Fe III and Fe III Fe IV Compounds: Electron and Proton Transfers

Author

Patrick Dubourdeaux, Geneviève Blondin, Jean-Marc Latour, Physiochimie des Métaux (PMB), Laboratoire de Chimie et Biologie des Métaux (LCBM - UMR 5249), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes (UGA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), and Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes (UGA)

Subjects
Valence (chemistry), proton transfer, biology, Proton, Chemistry, Active site, Intervalence charge transfer, electron transfer, Photochemistry, Redox, Tautomer, Atomic and Molecular Physics, and Optics, Ion, tautomerism, Electron transfer, CPET, biology.protein, [CHIM.COOR]Chemical Sciences/Coordination chemistry, Physical and Theoretical Chemistry, mixed-valent diiron compound
Abstract

International audience; Mixed-valence non-heme diiron centers are present at the active sites of a few enzymes and confer them interesting reactivities with the two ions acting in concert. Related (μ-phenoxido)diiron complexes have been developed as enzyme mimics. They exhibit very rich spectroscopic properties enabling independent monitoring of each individual ion, which proved useful for mechanistic studies of catalytic hydrolysis and oxidation reactions. In our studies of such complexes, we observed that these compounds give rise to a wide variety of electron transfers (intervalence charge transfer), proton transfers (tautomerism), coupled electron and proton transfers (H. abstraction and PCET). In this minireview, we present and analyze the main results illustrating the latter aspects.

Published
2021
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5. Nitrene transfers mediated by natural and artificial iron enzymes

Author

Guillaume Coin, Jean-Marc Latour, Physiochimie des Métaux (PMB), Laboratoire de Chimie et Biologie des Métaux (LCBM - UMR 5249), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes (UGA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes (UGA), Département de Chimie Moléculaire - Chimie Inorganique Redox Biomimétique (DCM - CIRE ), Département de Chimie Moléculaire (DCM), Université Grenoble Alpes (UGA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes (UGA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Département de Chimie Moléculaire - Chimie Inorganique Redox (DCM - CIRE ), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes (UGA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes (UGA), and ANR-17-EURE-0003,CBH-EUR-GS,CBH-EUR-GS(2017)

Subjects
Hemeproteins, Nitrene, Iron, Nitrene transfer, Heme, [CHIM.INOR]Chemical Sciences/Inorganic chemistry, 010402 general chemistry, Protein Engineering, 01 natural sciences, Biochemistry, Catalysis, Organic molecules, Inorganic Chemistry, 03 medical and health sciences, Cytochrome P-450 Enzyme System, Nitrene precursor, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, Amines, 030304 developmental biology, Amination, 0303 health sciences, Chemistry, Hemoprotein, 0104 chemical sciences, Cyclization, Biocatalysis, Iron enzyme, Biochemical engineering, Mechanism
Abstract

International audience; Amines are ubiquitous in biology and pharmacy. As a consequence, introducing N functionalities in organic molecules is attracting strong continuous interest. The past decade has witnessed the emergence of very efficient and selective catalytic systems achieving this goal thanks to engineered hemoproteins. In this review, we examine how these enzymes have been engineered focusing rather on the rationale behind it than the meth-odology employed. These studies are put in perspective with respect to in vitro and in vivo nitrene transfer processes performed by cytochromes P450. An emphasis is put on mechanistic aspects which are confronted to current molecular knowledge of these reactions. Forthcoming developments are delineated.

Published
2021
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6. Fe‐Based Complexes as Styrene Aziridination Catalysts: Ligand Substitution Tunes Catalyst Activity

Author

Ludovic Castro, Pascale Maldivi, Martin Clémancey, Colette Lebrun, Jacques Pécaut, Guillaume Coin, Sylvie Chardon-Noblat, Patrick Dubourdeaux, Ranjan Patra, Jean-Marc Latour, Physiochimie des Métaux (PMB), Laboratoire de Chimie et Biologie des Métaux (LCBM - UMR 5249), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Département de Chimie Moléculaire (DCM), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019]), Eidgenössische Technische Hochschule - Swiss Federal Institute of Technology [Zürich] (ETH Zürich), Conception d’Architectures Moléculaires et Processus Electroniques (CAMPE), SYstèmes Moléculaires et nanoMatériaux pour l’Energie et la Santé (SYMMES), Amity Univ, AICCRS, Chimie Interface Biologie pour l’Environnement, la Santé et la Toxicologie (CIBEST ), ANR-17-EURE-0003,CBH-EUR-GS,CBH-EUR-GS(2017), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019]), Institut de Chimie du CNRS (INC)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), and Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)

Subjects
iron catalyst, 010405 organic chemistry, Ligand, Organic Chemistry, Substitution (logic), mechanism, [CHIM.CATA]Chemical Sciences/Catalysis, DFT calculations, aziridination, 010402 general chemistry, 01 natural sciences, Catalysis, 0104 chemical sciences, 3. Good health, Styrene, Inorganic Chemistry, chemistry.chemical_compound, chemistry, redox properties, Polymer chemistry, Fe based, Physical and Theoretical Chemistry, Iron catalyst
Abstract

International audience; As part of our effort to improve our understanding of aziridination mechanism, we used tetra substitution of a diphenol ligand to modify the redox properties of corresponding Fe complexes. This allowed us to confirm that aziridination catalysis by Fe-based complexes is governed by electron affinity of the active species and further show that it correlates with the Fe-III/Fe-II redox potential.

Published
2019
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7. Imidazoline synthesis: mechanistic investigations show that Fe catalysts promote a new multicomponent redox reaction

Author

Pascale Maldivi, Patrick Dubourdeaux, Jean-Marc Latour, Pierre-Alain Bayle, Guillaume Coin, Colette Lebrun, Physiochimie des Métaux (PMB), Laboratoire de Chimie et Biologie des Métaux (LCBM - UMR 5249), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes (UGA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes (UGA), Département de Chimie Moléculaire (DCM), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes (UGA), Modélisation et Exploration des Matériaux (MEM), Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Chimie Interface Biologie pour l’Environnement, la Santé et la Toxicologie (CIBEST ), SYstèmes Moléculaires et nanoMatériaux pour l’Energie et la Santé (SYMMES), Département Interfaces pour l'énergie, la Santé et l'Environnement (DIESE), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Conception d’Architectures Moléculaires et Processus Electroniques (CAMPE ), ANR-17-EURE-0003,CBH-EUR-GS,CBH-EUR-GS(2017), and Université Grenoble Alpes (UGA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)

Subjects
Coordination sphere, 010405 organic chemistry, Chemistry, Nitrene, [CHIM.CATA]Chemical Sciences/Catalysis, Aziridine, [MATH.MATH-FA]Mathematics [math]/Functional Analysis [math.FA], 010402 general chemistry, 01 natural sciences, Combinatorial chemistry, 0104 chemical sciences, Catalysis, Inorganic Chemistry, Amidine, chemistry.chemical_compound, Nucleophile, [CHIM]Chemical Sciences, Lewis acids and bases, Acetonitrile
Abstract

International audience; Multicomponent reactions are attracting strong interest because they contribute to develop more efficient synthetic chemistry. Understanding their mechanism at the molecular level is thus an important issue to optimize their operation. The development of integrated experimental and theoretical approaches has very recently emerged as most powerful to achieve this goal. In the wake of our recent investigation of amidine synthesis, we used this approach to explore how an Fe-catalyzed aziridination can lead to an imidazoline when run in acetonitrile. We report that the synthesis of imidazoline by combination of styrene, acetonitrile, an iron catalyst and a nitrene precursor occurs along a new kind of multicomponent reaction. The formation of imidazoline results from acetonitrile interception of a benzyl radical styrene aziridination intermediate within Fe coordination sphere, as opposed to classical nucleophilic opening of the aziridine by a Lewis acid. Comparison of this mechanism to that of amidine formation allows a rationalization of the modes of intermediates trapping by acetonitrile according to the oxidation state Fe active species. The molecular understanding of these processes may help to design other multicomponent reactions.

Published
2021
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8. Spin State Tunes Oxygen Atom Transfer towards Fe IV O Formation in Fe II Complexes

Author

Jean-Marc Latour, Laia Vicens, Ilaria Gamba, Carmen E. Castillo, Miquel Costas, Manuel G. Basallote, Martin Clémancey, Departamento de Ciencia de los Materiales e Ingeniería Metalúrgica, y Química Inorgánica, Institut de Química Computacional i Catàlisi and Departament de Química, Universitat de Girona (IQCC), Universitat de Girona (UdG), Physiochimie des Métaux (PMB), Laboratoire de Chimie et Biologie des Métaux (LCBM - UMR 5249), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes (UGA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), and Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes (UGA)

Subjects
Substitution reaction, Steric effects, Reaction mechanism, 010405 organic chemistry, Chemistry, Ligand, oxidation, Organic Chemistry, General Chemistry, 010402 general chemistry, 01 natural sciences, Catalysis, 0104 chemical sciences, Chemical kinetics, chemistry.chemical_compound, Crystallography, reaction mechanisms, iron, spin crossover, Spin crossover, kinetics, [CHIM.COOR]Chemical Sciences/Coordination chemistry, Acetonitrile, Trifluoromethanesulfonate
Abstract

International audience; Oxoiron(IV) complexes bearing tetradentate ligands have been extensively studied as models for the active oxidants in non-heme iron-dependent enzymes. These species are commonly generated by oxidation of their ferrous precursors. The mechanisms of these reactions have seldom been investigated. In this work, the reaction kinetics of complexes [Fe-II(CH3CN)(2)L](SbF6)(2) ([1](SbF6)(2) and [2](SbF6)(2)) and [Fe-II(CF3SO3)(2)L] ([1](OTf)(2) and [2](OTf)(2) (1, L=(Me,H)Pytacn; 2, L=(nP,H)Pytacn; (R,R ')Pytacn=1-[(6-R '-2-pyridyl)methyl]-4,7- di-R-1,4,7-triazacyclononane) with Bu4NIO4 to form the corresponding [Fe-IV(O)(CH3CN)L](2+) (3, L=(Me,H)Pytacn; 4, L=(nP,H)Pytacn) species was studied in acetonitrile/acetone at low temperatures. The reactions occur in a single kinetic step with activation parameters independent of the nature of the anion and similar to those obtained for the substitution reaction with Cl- as entering ligand, which indicates that formation of [Fe-IV(O)(CH3CN)L](2+) is kinetically controlled by substitution in the starting complex to form [Fe-II(IO4)(CH3CN)L](+) intermediates that are converted rapidly to oxo complexes 3 and 4. The kinetics of the reaction is strongly dependent on the spin state of the starting complex. A detailed analysis of the magnetic susceptibility and kinetic data for the triflate complexes reveals that the experimental values of the activation parameters for both complexes are the result of partial compensation of the contributions from the thermodynamic parameters for the spin-crossover equilibrium and the activation parameters for substitution. The observation of these opposite and compensating effects by modifying the steric hindrance at the ligand illustrates so far unconsidered factors governing the mechanism of oxygen atom transfer leading to high-valent iron oxo species.

Published
2021
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9. Experiments and DFT Computations Combine to Decipher Fe-Catalyzed Amidine Synthesis through Nitrene Transfer and Nitrile Insertion

Author

Colette Lebrun, Ranjan Patra, Guillaume Coin, Jacques Pécaut, Ludovic Castro, Pascale Maldivi, Patrick Dubourdeaux, Jean-Marc Latour, Pierre-Alain Bayle, Frédéric Avenier, Geneviève Blondin, Physiochimie des Métaux (PMB), Laboratoire de Chimie et Biologie des Métaux (LCBM - UMR 5249), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes (UGA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes (UGA), Département de Chimie Moléculaire - Chimie Inorganique Redox (DCM - CIRE ), Département de Chimie Moléculaire (DCM), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes (UGA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes (UGA), Institut de Chimie Moléculaire et des Matériaux d'Orsay (ICMMO), Institut de Chimie du CNRS (INC)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Amity Institute of Click Chemistry Research & Studies (AICCRS), Conception d’Architectures Moléculaires et Processus Electroniques (CAMPE ), SYstèmes Moléculaires et nanoMatériaux pour l’Energie et la Santé (SYMMES), Département Interfaces pour l'énergie, la Santé et l'Environnement (DIESE), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Chimie Interface Biologie pour l’Environnement, la Santé et la Toxicologie (CIBEST ), Modélisation et Exploration des Matériaux (MEM), Institut de Recherche Interdisciplinaire de Grenoble (IRIG), ANR-17-EURE-0003,CBH-EUR-GS,CBH-EUR-GS(2017), Département de Chimie Moléculaire - Chimie Inorganique Redox Biomimétique (DCM - CIRE ), and Université Grenoble Alpes (UGA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes (UGA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)

Subjects
multicomponent reaction, Nitrile, 010405 organic chemistry, nitrene transfer, Nitrene, mechanism, General Chemistry, [CHIM.CATA]Chemical Sciences/Catalysis, 010402 general chemistry, [MATH.MATH-FA]Mathematics [math]/Functional Analysis [math.FA], DFT calculations, 01 natural sciences, Combinatorial chemistry, Chemical synthesis, Catalysis, 0104 chemical sciences, Amidine, chemistry.chemical_compound, chemistry, amidine synthesis
Abstract

International audience; Multicomponent reactions are attracting strong interest as they contribute to the development of more efficient synthetic chemistry. Understanding their mechanism is thus an important issue to optimize their operation. However, it is also a challenging task owing to the complexity of the succession of molecular events involved. Computational methods have recently proven to be of utmost interest to help decipher some of these processes, and the development of integrated experimental and theoretical approaches thus appears as the most powerful means to understand these mechanisms at the molecular level. A good example is given by the synthesis of amidines which are important pharmaceutical compounds. Their synthesis requires the association of three components, often an alkyne, a secondary amine, and an organic azide as the nitrene precursor. We found that an alternative way is offered by an Fe-catalyzed combination of a hydrocarbon, a nitrile, and a nitrene which gives amidines in good yields under mild conditions. The efficiency of the transformation and the paucity of mechanistic information on these reactions prompted us to thoroughly investigate its mechanism. Several mechanistic scenarios were explored using experimental techniques, including radical trap and N-15 labeling studies, combined with density-functional theory (DFT) calculations of reaction profiles. This allowed us to show that the amidination reaction involves the trapping of an intermediate substrate cation by an Fe-released acetonitrile molecule pointing to a true multicomponent reaction occurring exclusively within the cage around the metal center. Moreover, the calculated energy barriers of the individual steps explained how amidination outweighs direct amination in these reactions. The perfect consistency between DFT results and specific experiments to validate them strongly supports these mechanistic conclusions and highlights the potency of this combined approach.

Published
2021
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10. Bioinspired symmetrical and unsymmetrical diiron complexes for selective oxidation catalysis with hydrogen peroxide

Author

Geneviève Blondin, Martin Clémancey, Jean-Pierre Mahy, Régis Guillot, Frédéric Avenier, Jean-Marc Latour, Alexandre Trehoux, Equipe de Chimie Bioorganique et Bioinorganique, Institut de Chimie Moléculaire et des Matériaux d'Orsay (ICMMO), Institut de Chimie du CNRS (INC)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Physiochimie des Métaux (PMB), Laboratoire de Chimie et Biologie des Métaux (LCBM - UMR 5249), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes (UGA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), and Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes (UGA)

Subjects
chemistry.chemical_classification, Alkane, 010405 organic chemistry, Alkene, [CHIM.CATA]Chemical Sciences/Catalysis, 010402 general chemistry, Mass spectrometry, 01 natural sciences, Redox, 0104 chemical sciences, Catalysis, Inorganic Chemistry, chemistry.chemical_compound, chemistry, Mössbauer spectroscopy, Polymer chemistry, [CHIM.COOR]Chemical Sciences/Coordination chemistry, Hydrogen peroxide, Acetonitrile
Abstract

International audience; Two new symmetrical and unsymmetrical diiron(iii) complexes were synthesized and characterized by X-ray diffraction analysis, mass spectrometry, UV-visible and Mossbauer spectroscopies. They proved to be good catalysts for alkene and alkane oxidation reactions by H2O2 in acetonitrile solution, and interesting effects of both the nature and the symmetry of the complexes were observed on catalysis in the presence of water.

Published
2020
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11. Spin State Tunes Oxygen Atom Transfer towards Fe

Author

Carmen E, Castillo, Ilaria, Gamba, Laia, Vicens, Martin, Clémancey, Jean-Marc, Latour, Miquel, Costas, and Manuel G, Basallote

Abstract

Oxoiron(IV) complexes bearing tetradentate ligands have been extensively studied as models for the active oxidants in non-heme iron-dependent enzymes. These species are commonly generated by oxidation of their ferrous precursors. The mechanisms of these reactions have seldom been investigated. In this work, the reaction kinetics of complexes [Fe

Published
2020

12. Fe-Catalyzed Aziridination Is Governed by the Electron Affinity of the Active Imido-Iron Species

Author

Jean-Marc Latour, Sam P. de Visser, Jyoti Prasad Biswas, Martin Clémancey, Debabrata Maiti, Patrick Dubourdeaux, Pascale Maldivi, Guillaume Coin, Ranjan Patra, Sujoy Rana, Physiochimie des Métaux (PMB), Laboratoire de Chimie et Biologie des Métaux (LCBM - UMR 5249), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes (UGA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes (UGA), Département de Chimie Moléculaire (DCM), Université Grenoble Alpes (UGA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Conception d’Architectures Moléculaires et Processus Electroniques (CAMPE ), SYstèmes Moléculaires et nanoMatériaux pour l’Energie et la Santé (SYMMES), Amity Institute of Click Chemistry Research & Studies (AICCRS), Department of Chemistry, University of North Bengal, Department of Chemistry,Indian Institute of Technology Bombay (IIT Bombay)), Manchester Institute of Biotechnology and Department of Chemical Engineering and Analytical Science, Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes (UGA), and ANR-17-EURE-0003,CBH-EUR-GS,CBH-EUR-GS(2017)

Subjects
chemistry.chemical_classification, catalysis, Mössbauer spectroscopy, 010405 organic chemistry, Mossbauer spectroscopy, General Chemistry, [CHIM.CATA]Chemical Sciences/Catalysis, reaction profile, 010402 general chemistry, aziridination, DFT calculations, 01 natural sciences, Combinatorial chemistry, 0104 chemical sciences, Catalysis, chemistry.chemical_compound, Enzyme, iron complexes, chemistry, Electron affinity (data page), electron affinity, [PHYS.PHYS.PHYS-CHEM-PH]Physics [physics]/Physics [physics]/Chemical Physics [physics.chem-ph], Heme
Abstract

International audience; Aziridination has very recently been found to be catalyzed by heme and nonheme Fe enzymes, opening the way to biotechnological developments. However, its mechanism is not fully understood owing to the contrasting behaviors exhibited by several Fe catalysts. Indeed, whereas a few Fe catalysts exhibit an activity dominated by inductive effects, the activity of others reveal significant and even dominant radical delocalization. Therefore, no clear and general rationale of aziridination has yet emerged. Elaborating on our previous studies, we anticipated that replacing two pyridines of a pentanitrogen ligand by two quinolines would enhance the electron affinity of the corresponding imido FeIV active species and hence its aziridination activity. This proved to be the case, and Hammett correlations indicate an electrophilic active species and dominant inductive effects. The calculated reaction profile points to a two-step mechanism with the formation of the first C-N bond being rate-determining and involving a strong charge transfer in the transition state. The aziridine ring closure in the second step is almost barrierless. A clear correlation of aziridination yields with calculated EA for Fe-catalysts indicate that the dependence of aziridination efficacy on EA of active species is a quite general feature. To generalize this analysis, we reinvestigated a catalyst exhibiting a radical delocalization dominance. Indeed, a similar two-step mechanism was found, which involves a partial charge transfer in the C-N bond formation as all other cases. The interesting point is that owing to the strong steric hindrance of the catalyst substitution, the aziridine ring closure of the intermediate benzylic radical (second step) becomes rate-determining, thus explaining the dominance of the radical delocalization effect. Eventually, a general aziridination two-step mechanism has been rationalized, and EA thus appears as the key descriptor for Fe-based catalytic aziridination that can be used in a predictable way.

Published
2020
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13. Comparative Study of the Electronic Structures of μ-Oxo, μ-Nitrido, and μ-Carbido Diiron Octapropylporphyrazine Complexes and Their Catalytic Activity in Cyclopropanation of Olefins

Author

Pascale Maldivi, Martin Clémancey, Alexander B. Sorokin, Jessica Barilone, Jean-Marc Latour, Lucie P. Cailler, Institut de recherches sur la catalyse et l'environnement de Lyon (IRCELYON), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Département Interfaces pour l'énergie, la Santé et l'Environnement (DIESE), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes (UGA), Laboratoire de Chimie et Biologie des Métaux (LCBM - UMR 5249), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), SYstèmes Moléculaires et nanoMatériaux pour l’Energie et la Santé (SYMMES), Physiochimie des Métaux (PMB), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes (UGA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Conception d’Architectures Moléculaires et Processus Electroniques (CAMPE ), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), ANR-16-CE29-0018,BICCCAT,Complexes de fer binucléaires pour réactions catalytiques difficiles(2016), and ANR-17-EURE-0003,CBH-EUR-GS,CBH-EUR-GS(2017)

Subjects
010405 organic chemistry, Cyclopropanation, Quadrupole splitting, [CHIM.CATA]Chemical Sciences/Catalysis, [CHIM.INOR]Chemical Sciences/Inorganic chemistry, 010402 general chemistry, 01 natural sciences, 0104 chemical sciences, Inorganic Chemistry, [CHIM.THEO]Chemical Sciences/Theoretical and/or physical chemistry, Crystallography, chemistry.chemical_compound, Ethyl diazoacetate, chemistry, Mössbauer spectroscopy, [CHIM]Chemical Sciences, Reactivity (chemistry), Density functional theory, [CHIM.COOR]Chemical Sciences/Coordination chemistry, Singlet state, [PHYS.PHYS.PHYS-CHEM-PH]Physics [physics]/Physics [physics]/Chemical Physics [physics.chem-ph], Physical and Theoretical Chemistry, Carbene, ComputingMilieux_MISCELLANEOUS
Abstract

International audience; The electronic structure of three single-atom bridged diiron octapropylporphyrazine complexes (FePzPr8)2X having Fe(III)-O-Fe(III), Fe(III)-N-Fe(IV) and Fe(IV)-C-Fe(IV) structural units was investigated by Mössbauer spectroscopy and density functional theory (DFT) calculations. In this series, the isomer shift values decrease, whereas the values of quadrupole splitting become progressively greater indicating the increase of covalency of Fe-X bond in the μ-oxo, μ-nitrido, μ-carbido row. The Mössbauer data point to low-spin systems for the three complexes, and calculated data with B3LYP-D3 show a singlet state for μ-oxo and μ-carbido and a doublet state for μ-nitrido complexes. An excellent agreement was obtained between B3LYP-D3 optimized geometries and X-ray structural data. Among (FePzPr8)2X complexes, μ-oxo diiron species showed a higher reactivity in the cyclopropanation of styrene by ethyl diazoacetate to afford a 95% product yield with 0.1 mol % catalyst loading. A detailed DFT study allowed to get insight into electronic structure of binuclear carbene species and to confirm their involvement into carbene transfer reactions.

Published
2020
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14. Selective Formation of an FeIV O or an FeIII OOH Intermediate From Iron(II) and H2 O2 : Controlled Heterolytic versus Homolytic Oxygen-Oxygen Bond Cleavage by the Second Coordination Sphere

Author

Frédéric Avenier, Jean-Marc Latour, Régis Guillot, Sam P. de Visser, Martin Clémancey, M. Qadri E. Mubarak, Frédéric Banse, Katell Sénéchal-David, Khaled Cheaib, Jean-Pierre Mahy, Christian Herrero, Institut de Chimie Moléculaire et des Matériaux d'Orsay (ICMMO), Université Paris-Sud - Paris 11 (UP11)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), University of Manchester [Manchester], School of Chemical Engineering and Analytical Sciences [Manchester], Physiochimie des Métaux (PMB), Laboratoire de Chimie et Biologie des Métaux (LCBM - UMR 5249), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), ANR-17-EURE-0003,CBH-EUR-GS,CBH-EUR-GS(2017), Université Paris-Sud - Paris 11 (UP11)-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), and Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])

Subjects
Coordination sphere, Chemistry, Concerted reaction, 010405 organic chemistry, General Chemistry, General Medicine, Cleavage (embryo), Photochemistry, 010402 general chemistry, Heterolysis, 01 natural sciences, Catalysis, Homolysis, 0104 chemical sciences, Electron transfer, iron complexes, O−O bond breaking, FeIV-oxo species, N ligands, [CHIM]Chemical Sciences, Reactivity (chemistry), [PHYS.PHYS.PHYS-CHEM-PH]Physics [physics]/Physics [physics]/Chemical Physics [physics.chem-ph], proton coupled electron transfer (PCET), Bond cleavage
Abstract

International audience; We demonstrate that the devised incorporation of an alkylamine group into the second coordination sphere of an FeII complex allows to switch its reactivity with H2 O2 from the usual formation of FeIII species towards the selective generation of an FeIV -oxo intermediate. The FeIV -oxo species was characterized by UV/Vis absorption and Mössbauer spectroscopy. Variable-temperature kinetic analyses point towards a mechanism in which the heterolytic cleavage of the O-O bond is triggered by a proton transfer from the proximal to the distal oxygen atom in the FeII -H2 O2 complex with the assistance of the pendant amine. DFT studies reveal that this heterolytic cleavage is actually initiated by an homolytic O-O cleavage immediately followed by a proton-coupled electron transfer (PCET) that leads to the formation of the FeIV -oxo and release of water through a concerted mechanism.

Published
2018
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15. Heteroleptic, two-coordinate [M(NHC){N(SiMe3)2}] (M = Co, Fe) complexes: synthesis, reactivity and magnetism rationalized by an unexpected metal oxidation state

Author

Andreas A. Danopoulos, Moniek Tromp, Jean-Marc Latour, Martin Clémancey, Pierre Braunstein, Kirill Yu. Monakhov, Elixabete Rezabal, Anass Benayad, Jan van Leusen, Gilles Frison, Paul Kögerler, Institut de Chimie de Strasbourg, Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC), Institute of Inorganic Chemistry [Aachen], Rheinisch-Westfälische Technische Hochschule Aachen (RWTH), Laboratoire de Chimie et Biologie des Métaux (LCBM - UMR 5249), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Laboratoire d'Innovation pour les Technologies des Energies Nouvelles et les nanomatériaux (LITEN), Institut National de L'Energie Solaire (INES), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Savoie Mont Blanc (USMB [Université de Savoie] [Université de Chambéry])-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Savoie Mont Blanc (USMB [Université de Savoie] [Université de Chambéry])-Centre National de la Recherche Scientifique (CNRS), Van't Hoff Institute for Molecular Sciences, Universiteit van Amsterdam (UvA), Laboratoire de chimie moléculaire (LCM), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-École polytechnique (X), Université de Strasbourg (UNISTRA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Institute of Inorganic Chemistry [Aachen] (IAC RWTH), Rheinisch-Westfälische Technische Hochschule Aachen University (RWTH), van ‘t Hoff Institute for Molecular Sciences, École polytechnique (X)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Catalyst Characterisation (HIMS, FNWI), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), and Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])

Subjects
010405 organic chemistry, Stereochemistry, Chemistry, 010402 general chemistry, 01 natural sciences, XANES, 0104 chemical sciences, 3. Good health, [CHIM.THEO]Chemical Sciences/Theoretical and/or physical chemistry, Inorganic Chemistry, Metal, Crystallography, Magnetization, X-ray photoelectron spectroscopy, Heteronuclear molecule, Oxidation state, visual_art, ddc:540, visual_art.visual_art_medium, [CHIM.COOR]Chemical Sciences/Coordination chemistry, Reactivity (chemistry), Isostructural
Abstract

The linear, two-coordinate and isostructural heteroleptic [M(IPr){N(SiMe3)2}] (IPr = 1,3-bis(diisopropylphenyl)-imidazol-2-ylidene), formally MI complexes (M = Co, 3; Fe, 4) were obtained by the reduction of [M(IPr)Cl{N(SiMe3)2}] with KC8, or [Co(IPr){N(SiMe3)2}2] with mes*PH2, mes* = 2,4,6-tBu3C6H2. The magnetism of 3 and 4 implies CoII and FeII centres coupled to one ligand-delocalized electron, in line with XPS and XANES data; the ac susceptibility of 4 detected a pronounced frequency dependence due to slow magnetization relaxation. Reduction of [Fe(IPr)Cl{N(SiMe3)2}] with excess KC8 in toluene gave the heteronuclear ‘inverse-sandwich’ Fe–K complex 7, featuring η6-toluene sandwiched between one Fe0 and one K+ centre.

Published
2017
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16. Understanding Active Sites in Pyrolyzed Fe–N–C Catalysts for Fuel Cell Cathodes by Bridging Density Functional Theory Calculations and 57 Fe Mössbauer Spectroscopy

Author

Martin Clémancey, Jean-Marc Latour, Tzonka Mineva, Moulay Tahar Sougrati, Frédéric Jaouen, Lorenzo Stievano, Plamen Atanassov, Amélie Kochem, Ivana Matanovic, Institut Charles Gerhardt Montpellier - Institut de Chimie Moléculaire et des Matériaux de Montpellier (ICGM), Ecole Nationale Supérieure de Chimie de Montpellier (ENSCM)-Institut de Chimie du CNRS (INC)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), Theoretical Division [LANL], Los Alamos National Laboratory (LANL), Center For Emerging Energy Technologies [Albuquerque] (CEET), The University of New Mexico [Albuquerque], Physiochimie des Métaux (PMB), Laboratoire de Chimie et Biologie des Métaux (LCBM - UMR 5249), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), ANR-10-LABX-0005,CheMISyst,CHEmistry of Molecular and Interfacial Systems(2010), European Project: 779366,CRESCENDO, Institut Charles Gerhardt Montpellier - Institut de Chimie Moléculaire et des Matériaux de Montpellier (ICGM ICMMM), Ecole Nationale Supérieure de Chimie de Montpellier (ENSCM)-Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM)-Université Montpellier 1 (UM1)-Université Montpellier 2 - Sciences et Techniques (UM2)-Institut de Chimie du CNRS (INC), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), and Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])

Subjects
cathode, Bridging (networking), Materials science, Spin states, Mossbauer spectroscopy, 010402 general chemistry, 01 natural sciences, Catalysis, law.invention, fuel cell, law, Mössbauer spectroscopy, quadrupole energy splitting, density functional theory, 010405 organic chemistry, General Chemistry, [CHIM.CATA]Chemical Sciences/Catalysis, Cathode, 0104 chemical sciences, oxygen reduction, Fe-N-C, Membrane, Chemical engineering, Density functional theory, Pyrolysis, FeN4
Abstract

International audience; Pyrolyzed Fe-N-C materials are promising platinum-group-metal-free catalysts for proton-exchange membrane fuel cell cathodes. However, the detailed structure, oxidation, and spin states of their active sites are still undetermined. Fe-57 Mossbauer spectroscopy has identified FeNx moieties as the most active sites, with their fingerprint being a doublet in low-temperature Mossbauer spectra. However, the interpretation of the doublets for such materials has lacked theoretical basis. Here, we applied density functional theory to calculate the quadrupole splitting energy of doublets (Delta E-QS) for a range of FeNx structures in different oxidation and spin states. The calculated and experimental values are then compared for a reference Fe-N-C catalyst, whereas further information on the Fe oxidation and spin states was obtained from electron paramagnetic resonance, superconducting quantum interference device, and Fe-57 Mossbauer spectroscopy under external magnetic field. The combined theoretical and experimental results identify the main presence of FeNx moieties in Fe(II) low-spin and Fe(III) high-spin states, whereas a minor fraction of sites could exist in the Fe(II) S = 1 state. From the analysis of the Fe-57 Mossbauer spectrum under the external magnetic field and the comparison of calculated and measured Delta E-QS values, we assign the experimental doublet D1 with a mean Delta E-QS value of around 0.9 mm.s(-1) to Fe(III)N4C12 moieties in high-spin state and the experimental doublet D2 with a mean Delta E-QS value of around 2.3 mm.s(-1) to Fe(II)N4C10 moieties in low and medium spin. These conclusions indicate that D1 corresponds to surface-exposed sites, whereas D2 may correspond either to bulk sites that are inaccessible to O-2 or to surface sites that bind O-2 weaker than D1.

Published
2019
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17. Design of specific inhibitors of quinolinate synthase based on [4Fe-4S] cluster coordination

Author

J. Saez Cabodevilla, Anne Volbeda, Martin Clémancey, Jean-Marc Latour, Juan-Carlos Fontecilla-Camps, Patricia Amara, S. Ollagnier de Choudens, Claudine Darnault, Océane Gigarel, Olivier Hamelin, Debora Reichmann, Biocatalyse (BIOCAT ), Laboratoire de Chimie et Biologie des Métaux (LCBM - UMR 5249), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019]), Groupe Métalloprotéines (IBS-METALLO ), Institut de biologie structurale (IBS - UMR 5075 ), Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), Catalyse Bioinorganique et Environnement (BioCE ), Physiochimie des Métaux (PMB), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), ANR-16-CE18-0026,NADIN,BIOSYNTHESE DU NAD: VERS LA DECOUVERTE DE NOUVEAUX ANTIBACTERIENS(2016), and ANR-17-EURE-0003,CBH-EUR-GS,CBH-EUR-GS(2017)

Subjects
010402 general chemistry, 01 natural sciences, Catalysis, Cofactor, 03 medical and health sciences, chemistry.chemical_compound, Materials Chemistry, Transferase, 030304 developmental biology, chemistry.chemical_classification, 0303 health sciences, ATP synthase, biology, Metals and Alloys, General Chemistry, [CHIM.CATA]Chemical Sciences/Catalysis, Quinolinate, 0104 chemical sciences, Surfaces, Coatings and Films, Electronic, Optical and Magnetic Materials, Enzyme, chemistry, Biochemistry, Ceramics and Composites, biology.protein, NAD+ kinase, Quinolinic acid
Abstract

International audience; Quinolinate synthase (NadA) is a [4Fe-4S] cluster-containing enzyme involved in the formation of quinolinic acid, the precursor of the essential NAD coenzyme. Here, we report the synthesis and activity of derivatives of the first inhibitor of NadA. Using multidisciplinary approaches we have investigated their action mechanism and discovered additional specific inhibitors of this enzyme.

Published
2019
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18. Model peptide for anti-sigma factor domain HHCC zinc fingers: high reactivity toward 1O2 leads to domain unfolding

Author

Vincent Lebrun, Jean-Marc Latour, Olivier Sénèque, Colette Lebrun, Valentin Chabert, Physiochimie des Métaux (PMB), Laboratoire de Chimie et Biologie des Métaux (LCBM - UMR 5249), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Chimie Interface Biologie pour l’Environnement, la Santé et la Toxicologie (CIBEST ), SYstèmes Moléculaires et nanoMatériaux pour l’Energie et la Santé (SYMMES), ANR-17-EURE-0003,CBH-EUR-GS,CBH-EUR-GS(2017), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019]), Institut de Chimie du CNRS (INC)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), and Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)

Subjects
chemistry.chemical_classification, Zinc finger, Circular dichroism, Reactive oxygen species, 010405 organic chemistry, Singlet oxygen, Stereochemistry, chemistry.chemical_element, Peptide, General Chemistry, Zinc, 010402 general chemistry, 01 natural sciences, 0104 chemical sciences, chemistry.chemical_compound, Reaction rate constant, chemistry, Peptide synthesis, [CHIM]Chemical Sciences
Abstract

International audience; All organisms have to cope with the deleterious effects of reactive oxygen species. Some of them are able to mount a transcriptional response to various oxidative stresses, which involves sensor proteins capable of assessing the redox status of the cell or to detect reactive oxygen species. In this article, we describe the design, synthesis and characterization of Zn·LASD(HHCC), a model for the Zn(Cys)2(His)2 zinc finger site of ChrR, a sensor protein involved in the bacterial defence against singlet oxygen that belongs to the family of zinc-binding anti-sigma factors possessing a characteristic H/C–X24/25–H–X3–C–X2–C motif. The 46-amino acid model peptide LASD(HHCC) was synthetized by solid phase peptide synthesis and its Zn2+-binding properties were investigated using electronic absorption, circular dichroism and NMR. LASD(HHCC) forms a 1 : 1 complex with Zn2+, namely Zn·LASD(HHCC), that adopts a well-defined conformation with the Zn2+ ion capping a 3-helix core that reproduces almost perfectly the fold of the ChrR in the vicinity of its zinc site. H2O2 reacts with Zn·LASD(HHCC) to yield a disulfide with a second order rate constant of 0.030 ± 0.002 M−1 s−1. Zn·LASD(HHCC) reacts rapidly with singlet oxygen to yield sulfinates and sulfonates. A lower limit of the chemical reaction rate constant between Zn·LASD(HHCC) and 1O2 was determined to be 3.9 × 106 M−1 s−1. Therefore, the Zn(Cys)2(His)2 site of Zn·LASD(HHCC) appears to be at least 5 times more reactive toward these two oxidants than that of a classical ββα zinc finger. Consequences for the activation mechanism of ChrR are discussed.

Published
2019
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19. Design of Iron Coordination Complexes as Highly Active Homogenous Water Oxidation Catalysts by Deuteration of Oxidation-Sensitive Sites

Author

Ferran Acuña-Parés, Julio Lloret-Fillol, Zoel Codolà, Carla Casadevall, Ilaria Gamba, Jean-Marc Latour, Josep M. Luis, Miquel Costas, Martin Clémancey, Institut de Química Computacional i Catàlisi and Departament de Química, Universitat de Girona (IQCC), Universitat de Girona (UdG), Institute of Chemical Research of Catalonia (ICIQ), Barcelona Institute of Science and Technology (BIST), Physiochimie des Métaux (PMB), Laboratoire de Chimie et Biologie des Métaux (LCBM - UMR 5249), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019]), Institució Catalana de Recerca i Estudis Avançats (ICREA), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), ANR-17-EURE-0003,CBH-EUR-GS,CBH-EUR-GS(2017), and Ministerio de Economía y Competitividad (Espanya)

Subjects
chemistry.chemical_classification, Chemistry, Ligand, General Chemistry, [CHIM.CATA]Chemical Sciences/Catalysis, Oxidació, 010402 general chemistry, 01 natural sciences, Biochemistry, Chemical reaction, Medicinal chemistry, Redox, Catalysis, Reaccions químiques, 0104 chemical sciences, Coordination complex, Reaction rate, Colloid and Surface Chemistry, Chemical reactions, Oxidation, Oxidizing agent, [CHIM.COOR]Chemical Sciences/Coordination chemistry, [PHYS.PHYS.PHYS-CHEM-PH]Physics [physics]/Physics [physics]/Chemical Physics [physics.chem-ph], Trifluoromethanesulfonate
Abstract

Data de publicació online és 30 de novembbre de 2018, malgrat que apareix publicat en una revista del 2019 The nature of the oxidizing species in water oxidation reactions with chemical oxidants catalyzed by α-[Fe(OTf)2(mcp)] (1α; mcp = N,N′-dimethyl-N,N′-bis(pyridin-2-ylmethyl)cyclohexane-1,2-diamine, OTf = trifluoromethanesulfonate anion) and β-[Fe(OTf)2(mcp)] (1β) has been investigated. Mössbauer spectroscopy provides definitive evidence that 1α and 1β generate oxoiron(IV) species as the resting state. Decomposition paths of the catalysts have been investigated by identifying and quantifying ligand fragments that form upon degradation. This analysis correlates the water oxidation activity of 1α and 1β with stability against oxidative damage of the ligand via aliphatic C-H oxidation. The site of degradation and the relative stability against oxidative degradation are shown to be dependent on the topology of the catalyst. Furthermore, the mechanisms of catalyst degradation have been rationalized by computational analyses, which also explain why the topology of the catalyst enforces different oxidation-sensitive sites. This information has served in creating catalysts where sensitive C-H bonds have been replaced by C-D bonds. The deuterated analogues D4-α-[Fe(OTf)2(mcp)] (D4-1α), D4-β-[Fe(OTf)2(mcp)] (D4-1β), and D6-β-[Fe(OTf)2(mcp)] (D6-1β) were prepared, and their catalytic activity has been studied. D4-1α proves to be an extraordinarily active and efficient catalyst (up to 91% of O2 yield); it exhibits initial reaction rates identical with those of its protio analogue, but it is substantially more robust toward oxidative degradation and yields more than 3400 TON (n(O2)/n(Fe)). Altogether this evidences that the water oxidation catalytic activity is performed by a well-defined coordination complex and not by iron oxides formed after oxidative degradation of the ligands We acknowledge the Spanish Ministry of Science CTQ2015-70795-P (M. C.), CTQ2016- 80038-R (J. LL. F.), CTQ2014-59212-P (J. M. Lluis). We would like to thank the European Commission for the ERC-CG-2014-648304 (J.Ll.-F) project

Published
2019
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20. A Mononuclear Nonheme Iron(IV)–Amido Complex Relevant for the Compound II Chemistry of Cytochrome P450

Author

Shunichi Fukuzumi, Martin Clémancey, Mi Sook Seo, Ritimukta Sarangi, Yong Min Lee, Xiaoyan Lu, Xiao Xi Li, Wonwoo Nam, Jean-Marc Latour, Pascale Maldivi, Department of Chemistry and Nano Science, EWHA Womans University (EWHA), Physiochimie des Métaux (PMB), Laboratoire de Chimie et Biologie des Métaux (LCBM - UMR 5249), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019]), Conception d’Architectures Moléculaires et Processus Electroniques (CAMPE), SYstèmes Moléculaires et nanoMatériaux pour l’Energie et la Santé (SYMMES), Institut de Chimie du CNRS (INC)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), Département Interfaces pour l'énergie, la Santé et l'Environnement (DIESE), Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Stanford Synchrotron Radiation Lightsource (SSRL SLAC), SLAC National Accelerator Laboratory (SLAC), Stanford University-Stanford University, Lanzhou Institute of Chemical Physics (LICP), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), and Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG)

Subjects
biology, Chemistry, Extramural, Iron, Cytochrome P450, General Chemistry, Hydrogen atom, 010402 general chemistry, 01 natural sciences, Biochemistry, Medicinal chemistry, Amides, Catalysis, Nonheme iron, Article, 0104 chemical sciences, [CHIM.THEO]Chemical Sciences/Theoretical and/or physical chemistry, Colloid and Surface Chemistry, Cytochrome P-450 Enzyme System, Coordination Complexes, biology.protein, Macrocyclic ligand
Abstract

International audience; A mononuclear nonheme iron(IV)–amido complex bearing a tetraamido macrocyclic ligand, [(TAML)FeIV(NHTs)]− (1), was synthesized via a hydrogen atom (H atom) abstraction reaction of an iron(V)–imido complex, [(TAML)FeV(NTs)]− (2), and fully characterized using various spectroscopies. We then investigated (1) the pKa of 1, (2) the reaction of 1 with a carbon-centered radical, and (3) the H atom abstraction reaction of 1. To the best of our knowledge, the present study reports for the first time the synthesis and chemical properties/reactions of a high-valent iron(IV)–amido complex.

Published
2019
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21. Intramolecular Electron Transfers Thwart Bistability in a Pentanuclear Iron Complex

Author

Bertrand Gerey, Jacques Pécaut, Eric Gouré, Jean-Marc Latour, Martin Clémancey, Geneviève Blondin, Florian Molton, Marie-Noëlle Collomb, Département de Chimie Moléculaire (DCM), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019]), Laboratoire de Chimie et Biologie des Métaux (LCBM - UMR 5249), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019]), Reconnaissance Ionique et Chimie de Coordination (RICC), SYstèmes Moléculaires et nanoMatériaux pour l’Energie et la Santé (SYMMES), Institut de Chimie du CNRS (INC)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), and Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG)

Subjects
Spin states, 010405 organic chemistry, Chemistry, Inorganic chemistry, Electron, [CHIM.INOR]Chemical Sciences/Inorganic chemistry, 010402 general chemistry, 01 natural sciences, Redox, 0104 chemical sciences, Ion, Inorganic Chemistry, Crystallography, chemistry.chemical_compound, Intramolecular force, Mössbauer spectroscopy, [CHIM.COOR]Chemical Sciences/Coordination chemistry, Bulk electrolysis, Physical and Theoretical Chemistry, Acetonitrile
Abstract

International audience; With the intention to investigate the redox properties of polynuclear complexes as previously reported for the pentamanganese complex [{Mn(II)(μ-bpp)3}2Mn(III)Mn(II)2(μ3-O)](3+) (2(3+)), we focused on the analogous pentairon complex that was previously isolated as all-ferrous. As Masaoka and co-workers recently published, aerobic synthesis leads to the [{Fe(II)(μ-bpp)3}2Fe(III)Fe(II)2(μ3-O)](3+) complex (1(3+)). This species exhibits in acetonitrile solution four reversible one-electron oxidation waves. Accordingly, the three oxidized species 1(4+), 1(5+), and 1(6+) with a 3Fe(II)2Fe(III), 2Fe(II)3Fe(III), and 1Fe(II)4Fe(III) composition, respectively, were generated by bulk electrolysis and isolated. Mössbauer spectroscopy allowed us to determine the spin states of all the iron ions and to unambiguously locate the sites of the successive oxidations. They all occur in the μ3-oxo core except for the 1(4+) to 1(5+) process that presents a striking electronic rearrangement, with both metals in axial position being oxidized while the core is reduced to the [Fe(III)Fe(II)2(μ3-O)](5+) oxidation level. This strongly differs from the redox behavior of the Mn5 system. The origin of this electronic switch is discussed.

Published
2016
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22. Reaction of PerR with Molecular Oxygen May Assist H2O2 Sensing in Anaerobes

Author

Eric Gouré, Ramakrishnan Sethu, Luca Signor, Martin Clémancey, Jean-Marc Latour, Victor Duarte, Christelle Caux-Thang, Laboratoire de Chimie et Biologie des Métaux (LCBM - UMR 5249), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Institut de biologie structurale (IBS - UMR 5075 ), Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), and Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG)

Subjects
DNA, Bacterial, 0301 basic medicine, Staphylococcus aureus, 030106 microbiology, Microbial metabolism, Regulator, medicine.disease_cause, Bioinformatics, Biochemistry, Peroxide, Bacteria, Anaerobic, 03 medical and health sciences, chemistry.chemical_compound, Bacterial Proteins, medicine, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, chemistry.chemical_classification, biology, Pathogenic bacteria, Hydrogen Peroxide, General Medicine, biology.organism_classification, [SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology, Oxygen, Repressor Proteins, Enzyme, chemistry, Molecular Medicine, Oxidation-Reduction, DNA, Bacteria, Bacillus subtilis
Abstract

International audience; PerR is the peroxide resistance regulator found in several pathogenic bacteria and governs their resistance to peroxide stress by inducing enzymes that destroy peroxides. However, it has recently been implicated as a key component of the aerotolerance in several facultative or strict anaerobes, including the highly pathogenic Staphylococcus aureus. By combining (18)O labeling studies to ESI- and MALDI-TOF MS detection and EMSA experiments, we demonstrate that the active form of PerR reacts with dioxygen, which leads ultimately to disruption of the PerR/DNA complex and is thus physiologically meaningful. Moreover, we show that the presence of O2 assists PerR sensing of H2O2, another feature likely to be important for anaerobic organisms. These results allow one to envisage different scenarios for the response of anaerobes to air exposure.

Published
2016
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23. Selective Formation of an Fe

Author

Khaled, Cheaib, M Qadri E, Mubarak, Katell, Sénéchal-David, Christian, Herrero, Régis, Guillot, Martin, Clémancey, Jean-Marc, Latour, Sam P, de Visser, Jean-Pierre, Mahy, Frédéric, Banse, and Frédéric, Avenier

Abstract

We demonstrate that the devised incorporation of an alkylamine group into the second coordination sphere of an Fe

Published
2018

24. Trinuclear copper complexes as biological mimics: Ligand designs and reactivities

Author

Lionel Dubois, Elena Salvadeo, Jean-Marc Latour, Laboratoire de Chimie et Biologie des Métaux (LCBM - UMR 5249), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), SYstèmes Moléculaires et nanoMatériaux pour l’Energie et la Santé (SYMMES), ANR-11-LABX-0003,ARCANE,Grenoble, une chimie bio-motivée(2011), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019]), Institut de Chimie du CNRS (INC)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), and Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)

Subjects
chemistry.chemical_element, Phosphate esters hydrolysis, 010402 general chemistry, 01 natural sciences, Ligand design, Inorganic Chemistry, Materials Chemistry, Oxygen reduction reaction, Reactivity (chemistry), [CHIM.COOR]Chemical Sciences/Coordination chemistry, Metal catalyst, Physical and Theoretical Chemistry, Binding site, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], Dioxygen activation, biology, 010405 organic chemistry, Ligand, Active site, Combinatorial chemistry, Copper, Tris-copper centers, 0104 chemical sciences, chemistry, biology.protein, Molecular oxygen
Abstract

International audience; Tris-copper centers are present at the active site of multicopper oxidases (MCO) which couple the four electron reduction of molecular oxygen to water with the oxidation of substrates. Modelling these sites with small molecular complexes has thus attracted the interest of many groups in the (bio)inorganic community over the past three decades and still appears a challenge. These enzymes and their model complexes presently enjoy a renewed interest as potential non-precious metal catalyst for the Oxygen Reduction Reaction. Moreover recent work has revealed that tris-copper centers can catalyze methane oxidation. Therefore the elaboration of tris-copper system constitutes an important and timely issue. The aim of the present review is to analyze the various attempts at preparing tris-copper complexes in terms of strategy of ligand design. Of course the challenge to be met is to force three independent binding sites to converge and react in concert. Three main approaches have been developed to anchor these binding sites based on the use of (i) a node either (a) a single atom node (tren-based systems and related), or (b) an hexa-atom node (mesityl-based systems and derivatives), (ii) macrocyclic systems, and (iii) combination of mono- and dinuclear sites. The structures of the different systems will be described and analyzed accordingly. Then the various reactivities exhibited by these systems will be presented so as to evaluate how the ligand design influences the reactivity and to discern promising future directions.

Published
2018
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25. Selective C–H halogenation over hydroxylation by non-heme iron(IV)-oxo

Author

Martin Clémancey, Jean-Marc Latour, Debabrata Maiti, Gopalan Rajaraman, Jyoti Prasad Biswas, Asmita Sen, Sujoy Rana, Geneviève Blondin, Department of Chemistry [Mumbai], Indian Institute of Technology Bombay (IIT Bombay), Laboratoire de Chimie et Biologie des Métaux (LCBM - UMR 5249), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019]), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), and Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)

Subjects
chemistry.chemical_classification, inorganic chemicals, 010405 organic chemistry, Ligand, Halide, Halogenation, General Chemistry, 010402 general chemistry, Hydrogen atom abstraction, 01 natural sciences, Medicinal chemistry, 0104 chemical sciences, Hydroxylation, chemistry.chemical_compound, Chemistry, Enzyme, chemistry, Halogen, [CHIM]Chemical Sciences, Selectivity
Abstract

Synthetic non-heme iron-oxo and iron-halide complexes promote selective halogenation of the sp3-C–H bonds via hydrogen atom abstraction and halide rebound phenomenon., Non-heme iron based halogenase enzymes promote selective halogenation of the sp3-C–H bond through iron(iv)-oxo-halide active species. During halogenation, competitive hydroxylation can be prevented completely in enzymatic systems. However, synthetic iron(iv)-oxo-halide intermediates often result in a mixture of halogenation and hydroxylation products. In this report, we have developed a new synthetic strategy by employing non-heme iron based complexes for selective sp3-C–H halogenation by overriding hydroxylation. A room temperature stable, iron(iv)-oxo complex, [Fe(2PyN2Q)(O)]2+ was directed for hydrogen atom abstraction (HAA) from aliphatic substrates and the iron(ii)-halide [FeII(2PyN2Q)(X)]+ (X, halogen) was exploited in conjunction to deliver the halogen atom to the ensuing carbon centered radical. Despite iron(iv)-oxo being an effective promoter of hydroxylation of aliphatic substrates, the perfect interplay of HAA and halogen atom transfer in this work leads to the halogenation product selectively by diverting the hydroxylation pathway. Experimental studies outline the mechanistic details of the iron(iv)-oxo mediated halogenation reactions. A kinetic isotope study between PhCH3 and C6D5CD3 showed a value of 13.5 that supports the initial HAA step as the RDS during halogenation. Successful implementation of this new strategy led to the establishment of a functional mimic of non-heme halogenase enzymes with an excellent selectivity for halogenation over hydroxylation. Detailed theoretical studies based on density functional methods reveal how the small difference in the ligand design leads to a large difference in the electronic structure of the [Fe(2PyN2Q)(O)]2+ species. Both experimental and computational studies suggest that the halide rebound process of the cage escaped radical with iron(iii)-halide is energetically favorable compared to iron(iii)-hydroxide and it brings in selective formation of halogenation products over hydroxylation.

Published
2018
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26. Contribution of Mössbauer spectroscopy to the investigation of Fe/S biogenesis

Author

Martin Clémancey, Geneviève Blondin, Jean-Marc Latour, Ricardo Garcia-Serres, Laboratoire de Chimie et Biologie des Métaux (LCBM - UMR 5249), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019]), ANR-14-CE09-0026,FRATISCA,Mieux comprendre les stades précoces et tardifs de l'assemblage des noyaux Fe-S dans la mitochondrie(2014), ANR-11-LABX-0003,ARCANE,Grenoble, une chimie bio-motivée(2011), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), and Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)

Subjects
0301 basic medicine, 030102 biochemistry & molecular biology, biology, Chemistry, Iron–sulfur cluster, Vacuole, Mitochondrion, [CHIM.INOR]Chemical Sciences/Inorganic chemistry, Biochemistry, Inorganic Chemistry, 03 medical and health sciences, Cytosol, chemistry.chemical_compound, 030104 developmental biology, Iron-sulfur protein, Mössbauer spectroscopy, biology.protein, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, [PHYS.PHYS.PHYS-CHEM-PH]Physics [physics]/Physics [physics]/Chemical Physics [physics.chem-ph], Spectroscopy, Biogenesis
Abstract

Fe/S cluster biogenesis involves a complex machinery comprising several mitochondrial and cytosolic proteins. Fe/S cluster biosynthesis is closely intertwined with iron trafficking in the cell. Defects in Fe/S cluster elaboration result in severe diseases such as Friedreich ataxia. Deciphering this machinery is a challenge for the scientific community. Because iron is a key player, 57Fe-Mossbauer spectroscopy is especially appropriate for the characterization of Fe species and monitoring the iron distribution. This minireview intends to illustrate how Mossbauer spectroscopy contributes to unravel steps in Fe/S cluster biogenesis. Studies were performed on isolated proteins that may be present in multiple protein complexes. Since a few decades, Mossbauer spectroscopy was also performed on whole cells or on isolated compartments such as mitochondria and vacuoles, affording an overview of the iron trafficking. This minireview aims at presenting selected applications of 57Fe-Mossbauer spectroscopy to Fe/S cluster biogenesis.

Published
2018
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27. Development of a rubredoxin-type center embedded in a de novo designed three-helix bundle

Author

Tyler B. J. Pinter, Jean-Marc Latour, Vincent L. Pecoraro, Geneviève Blondin, Alison G. Tebo, Nicolai Lehnert, Ricardo Garcia-Serres, Cédric Tard, Olivier Sénèque, Amy L. Speelman, James E. Penner-Hahn, University of Michigan [Ann Arbor], University of Michigan System, Department of Chemistry and Biophysics, University of Michigan, University of Michigan System-University of Michigan System, Laboratoire de Chimie et Biologie des Métaux (LCBM - UMR 5249), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019]), Laboratoire de chimie moléculaire (LCM), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-École polytechnique (X), ANR-11-LABX-0003,ARCANE,Grenoble, une chimie bio-motivée(2011), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), and École polytechnique (X)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)

Subjects
Models, Molecular, Protein Conformation, alpha-Helical, Circular dichroism, Iron, Protein design, 010402 general chemistry, Ferric Compounds, 01 natural sciences, Biochemistry, Article, law.invention, Electron Transport, Electron transfer, Protein structure, law, Rubredoxin, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, Electron paramagnetic resonance, Helix bundle, 010405 organic chemistry, Magnetic circular dichroism, Chemistry, Circular Dichroism, Rubredoxins, Electron Spin Resonance Spectroscopy, 0104 chemical sciences, [SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biophysics, Crystallography, Oxidation-Reduction
Abstract

Protein design is a powerful tool for interrogating the basic requirements for the function of a metal site in a way that allows for the selective incorporation of elements that are important for function. Rubredoxins are small electron transfer proteins with a reduction potential centered near 0 mV (vs normal hydrogen electrode). All previous attempts to design a rubredoxin site have focused on incorporating the canonical CXXC motifs in addition to reproducing the peptide fold or using flexible loop regions to define the morphology of the site. We have produced a rubredoxin site in an utterly different fold, a three-helix bundle. The spectra of this construct mimic the ultraviolet–visible, Mössbauer, electron paramagnetic resonance, and magnetic circular dichroism spectra of native rubredoxin. Furthermore, the measured reduction potential suggests that this rubredoxin analogue could function similarly. Thus, we have shown that an α-helical scaffold sustains a rubredoxin site that can cycle with the desired potential between the Fe(II) and Fe(III) states and reproduces the spectroscopic characteristics of this electron transport protein without requiring the classic rubredoxin protein fold.

Published
2018
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28. Achieving One-Electron Oxidation of a Mononuclear Nonheme Iron(V)-Imido Complex

Author

Jean-Marc Latour, Xiaoyan Lu, Takehiro Ohta, Takashi Ogura, Seungwoo Hong, Wonwoo Nam, Ritimukta Sarangi, Pascale Maldivi, Yong Min Lee, Mi Sook Seo, Martin Clémancey, Department of Chemistry and Nano Science, EWHA Womans University (EWHA), Department of Chemistry, Sookmyung Women's University , Seoul 04310, Korea., Picobiology Institute, Graduate School of Life Science, University of Hyogo, Laboratoire de Chimie et Biologie des Métaux (LCBM - UMR 5249), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), SYstèmes Moléculaires et nanoMatériaux pour l’Energie et la Santé (SYMMES), Institut de Chimie du CNRS (INC)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), Stanford Synchrotron Radiation Lightsource (SSRL SLAC), SLAC National Accelerator Laboratory (SLAC), Stanford University-Stanford University, Lanzhou Institute of Chemical Physics, Chinese Academy of Sciences, Lanzhou 730000, China, ANR-11-LABX-0003,ARCANE,Grenoble, une chimie bio-motivée(2011), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), and Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])

Subjects
Stereochemistry, Nitrene, Iron, Electrons, 010402 general chemistry, Ligands, 01 natural sciences, Biochemistry, Medicinal chemistry, Catalysis, Antiferromagnetic coupling, Article, Colloid and Surface Chemistry, Reactivity (chemistry), [CHIM.COOR]Chemical Sciences/Coordination chemistry, Cation radical, 010405 organic chemistry, Ligand, Chemistry, Hydrogen bond, General Chemistry, Nonheme iron, 0104 chemical sciences, Macrocyclic ligand, Imines, Oxidation-Reduction
Abstract

International audience; A mononuclear nonheme iron(V)-imido complex bearing a tetraamido macrocyclic ligand (TAML), [FeV(NTs)(TAML)]- (1), was oxidized by one-electron oxidants, affording formation of an iron(V)-imido TAML cation radical species, [FeV(NTs)(TAML+•)] (2); 2 is a diamagnetic (S = 0) complex, resulting from the antiferromagnetic coupling of the low-spin iron(V) ion (S = 1/2) with the one-electron oxidized ligand (TAML+•). 2 is a competent oxidant in C-H bond functionalization and nitrene transfer reaction, showing that the reactivity of 2 is greater than that of 1.

Published
2017
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29. Rational design of Fe catalysts for olefin aziridination through DFT-based mechanistic analysis

Author

Patrick Dubourdeaux, Pascale Maldivi, Ludovic Castro, Martin Clémancey, Colette Lebrun, Guillaume Coin, Ranjan Patra, Jean-Marc Latour, Jacques Pécaut, Laboratoire de Chimie et Biologie des Métaux (LCBM - UMR 5249), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Panjab University [Chandigarh], Conception d’Architectures Moléculaires et Processus Electroniques (CAMPE), SYstèmes Moléculaires et nanoMatériaux pour l’Energie et la Santé (SYMMES), Institut de Chimie du CNRS (INC)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), Département de Chimie Moléculaire (DCM), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019]), Chimie Interface Biologie pour l’Environnement, la Santé et la Toxicologie (CIBEST ), ANR-11-LABX-0003,ARCANE,Grenoble, une chimie bio-motivée(2011), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), and Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])

Subjects
Olefin fiber, 010405 organic chemistry, Chemistry, Nitrene, Rational design, Electronic structure, [CHIM.CATA]Chemical Sciences/Catalysis, 010402 general chemistry, Photochemistry, 01 natural sciences, Catalysis, 0104 chemical sciences, Computational chemistry, Mechanism (philosophy), Electron affinity, Amine derivatives
Abstract

International audience; Nitrene transfer reactions are increasingly used to access various kinds of amine derivatives but the underlying mechanisms have not been unraveled in most cases. Fe-catalyzed aziridination of alkenes has appeared as a promising route to aziridines which are important derivatives both per se and as intermediates in many synthetic procedures. We report the strong activity and the mechanism of di-iron catalysts for aziridination of styrenes using phenyltosyliodinane (PhI[double bond, length as m-dash]NTs). In addition, we have developed a similar mono-iron catalyst which operates under the same mechanism albeit with a reduced activity. DFT calculations were performed to investigate the structure and electronic structure of the FeIVNTs species of the latter catalyst. They suggest that the reaction pathway leading to the nitrene transfer to the olefin involves a transient charge transfer on the way to a radical intermediate, which is totally consistent with the experimental results. Moreover, these calculations identify the electron affinity (EA) of the active species as one key parameter allowing rationalization of the observations, which opens the way to improving the catalyst efficiency on a rational basis.

Published
2017
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30. Spectroscopic evidence for cofactor-substrate interaction in the radical-SAM enzyme TYW1

Author

Farhad Forouhar, Serge Gambarelli, Ricardo Garcia-Serres, Jean-Marc Latour, Mohamed G. Atta, Phanélie Perche-Letuvée, Velavan Kathirvelu, Conception d’Architectures Moléculaires et Processus Electroniques (CAMPE), SYstèmes Moléculaires et nanoMatériaux pour l’Energie et la Santé (SYMMES), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Laboratoire de Chimie et Biologie des Métaux (LCBM - UMR 5249), Columbia University [New York], ANR-10-BLAN-0737,INSERAD,Modifications post-transcriptionnelles des ARNs de transfert par insertion radicalaire.(2010), ANR-11-LABX-0003,ARCANE,Grenoble, une chimie bio-motivée(2011), Institut de Chimie du CNRS (INC)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), and Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])

Subjects
0301 basic medicine, Iron-Sulfur Proteins, Pyrococcus abyssi, S-Adenosylmethionine, Stereochemistry, Carboxy-Lyases, Radical, Archaeal Proteins, Coenzymes, Guanosine, Cofactor, Substrate Specificity, Inorganic Chemistry, 03 medical and health sciences, chemistry.chemical_compound, Spectroscopy, Mossbauer, Pyruvic Acid, Moiety, [CHIM]Chemical Sciences, Substrate Interaction, 030102 biochemistry & molecular biology, biology, Electron Spin Resonance Spectroscopy, Nucleosides, [CHIM.CATA]Chemical Sciences/Catalysis, Protein Structure, Tertiary, chemistry, Docking (molecular), biology.protein, Biocatalysis, Mutagenesis, Site-Directed, [PHYS.PHYS.PHYS-CHEM-PH]Physics [physics]/Physics [physics]/Chemical Physics [physics.chem-ph], Radical SAM, Wybutosine
Abstract

International audience; TYW1 is a metalloenzyme involved in the modifications of guanosine 37 of Phe-tRNA of Eukaryota and Archaea. It catalyzes the second step of Wybutosine biosynthesis, which consists of the formation of the tricyclic compound imG-14 from m1G using pyruvate and SAM (S-adenosyl-methionine) as co-substrates. Two [4Fe-4S] clusters are needed in the catalytic process. One effects the reductive binding of SAM, which initiates the radical reaction that inserts a C-C moiety into m1G. The other [4Fe-4S] cluster binds the pyruvate molecule that provides the C-C motif. Using a combination of EPR and Mössbauer spectroscopy, we have been able to probe the binding of both cofactors to the FeS clusters. The results highlight an interaction between pyruvate and SAM, indicating that they bind in close vicinity inside the catalytic pocket. They also indicate a chelating binding mode of pyruvate to the accessible Fe site of the corresponding FeS cluster. This binding mode has been used to construct a docking model of holoTYW1 with pyruvate and SAM, which is consistent with the spectroscopic findings.

Published
2017
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31. Redox Self-Adaptation of a Nitrene Transfer Catalyst to the Substrate Needs

Author

Colette Lebrun, Florian Albrieux, Guillaume Coin, Eric Gouré, Jean-Marc Latour, Patrick Dubourdeaux, Frédéric Avenier, Dhurairajan Senthilnathan, Pascale Maldivi, Laboratoire de Chimie et Biologie des Métaux (LCBM - UMR 5249), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), SYstèmes Moléculaires et nanoMatériaux pour l’Energie et la Santé (SYMMES), Institut de Chimie du CNRS (INC)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), Center for Computational Chemistry, CRD, PRIST University Vallam, Thanjavur, Tamilnadu, India., Centre Commun de Spectrometrie de Masse (CCSM), Institut de Chimie et Biochimie Moléculaires et Supramoléculaires (ICBMS), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National des Sciences Appliquées de Lyon (INSA Lyon), Institut National des Sciences Appliquées (INSA)-Université de Lyon-Institut National des Sciences Appliquées (INSA)-Institut de Chimie du CNRS (INC)-École Supérieure Chimie Physique Électronique de Lyon-Centre National de la Recherche Scientifique (CNRS)-Université Claude Bernard Lyon 1 (UCBL), Institut National des Sciences Appliquées (INSA)-Université de Lyon-Institut National des Sciences Appliquées (INSA)-Institut de Chimie du CNRS (INC)-École Supérieure Chimie Physique Électronique de Lyon-Centre National de la Recherche Scientifique (CNRS), Institut de Chimie Moléculaire et des Matériaux d'Orsay (ICMMO), Université Paris-Sud - Paris 11 (UP11)-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC), Université de Lyon-Université de Lyon-École Supérieure de Chimie Physique Électronique de Lyon (CPE)-Institut National des Sciences Appliquées de Lyon (INSA Lyon), Université de Lyon-Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Université Paris-Sud - Paris 11 (UP11)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), and Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])

Subjects
Green chemistry, Chemistry, 010405 organic chemistry, Nitrene, Substrate (chemistry), Context (language use), amination, General Chemistry, General Medicine, [CHIM.CATA]Chemical Sciences/Catalysis, [CHIM.MATE]Chemical Sciences/Material chemistry, Photochemistry, 010402 general chemistry, Redox, 01 natural sciences, homogeneous catalysis, Catalysis, 0104 chemical sciences, tautomerism, iron, Electron affinity, [CHIM]Chemical Sciences, Amination, nitrene
Abstract

International audience; The development of iron catalysts for carbon-heteroatom bond formation, which has attracted strong interest in the context of green chemistry and nitrene transfer, has emerged as the most promising way to versatile amine synthetic processes. A diiron system was previously developed that proved efficient in catalytic sulfimidations and aziridinations thanks to an FeIII FeIV active species. To deal with more demanding benzylic and aliphatic substrates, the catalyst was found to activate itself to a FeIII FeIV L. active species able to catalyze aliphatic amination. Extensive DFT calculations show that this activation event drastically enhances the electron affinity of the active species to match the substrates requirements. Overall this process consists in a redox self-adaptation of the catalyst to the substrate needs.

Published
2017
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32. Structural Insights into the Nature of Fe 0 and Fe I Low-Valent Species Obtained upon the Reduction of Iron Salts by Aryl Grignard Reagents

Author

Jean-Marc Latour, Geneviève Blondin, Martin Clémancey, Thibault Cantat, Guillaume Lefèvre, Pierre Dorlet, Laboratoire de Chimie et Biologie des Métaux (LCBM - UMR 5249), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Laboratoire de Chimie Moléculaire et de Catalyse pour l'Energie (ex LCCEF) (LCMCE), Nanosciences et Innovation pour les Matériaux, la Biomédecine et l'Energie (ex SIS2M) (NIMBE UMR 3685), Institut Rayonnement Matière de Saclay (IRAMIS), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut Rayonnement Matière de Saclay (IRAMIS), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Stress Oxydants et Détoxication (LSOD), Département Biochimie, Biophysique et Biologie Structurale (B3S), Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), CEA, CNRS, the ANR (Project JCJC SIROCCO-16 (G.L.), ANR-10-INBS-0005,FRISBI,Infrastructure Française pour la Biologie Structurale Intégrée(2010), Laboratoire de Chimie et Biologie des Métaux ( LCBM - UMR 5249 ), Université Joseph Fourier - Grenoble 1 ( UJF ) -Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Centre National de la Recherche Scientifique ( CNRS ) -Université Grenoble Alpes ( UGA ), Laboratoire de Chimie Moléculaire et de Catalyse pour l'Energie (ex LCCEF) ( LCMCE ), Nanosciences et Innovation pour les Matériaux, la Biomédecine et l'Energie (ex SIS2M) ( NIMBE UMR 3685 ), Institut Rayonnement Matière de Saclay ( IRAMIS ), Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Université Paris-Saclay-Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Université Paris-Saclay-Centre National de la Recherche Scientifique ( CNRS ) -Institut Rayonnement Matière de Saclay ( IRAMIS ), Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Université Paris-Saclay-Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Université Paris-Saclay-Centre National de la Recherche Scientifique ( CNRS ), Stress Oxydants et Détoxication ( LSOD ), Département Biochimie, Biophysique et Biologie Structurale ( B3S ), Institut de Biologie Intégrative de la Cellule ( I2BC ), Université Paris-Sud - Paris 11 ( UP11 ) -Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Université Paris-Saclay-Centre National de la Recherche Scientifique ( CNRS ) -Université Paris-Sud - Paris 11 ( UP11 ) -Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Université Paris-Saclay-Centre National de la Recherche Scientifique ( CNRS ) -Institut de Biologie Intégrative de la Cellule ( I2BC ), Université Paris-Sud - Paris 11 ( UP11 ) -Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Université Paris-Saclay-Centre National de la Recherche Scientifique ( CNRS ) -Université Paris-Sud - Paris 11 ( UP11 ) -Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Université Paris-Saclay-Centre National de la Recherche Scientifique ( CNRS ), Université Paris-Sud - Paris 11 ( UP11 ) -Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Université Paris-Saclay-Centre National de la Recherche Scientifique ( CNRS ), ANR-10-INBS-05-01/10-INBS-0005,FRISBI,Infrastructure Française pour la Biologie Structurale Intégrée ( 2010 ), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC)-Institut Rayonnement Matière de Saclay (IRAMIS), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), and Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])

Subjects
Inorganic chemistry, 010402 general chemistry, 01 natural sciences, DFT, law.invention, Inorganic Chemistry, chemistry.chemical_compound, law, Mössbauer spectroscopy, Polymer chemistry, Physical and Theoretical Chemistry, Electron paramagnetic resonance, Tetrahydrofuran, 010405 organic chemistry, Ligand, Aryl, [CHIM.MATE]Chemical Sciences/Material chemistry, Toluene, Low - valent iron, 0104 chemical sciences, chemistry, Reagent, [ CHIM.MATE ] Chemical Sciences/Material chemistry, Proton NMR, EPR spectroscopy
Abstract

International audience; Mechanistic studies of the reduction of Fe III and Fe II salts by aryl Grignard reagents in toluene/tetrahydrofuran mixtures in the absence of a supporting ligand, as well as structural insights regarding the nature of the low-valent iron species obtained at the end of this reduction process, are reported. It is shown that several reduction pathways can be followed, depending on the starting iron precursor. We demonstrate, moreover, that these pathways lead to a mixture of Fe 0 and Fe I complexes regardless of the nature of the precursor. Mö ssbauer and 1 H NMR spectroscopies suggest that diamagnetic 16-electron bisarene complexes such as (η 4-C 6 H 5 Me) 2 Fe 0 can be formed as major species (85% of the overall iron quantity). The formation of a η 6-arene-ligated low-spin Fe I complex as a minor species (accounting for ca. 15% of the overall iron quantity) is attested by Mö ssbauer spectroscopy, as well as by continuous-wave electron paramagnetic resonance (EPR) and pulsed-EPR (HYSCORE) spectroscopies. The nature of the Fe I coordination sphere is discussed by means of isotopic labeling experiments and density functional theory calculations. It is shown that the most likely low-spin Fe I candidate obtained in these systems is a diphenylarene-stabilized species [(η 6-C 6 H 5 Me)Fe I Ph 2 ] − exhibiting an idealized C 2v topology. This enlightens the nature of the lowest valence states accommodated by iron during the reduction of Fe III and Fe II salts by aryl Grignard reagents in the absence of any additional coligand, which so far remained rather unknown. The reactivity of these low-valent Fe I and Fe 0 complexes in aryl−heteroaryl Kumada cross-coupling conditions has also been investigated, and it is shown that the zerovalent Fe 0 species can be used efficiently as a precursor in this reaction, whereas the Fe I oxidation state does not exhibit any reactivity.

Published
2017
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33. Single Asparagine to Arginine Mutation Allows PerR to Switch from PerR Box to Fur Box

Author

Christelle Caux-Thang, Arhamatoulaye Maïga, Ramakrishnan Sethu, Aubérie Parent, Jean-Marc Latour, Geneviève Blondin, Victor Duarte, Laboratoire de Chimie et Biologie des Métaux (LCBM - UMR 5249), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), and Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)

Subjects
DNA, Bacterial, Transcription, Genetic, Molecular Sequence Data, Virulence, Bacillus subtilis, Biology, Arginine, Biochemistry, DNA sequencing, 03 medical and health sciences, chemistry.chemical_compound, Bacterial Proteins, Transcription (biology), [SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Genomics [q-bio.GN], Protein Interaction Domains and Motifs, Nucleotide, Asparagine, Gene, 030304 developmental biology, Genetics, chemistry.chemical_classification, 0303 health sciences, Base Sequence, integumentary system, 030306 microbiology, Gene Expression Regulation, Bacterial, General Medicine, biology.organism_classification, [SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology, Repressor Proteins, chemistry, Mutation, bacteria, Molecular Medicine, DNA, Protein Binding
Abstract

International audience; Fur family proteins, ubiquitous in prokaryotes, play a pivotal role in microbial survival and virulence in most pathogens. Metalloregulators, such as Fur and PerR, regulate the transcription of genes connected to iron homeostasis and response to oxidative stress, respectively. In Bacillus subtilis, Fur and PerR bind with high affinity to DNA sequences differing at only two nucleotides. In addition to these differences in the PerR and Fur boxes, we identify in this study a residue located on the DNA binding motif of the Fur protein that is critical to discrimination between the two close DNA sequences. Interestingly, when this residue is introduced into PerR, it lowers the affinity of PerR for its own DNA target but confers to the protein the ability to interact strongly with the Fur DNA binding sequence. The present data show how two closely related proteins have distinct biological properties just by changing a single residue.

Published
2014
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34. A Diiron(III,IV) Imido Species Very Active in Nitrene-Transfer Reactions

Author

Pascale Maldivi, Olivier Sénèque, Florian Albrieux, Jean-Marc Latour, Frédéric Avenier, Martin Clémancey, Eric Gouré, Colette Lebrun, Patrick Dubourdeaux, Laboratoire de Chimie et Biologie des Métaux (LCBM - UMR 5249), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Institut de Chimie et Biochimie Moléculaires et Supramoléculaires (ICBMS), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-École Supérieure de Chimie Physique Électronique de Lyon (CPE)-Institut National des Sciences Appliquées de Lyon (INSA Lyon), Université de Lyon-Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Reconnaissance Ionique et Chimie de Coordination (RICC), SYstèmes Moléculaires et nanoMatériaux pour l’Energie et la Santé (SYMMES), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Labex ARCANE (ANR-11-LABX-0003-01), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019]), Université de Lyon-Université de Lyon-Institut National des Sciences Appliquées de Lyon (INSA Lyon), Institut National des Sciences Appliquées (INSA)-Université de Lyon-Institut National des Sciences Appliquées (INSA)-Institut de Chimie du CNRS (INC)-École Supérieure Chimie Physique Électronique de Lyon-Centre National de la Recherche Scientifique (CNRS), Institut de Chimie du CNRS (INC)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), and Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)

Subjects
Spectrometry, Mass, Electrospray Ionization, 010405 organic chemistry, Chemistry, Nitrene, Iron, Imidazoles, Molecular Conformation, General Chemistry, General Medicine, 010402 general chemistry, Photochemistry, 01 natural sciences, Catalysis, 0104 chemical sciences, Ion, chemistry.chemical_compound, Nitrogen atom, Tosyl, Coordination Complexes, Amine synthesis, Reactivity (chemistry), [CHIM.COOR]Chemical Sciences/Coordination chemistry, Electron configuration, Imines
Abstract

International audience; Metal-catalyzed nitrene transfer reactions arouse intense interest as clean and efficient procedures for amine synthesis. Efficient Rh- and Ru-based catalysts exist but Fe alternatives are actively pursued. However, reactive iron imido species can be very short-lived and getting evidence of their occurrence in efficient nitrene-transfer reactions is an important challenge. We recently reported that a diiron(III,II) complex is a very efficient nitrene-transfer catalyst to various substrates. We describe herein how, by combining desorption electrospray ionization mass spectrometry, quantitative chemical quench experiments, and DFT calculations, we obtained conclusive evidence for the occurrence of an {Fe(III) Fe(IV) NTosyl} intermediate that is very active in H-abstraction and nitrene-transfer reactions. DFT calculations revealed a strong radical character of the tosyl nitrogen atom in very low-lying electronic configurations of the Fe(IV) ion which are likely to confer its high reactivity.

Published
2014
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35. Single Glutamate to Aspartate Mutation Makes Ferric Uptake Regulator (Fur) as Sensitive to H2O2as Peroxide Resistance Regulator (PerR)

Author

Aubérie Parent, Christelle Caux-Thang, Luca Signor, Martin Clémancey, Ramakrishnan Sethu, Geneviève Blondin, Pascale Maldivi, Victor Duarte, and Jean-Marc Latour

Subjects
0303 health sciences, 03 medical and health sciences, General Medicine, 010402 general chemistry, 01 natural sciences, 030304 developmental biology, 0104 chemical sciences
Published
2013
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36. Heme Binding Induces Dimerization and Nitration of Truncated β-Amyloid Peptide Aβ16 Under Oxidative Stress

Author

Luigi Casella, Jean-Marc Latour, Silvia Pizzocaro, Ricardo Garcia-Serres, Enrico Monzani, Gregory Thiabaud, Dipartimento di Chimica, Università degli Studi di Pavia, Laboratoire de Chimie et Biologie des Métaux (LCBM - UMR 5249), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019]), Università degli Studi di Pavia = University of Pavia (UNIPV), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), and Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)

Subjects
Heme binding, medicine.disease_cause, Catalysis, chemistry.chemical_compound, 03 medical and health sciences, 0302 clinical medicine, Alzheimer Disease, Nitration, medicine, Humans, [CHIM.COOR]Chemical Sciences/Coordination chemistry, Heme, ComputingMilieux_MISCELLANEOUS, 030304 developmental biology, 0303 health sciences, Amyloid beta-Peptides, Nitrates, Chemistry, General Chemistry, General Medicine, Peptide Fragments, Amyloid β peptide, 3. Good health, Kinetics, Biochemistry, Hemin, Tyrosine, β amyloid peptide, Dimerization, Oxidation-Reduction, Oxidative stress, 030217 neurology & neurosurgery
Abstract

International audience

Published
2013
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37. Unanticipated coordination of tris buffer to the Radical SAM cluster of the RimO methylthiotransferase

Author

Martin Clémancey, Farhad Forouhar, Giuseppe Sicoli, Etienne Mulliez, Velavan Kathirvelu, Mohamed G. Atta, Serge Gambarelli, Jean-Marc Latour, Thibaut Molle, Laboratoire de Chimie et Biologie des Métaux (LCBM - UMR 5249), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Service de Chimie Inorganique et Biologique (SCIB - UMR E3), Institut Nanosciences et Cryogénie (INAC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Centre National de la Recherche Scientifique (CNRS), and Department of Biological Sciences, Northeast Structural Genomics ConsortiumColumbia University

Subjects
0301 basic medicine, Tris, S-Adenosylmethionine, Stereochemistry, Mossbauer spectroscopy, Iron–sulfur cluster, Electron donor, Buffers, [CHIM.INOR]Chemical Sciences/Inorganic chemistry, 010402 general chemistry, Photochemistry, Biosynthesis, 01 natural sciences, Biochemistry, law.invention, Inorganic Chemistry, 03 medical and health sciences, chemistry.chemical_compound, law, Molecule, Moiety, Thermotoga maritima, Tromethamine, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], Electron paramagnetic resonance, Bond cleavage, Ligand binding, Cofactor, Chemistry, 0104 chemical sciences, Pulsed EPR, 030104 developmental biology, Sulfurtransferases, Radical SAM, Iron-sulfur cluster
Abstract

International audience; Radical SAM enzymes generally contain a [4Fe-4S](2+/1+) (RS cluster) cluster bound to the protein via the three cysteines of a canonical motif CxxxCxxC. The non-cysteinyl iron is used to coordinate SAM via its amino-carboxylate moiety. The coordination-induced proximity between the cluster acting as an electron donor and the adenosyl-sulfonium bond of SAM allows for the homolytic cleavage of the latter leading to the formation of the reactive 5'-deoxyadenosyl radical used for substrate activation. Most of the structures of Radical SAM enzymes have been obtained in the presence of SAM, and therefore, little is known about the situation when SAM is not present. In this report, we show that RimO, a methylthiotransferase belonging to the radical SAM superfamily, binds a Tris molecule in the absence of SAM leading to specific spectroscopic signatures both in Mössbauer and pulsed EPR spectroscopies. These data provide a cautionary note for researchers who work with coordinative unsaturated iron sulfur clusters.

Published
2016
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38. Redox Control of the Human Iron-Sulfur Repair Protein MitoNEET Activity via Its Iron-Sulfur Cluster

Author

Eric Guittet, Jérôme Santolini, Martin Clémancey, Jean-Marc Latour, Ewen Lescop, Cécile Bouton, Geneviève Blondin, Sergio Gonçalves, Cécile Mons, Marie-Pierre Golinelli-Cohen, Institut de Chimie des Substances Naturelles (ICSN), Centre National de la Recherche Scientifique (CNRS), Laboratoire de Chimie et Biologie des Métaux (LCBM - UMR 5249), Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Institut de Chimie des Substances Naturelles ( ICSN ), Centre National de la Recherche Scientifique ( CNRS ), Laboratoire de Chimie et Biologie des Métaux ( LCBM - UMR 5249 ), Université Joseph Fourier - Grenoble 1 ( UJF ) -Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Centre National de la Recherche Scientifique ( CNRS ) -Université Grenoble Alpes ( UGA ), Institut de Biologie Intégrative de la Cellule ( I2BC ), Université Paris-Sud - Paris 11 ( UP11 ) -Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Université Paris-Saclay-Centre National de la Recherche Scientifique ( CNRS ), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), 'Avenir' U983 Hopital Necker-Enfants Malades, Institut National de la Santé et de la Recherche Médicale (INSERM), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Stress Oxydants et Détoxication (LSOD), Département Biochimie, Biophysique et Biologie Structurale (B3S), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Institut de Biologie Intégrative de la Cellule (I2BC), and Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)

Subjects
Iron-Sulfur Proteins, 0301 basic medicine, nuclear magnetic resonance (NMR), [SDV]Life Sciences [q-bio], Mossbauer spectroscopy, Regulator, Iron–sulfur cluster, chemistry.chemical_element, [SDV.BC]Life Sciences [q-bio]/Cellular Biology, medicine.disease_cause, Biochemistry, Redox, Fe-S transfer, Mitochondrial Proteins, 03 medical and health sciences, chemistry.chemical_compound, Protein stability, medicine, Humans, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, Fe-S lability, Molecular Biology, [ SDV.BBM ] Life Sciences [q-bio]/Biochemistry, Molecular Biology, iron-sulfur protein, [ SDV ] Life Sciences [q-bio], 030102 biochemistry & molecular biology, [ SDV.BC ] Life Sciences [q-bio]/Cellular Biology, [ CHIM.COOR ] Chemical Sciences/Coordination chemistry, Cell Biology, Acceptor, Sulfur, Oxidative Stress, Cytosol, Metabolism, 030104 developmental biology, chemistry, protein stability, mitoNEET, Raman spectroscopy, Biophysics, Oxidation-Reduction, Oxidative stress
Abstract

International audience; Human mitoNEET (mNT) is the first identified Fe-S protein of the mammalian outer mitochondrial membrane. Recently, mNT has been implicated in cytosolic Fe-S repair of a key regulator of cellular iron homeostasis. Here, we aimed to decipher the mechanism by which mNT triggers its Fe-S repair capacity. By using tightly controlled reactions combined with complementary spectroscopic approaches, we have determined the differential roles played by both the redox state of the mNT cluster and dioxygen in cluster transfer and protein stability. We unambiguously demonstrated that only the oxidized state of the mNT cluster triggers cluster transfer to a generic acceptor protein and that dioxygen is neither required for the cluster transfer reaction nor does it affect the transfer rate. In the absence of apo-acceptors, a large fraction of the oxidized holo-mNT form is converted back to reduced holo-mNT under low oxygen tension. Reduced holo-mNT, which holds a [2Fe-2S](+)with a global protein fold similar to that of the oxidized form is, by contrast, resistant in losing its cluster or in transferring it. Our findings thus demonstrate that mNT uses an iron-based redox switch mechanism to regulate the transfer of its cluster. The oxidized state is the "active state," which reacts promptly to initiate Fe-S transfer independently of dioxygen, whereas the reduced state is a "dormant form." Finally, we propose that the redox-sensing function of mNT is a key component of the cellular adaptive response to help stress-sensitive Fe-S proteins recover from oxidative injury.

Published
2016
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39. Near diffusion-controlled reaction of a Zn(Cys)

Author

Vincent, Lebrun, Jean-Luc, Ravanat, Jean-Marc, Latour, and Olivier, Sénèque

Subjects
Chemistry
Abstract

Reaction rate constants of HOCl with zinc-bound cysteines are determined, demonstrating that zinc fingers are potent targets for HOCl and may serve as HOCl sensors., Hypochlorous acid (HOCl) is one of the strongest oxidants produced in mammals to kill invading microorganisms. The bacterial response to HOCl involves proteins that are able to sense HOCl using methionine, free cysteines or zinc-bound cysteines of zinc finger sites. Although the reactivity of methionine or free cysteine with HOCl is well documented at the molecular level, this is not the case for zinc-bound cysteines. We present here a study that aims at filling this gap. Using a model peptide of the Zn(Cys)4 zinc finger site of the chaperone Hsp33, a protein involved in the defence against HOCl in bacteria, we show that HOCl oxidation of this model leads to the formation of two disulfides. A detailed mechanistic and kinetic study of this reaction, relying on stopped-flow measurements and competitive oxidation with methionine, reveals very high rate constants: the absolute second-order rate constants for the reaction of the model zinc finger with HOCl and its conjugated base ClO– are (9.3 ± 0.8) × 108 M–1 s–1 and (1.2 ± 0.2) × 104 M–1 s–1, the former approaching the diffusion limit. Revised values of the second-order rate constants for the reaction of methionine with HOCl and ClO– were also determined to be (5.5 ± 0.8) × 108 M–1 s–1 and (7 ± 5) × 102 M–1 s–1, respectively. At physiological pH, the zinc finger site reacts faster with HOCl than methionine and glutathione or cysteine. This study demonstrates that zinc fingers are potent targets for HOCl and confirms that they may serve as HOCl sensors as proposed for Hsp33.

Published
2016

40. Mononuclear Nonheme High-Spin Iron(III)-Acylperoxo Complexes in Olefin Epoxidation and Alkane Hydroxylation Reactions

Author

Martin Clémancey, Ritimukta Sarangi, Mi Sook Seo, Yong Min Lee, Jean-Marc Latour, Bin Wang, Wonwoo Nam, Department of Chemistry and Nano Science, EWHA Womans University (EWHA), Laboratoire de Chimie et Biologie des Métaux (LCBM - UMR 5249), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019]), SLAC National Accelerator Laboratory (SLAC), Stanford University, Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), and Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)

Subjects
Allylic rearrangement, Cyclohexene, Alkenes, 010402 general chemistry, 01 natural sciences, Biochemistry, Medicinal chemistry, Ferric Compounds, Catalysis, Hydroxylation, chemistry.chemical_compound, Colloid and Surface Chemistry, Cyclam, Alkanes, Organic chemistry, [CHIM.COOR]Chemical Sciences/Coordination chemistry, Bond cleavage, Olefin fiber, Molecular Structure, 010405 organic chemistry, Ligand, Water, General Chemistry, [CHIM.CATA]Chemical Sciences/Catalysis, 0104 chemical sciences, chemistry, Epoxy Compounds, Oxidation-Reduction, Cyclohexene oxide
Abstract

International audience; Mononuclear nonheme high-spin iron(III)-acylperoxo complexes bearing an N-methylated cyclam ligand were synthesized, spectroscopically characterized, and investigated in olefin epoxidation and alkane hydroxylation reactions. In the epoxidation of olefins, epoxides were yielded as the major products with high stereo-, chemo-, and enantioselectivities; cis- and trans-stilbenes were oxidized to cis- and trans-stilbene oxides, respectively. In the epoxidation of cyclohexene, cyclohexene oxide was formed as the major product with a kinetic isotope effect (KIE) value of 1.0, indicating that nonheme iron(III)-acylperoxo complexes prefer C═C epoxidation to allylic C–H bond activation. Olefin epoxidation by chiral iron(III)-acylperoxo complexes afforded epoxides with high enantioselectivity, suggesting that iron(III)-acylperoxo species, not high-valent iron-oxo species, are the epoxidizing agent. In alkane hydroxylation reactions, iron(III)-acylperoxo complexes hydroxylated C–H bonds as strong as those in cyclohexane at −40 °C, wherein (a) alcohols were yielded as the major products with high regio- and stereoselectivities, (b) activation of C–H bonds by the iron(III)-acylperoxo species was the rate-determining step with a large KIE value and good correlation between reaction rates and bond dissociation energies of alkanes, and (c) the oxygen atom in the alcohol product was from the iron(III)-acylperoxo species, not from molecular oxygen. In isotopically labeled water (H218O) experiments, incorporation of 18O from H218O into oxygenated products was not observed in the epoxidation and hydroxylation reactions. On the basis of mechanistic studies, we conclude that mononuclear nonheme high-spin iron(III)-acylperoxo complexes are strong oxidants capable of oxygenating hydrocarbons prior to their conversion into iron-oxo species via O–O bond cleavage.

Published
2016
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41. Redox Behavior of the S-Adenosylmethionine (SAM)-Binding Fe-S Cluster in Methylthiotransferase RimO, toward Understanding Dual SAM Activity

Author

Jean-Luc Ravanat, Martin Clémancey, Yohann Moreau, Farhad Forouhar, Mohamed G. Atta, Jean-Marc Latour, Etienne Mulliez, Nicolas Duraffourg, Serge Gambarelli, Thibaut Molle, Vincent Fourmond, Laboratoire de Chimie et Biologie des Métaux (LCBM - UMR 5249), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Department of Biological Sciences, Columbia University, New York, New York, USA., Columbia University [New York], Northeast Structural Genomics Consortium, Laboratoire Lésions des Acides Nucléiques (LAN), Service de Chimie Inorganique et Biologique (SCIB - UMR E3), Institut Nanosciences et Cryogénie (INAC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Centre National de la Recherche Scientifique (CNRS)-Institut Nanosciences et Cryogénie (INAC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Centre National de la Recherche Scientifique (CNRS), Bioénergétique et Ingénierie des Protéines (BIP ), Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019]), Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-Institut Nanosciences et Cryogénie (INAC), Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), and Centre National de la Recherche Scientifique (CNRS)-Aix Marseille Université (AMU)

Subjects
Iron-Sulfur Proteins, 0301 basic medicine, S-Adenosylmethionine, Reaction mechanism, 010402 general chemistry, 01 natural sciences, Biochemistry, Chemical reaction, Redox, Catalysis, Cofactor, law.invention, 03 medical and health sciences, law, Cluster (physics), Molecule, [CHIM]Chemical Sciences, Electron paramagnetic resonance, biology, Chemistry, Escherichia coli Proteins, Spectrum Analysis, 0104 chemical sciences, 3. Good health, Crystallography, 030104 developmental biology, Sulfurtransferases, Mutagenesis, Site-Directed, biology.protein, Density functional theory, Oxidation-Reduction
Abstract

International audience; RimO, a radical-S-adenosylmethionine (SAM) enzyme, catalyzes the specific C3 methylthiolation of the D89 residue in the ribosomal S12 protein. Two intact iron–sulfur clusters and two SAM cofactors both are required for catalysis. By using electron paramagnetic resonance, Mössbauer spectroscopies, and site-directed mutagenesis, we show how two SAM molecules sequentially bind to the unique iron site of the radical-SAM cluster for two distinct chemical reactions in RimO. Our data establish that the two SAM molecules bind the radical-SAM cluster to the unique iron site, and spectroscopic evidence obtained under strongly reducing conditions supports a mechanism in which the first molecule of SAM causes the reoxidation of the reduced radical-SAM cluster, impeding reductive cleavage of SAM to occur and allowing SAM to methylate a HS– ligand bound to the additional cluster. Furthermore, by using density functional theory-based methods, we provide a description of the reaction mechanism that predicts the attack of the carbon radical substrate on the methylthio group attached to the additional [4Fe-4S] cluster.

Published
2016
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42. Near diffusion-controlled reaction of a Zn(Cys)(4) zinc finger with hypochlorous acid

Author

Jean-Luc Ravanat, Jean-Marc Latour, Olivier Sénèque, Vincent Lebrun, Laboratoire de Chimie et Biologie des Métaux (LCBM - UMR 5249), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019]), Laboratoire Lésions des Acides Nucléiques (LAN), Service de Chimie Inorganique et Biologique (SCIB - UMR E3), Institut Nanosciences et Cryogénie (INAC), Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-Institut Nanosciences et Cryogénie (INAC), Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Centre National de la Recherche Scientifique (CNRS)-Institut Nanosciences et Cryogénie (INAC), and Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Centre National de la Recherche Scientifique (CNRS)

Subjects
0301 basic medicine, Zinc finger, chemistry.chemical_classification, Methionine, Hypochlorous acid, Stereochemistry, Inorganic chemistry, Peptide, General Chemistry, Glutathione, 03 medical and health sciences, chemistry.chemical_compound, 030104 developmental biology, Reaction rate constant, chemistry, Hsp33, [CHIM]Chemical Sciences, Cysteine
Abstract

International audience; Hypochlorous acid (HOCl) is one of the strongest oxidants produced in mammals to kill invading microorganisms. The bacterial response to HOCl involves proteins that are able to sense HOCl using methionine, free cysteines or zinc-bound cysteines of zinc finger sites. Although the reactivity of methionine or free cysteine with HOCl is well documented at the molecular level, this is not the case for zinc-bound cysteines. We present here a study that aims at filling this gap. Using a model peptide of the Zn(Cys)(4) zinc finger site of the chaperone Hsp33, a protein involved in the defence against HOCl in bacteria, we show that HOCl oxidation of this model leads to the formation of two disulfides. A detailed mechanistic and kinetic study of this reaction, relying on stopped-flow measurements and competitive oxidation with methionine, reveals very high rate constants: the absolute second-order rate constants for the reaction of the model zinc finger with HOCl and its conjugated base ClO- are (9.3 +/- 0.8) x 10(8) M-1 s(-1) and (1.2 +/- 0.2) x 10(4) M-1 s(-1), the former approaching the diffusion limit. Revised values of the second-order rate constants for the reaction of methionine with HOCl and ClO- were also determined to be (5.5 +/- 0.8) x 10(8) M-1 s(-1) and (7 +/- 5) x 10(2) M-1 s(-1), respectively. At physiological pH, the zinc finger site reacts faster with HOCl than methionine and glutathione or cysteine. This study demonstrates that zinc fingers are potent targets for HOCl and confirms that they may serve as HOCl sensors as proposed for Hsp33.

Published
2016
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43. An N-bridged high-valent diiron–oxo species on a porphyrin platform that can oxidize methane

Author

Leonardo X Alvarez, Evgeny V Kudrik, Martin Clémancey, Florian Albrieux, Patrick Dubourdeaux, Pavel Afanasiev, Jean-Marc Latour, Denis Bouchu, Alexander B. Sorokin, Geneviève Blondin, Sergey E. Nefedov, Institut de recherches sur la catalyse et l'environnement de Lyon (IRCELYON), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC), Laboratoire de Chimie et Biologie des Métaux (LCBM - UMR 5249), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Institut de Chimie et Biochimie Moléculaires et Supramoléculaires (ICBMS), Université de Lyon-Université de Lyon-Institut National des Sciences Appliquées de Lyon (INSA Lyon), Université de Lyon-Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Institut de Chimie du CNRS (INC)-École Supérieure Chimie Physique Électronique de Lyon-Centre National de la Recherche Scientifique (CNRS), Kurnakov Institute of General and Inorganic Chemistry, Russian Academy of Sciences [Moscow] (RAS), BIOVERT (BIOVERT), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC)-Université Claude Bernard Lyon 1 (UCBL), RAFFINAGE (RAFFINAGE), Université de Lyon-Université de Lyon-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Université de Lyon-Université de Lyon-École Supérieure de Chimie Physique Électronique de Lyon (CPE)-Institut National des Sciences Appliquées de Lyon (INSA Lyon), and Université de Lyon-Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)

Subjects
Spectrometry, Mass, Electrospray Ionization, Reaction mechanism, Metalloporphyrins, Nitrogen, Methane monooxygenase, Stereochemistry, General Chemical Engineering, Electrospray ionization, Context (language use), 010402 general chemistry, Photochemistry, 01 natural sciences, Catalysis, chemistry.chemical_compound, Oxidizing agent, Tetraphenylporphyrin, [CHIM.COOR]Chemical Sciences/Coordination chemistry, biology, 010405 organic chemistry, [CHIM.CATA]Chemical Sciences/Catalysis, General Chemistry, [SDE.ES]Environmental Sciences/Environmental and Society, Porphyrin, 0104 chemical sciences, Chlorobenzoates, chemistry, 13. Climate action, biology.protein, Methane, Oxidation-Reduction
Abstract

BIOVERT:RAFFINAGE+EKU:PAF:ASO; High-valent oxo-metal complexes are involved in key biochemical processes of selective oxidation and removal of xenobiotics. The catalytic properties of cytochrome P-450 and soluble methane monooxygenase enzymes are associated with oxo species on mononuclear iron haem and diiron non-haem platforms, respectively. Bio-inspired chemical systems that can reproduce the fascinating ability of these enzymes to oxidize the strongest C-H bonds are the focus of intense scrutiny. In this context, the development of highly oxidizing diiron macrocyclic catalysts requires a structural determination of the elusive active species and elucidation of the reaction mechanism. Here we report the preparation of an Fe(IV)(mu-nitrido)Fe(IV) = O tetraphenylporphyrin cation radical species at -90 degrees C, characterized by ultraviolet-visible, electron paramagnetic resonance and Mossbauer spectroscopies and by electrospray ionization mass spectrometry. This species exhibits a very high activity for oxygen-atom transfer towards alkanes, including methane. These findings provide a foundation on which to develop efficient and clean oxidation processes, in particular transformations of the strongest C-H bonds.

Published
2012
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44. Biologically Relevant Heterodinuclear Iron–Manganese Complexes

Author

Colette Lebrun, Lionel Dubois, Geneviève Blondin, Martin Clémancey, Jacques Pécaut, Jean-Marc Latour, Florian Molton, Michaël Carboni, Laboratoire de Chimie et Biologie des Métaux (LCBM - UMR 5249), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Département de Chimie Moléculaire (DCM), Université Joseph Fourier - Grenoble 1 (UJF)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Reconnaissance Ionique et Chimie de Coordination (RICC), SYstèmes Moléculaires et nanoMatériaux pour l’Energie et la Santé (SYMMES), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Service de Chimie Inorganique et Biologique (SCIB - UMR E3), Institut Nanosciences et Cryogénie (INAC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Centre National de la Recherche Scientifique (CNRS), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019]), Institut de Chimie du CNRS (INC)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), and Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)

Subjects
Models, Molecular, Pyridines, Iron, chemistry.chemical_element, Manganese, Crystallography, X-Ray, Ligands, 010402 general chemistry, Ferric Compounds, 01 natural sciences, law.invention, Inorganic Chemistry, Cresols, Electron transfer, Coordination Complexes, law, Mössbauer spectroscopy, Antiferromagnetism, [CHIM.COOR]Chemical Sciences/Coordination chemistry, Ferrous Compounds, Physical and Theoretical Chemistry, Electron paramagnetic resonance, 010405 organic chemistry, Chemistry, Ligand, Magnetic susceptibility, 0104 chemical sciences, Crystallography, Proton NMR
Abstract

International audience; The heterodinuclear complexes [Fe(III)Mn(II)(L-Bn)(μ-OAc)(2)](ClO(4))(2) (1) and [Fe(II)Mn(II)(L-Bn)(μ-OAc)(2)](ClO(4)) (2) with the unsymmetrical dinucleating ligand HL-Bn {[2-bis[(2-pyridylmethyl)aminomethyl]]-6-[benzyl-2-(pyridylmethyl)aminomethyl]-4-methylphenol} were synthesized and characterized as biologically relevant models of the new Fe/Mn class of nonheme enzymes. Crystallographic studies have been completed on compound 1 and reveal an Fe(III)Mn(II)μ-phenoxobis(μ-carboxylato) core. A single location of the Fe(III) ion in 1 and of the Fe(II) ion in 2 was demonstrated by Mössbauer and (1)H NMR spectroscopies, respectively. An investigation of the temperature dependence of the magnetic susceptibility of 1 revealed a moderate antiferromagnetic interaction (J = 20 cm(-1)) between the high-spin Fe(III) and Mn(II) ions in 1, which was confirmed by Mössbauer and electron paramagnetic resonance (EPR) studies. The electrochemical properties of complex 1 are described. A quasireversible electron transfer at -40 mV versus Ag/AgCl corresponding to the Fe(III)Mn(II)/Fe(II)Mn(II) couple appears in the cyclic voltammogram. Thorough investigations of the Mössbauer and EPR signatures of complex 2 were performed. The analysis allowed evidencing of a weak antiferromagnetic interaction (J = 5.72 cm(-1)) within the Fe(II)Mn(II) pair consistent with that deduced from magnetic susceptibility measurements (J = 6.8 cm(-1)). Owing to the similar value of the Fe(II) zero-field splitting (D(Fe) = 3.55 cm(-1)), the usual treatment within the strong exchange limit was precluded and a full analysis of the electronic structure of the ground state of complex 2 was developed. This situation is reminiscent of that found in many diiron and iron-manganese enzyme active sites.

Published
2012
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45. Molecular organization, biochemical function, cellular role and evolution of NfuA, an atypical Fe-S carrier

Author

Ricardo Garcia Serres, Céline Brochier-Armanet, Frédéric Barras, Sandra Angelini, Catherine Gerez, Marc Fontecave, Daniel Vinella, Jean-Marc Latour, Béatrice Py, Sandrine Ollagnier de Choudens, Emmanuel Talla, Laurent Loiseau, and Rémy Planel

Subjects
0303 health sciences, Subfamily, Protein subunit, 030302 biochemistry & molecular biology, Plasma protein binding, Biology, medicine.disease_cause, Microbiology, Aconitase, 03 medical and health sciences, Biochemistry, Electron Transport Complex I, biology.protein, medicine, ISCU, Molecular Biology, Escherichia coli, Biogenesis, 030304 developmental biology
Abstract

Biosynthesis of iron-sulphur (Fe-S) proteins is catalysed by multi-protein systems, ISC and SUF. However, 'non-ISC, non-SUF' Fe-S biosynthesis factors have been described, both in prokaryotes and eukaryotes. Here we report in vitro and in vivo investigations of such a 'non-ISC, non SUF' component, the Nfu proteins. Phylogenomic analysis allowed us to define four subfamilies. Escherichia coli NfuA is within subfamily II. Most members of this subfamily have a Nfu domain fused to a 'degenerate' A-type carrier domain (ATC*) lacking Fe-S cluster co-ordinating Cys ligands. The Nfu domain binds a [4Fe-4S] cluster while the ATC* domain interacts with NuoG (a complex I subunit) and aconitase B (AcnB). In vitro, holo-NfuA promotes maturation of AcnB. In vivo, NfuA is necessary for full activity of complex I under aerobic growth conditions, and of AcnB in the presence of superoxide. NfuA receives Fe-S clusters from IscU/HscBA and SufBCD scaffolds and eventually transfers them to the ATCs IscA and SufA. This study provides significant information on one of the Fe-S biogenesis factors that has been often used as a building block by ISC and/or SUF synthesizing organisms, including bacteria, plants and animals.

Published
2012
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46. Mössbauer studies of frataxin role in iron-sulfur cluster assembly and dysfunction-related disease

Author

Ricardo Garcia-Serres, Jean-Marc Latour, Martin Clémancey, Jean-Louis Oddou, Annalisa Pastore, and Emmanuel Lesuisse

Subjects
Iron-sulfur cluster assembly, chemistry.chemical_classification, Nuclear and High Energy Physics, biology, Chemistry, Mutant, Iron–sulfur cluster, Mitochondrion, Gene mutation, Condensed Matter Physics, Atomic and Molecular Physics, and Optics, Ferritin, chemistry.chemical_compound, Biochemistry, biology.protein, Metalloprotein, Frataxin, Physical and Theoretical Chemistry
Abstract

Friedreich ataxia is a disease that is associated with defects in the gene coding for a small protein frataxin. Several different roles have been proposed for the protein, including iron chaperoning and iron storage. Mossbauer spectroscopy was used to probe these hypotheses. Iron accumulation in mutant mitochondria unable to assemble iron sulfur clusters proved to be insensitive to overexpression of frataxin, ruling out its potential involvement as an iron storage protein similar to ferritin. Rather, it was found that frataxin negatively regulates iron sulfur cluster assembly.

Published
2011
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47. Oxidation of Zn(Cys)4 Zinc Finger Peptides by O2 and H2O2: Products, Mechanism and Kinetics

Author

Colette Lebrun, Emilie Bourlès, Manon Isaac, Jean-Marc Latour, Olivier Sénèque, Laboratoire de Chimie et Biologie des Métaux (LCBM - UMR 5249), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019]), Reconnaissance Ionique et Chimie de Coordination (RICC), SYstèmes Moléculaires et nanoMatériaux pour l’Energie et la Santé (SYMMES), Institut de Chimie du CNRS (INC)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), ANR-06-JCJC-0018,ZINCCYS,Implications des sites zinc-cystéinates dans le stress peroxydique: approche mécanistique par des modèles peptidiques(2006), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), and Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG)

Subjects
Models, Molecular, Spectrometry, Mass, Electrospray Ionization, Circular dichroism, Reaction mechanism, Inorganic chemistry, chemistry.chemical_element, Dithionitrobenzoic Acid, Ether, Zinc, 010402 general chemistry, 01 natural sciences, Catalysis, 03 medical and health sciences, chemistry.chemical_compound, Reaction rate constant, [CHIM.COOR]Chemical Sciences/Coordination chemistry, Reactivity (chemistry), Chromatography, High Pressure Liquid, 030304 developmental biology, chemistry.chemical_classification, Zinc finger, 0303 health sciences, Chemistry, Organic Chemistry, Zinc Fingers, Hydrogen Peroxide, Resorcinols, General Chemistry, Hydrogen-Ion Concentration, 0104 chemical sciences, Oxygen, Oxidative Stress, Thiol, Peptides, Oxidation-Reduction, Nuclear chemistry
Abstract

International audience; The reactivity of a series of Zn(Cys)(4) zinc finger model peptides towards H(2)O(2) and O(2) has been investigated. The oxidation products were identified by HPLC and ESI-MS analysis. At pH

Published
2011
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48. Iron-Sulfur (Fe-S) Cluster Assembly

Author

Gunhild Layer, Ricardo Garcia-Serres, Martin Clémancey, Sandrine Ollagnier de Choudens, Luca Signor, Marc Fontecave, Jean-Marc Latour, and Silke Wollers

Subjects
Flavin adenine dinucleotide, chemistry.chemical_classification, Scaffold protein, 0303 health sciences, biology, Stereochemistry, Cysteine desulfurase, 030302 biochemistry & molecular biology, Flavoprotein, Cell Biology, Flavin group, Biochemistry, Cofactor, 03 medical and health sciences, chemistry.chemical_compound, chemistry, Adenine nucleotide, biology.protein, Metalloprotein, Molecular Biology, 030304 developmental biology
Abstract

Assembly of iron-sulfur (Fe-S) clusters and maturation of Fe-S proteins in vivo require complex machineries. In Escherichia coli, under adverse stress conditions, this process is achieved by the SUF system that contains six proteins as follows: SufA, SufB, SufC, SufD, SufS, and SufE. Here, we provide a detailed characterization of the SufBCD complex whose function was so far unknown. Using biochemical and spectroscopic analyses, we demonstrate the following: (i) the complex as isolated exists mainly in a 1:2:1 (B:C:D) stoichiometry; (ii) the complex can assemble a [4Fe-4S] cluster in vitro and transfer it to target proteins; and (iii) the complex binds one molecule of flavin adenine nucleotide per SufBC2D complex, only in its reduced form (FADH2), which has the ability to reduce ferric iron. These results suggest that the SufBC2D complex functions as a novel type of scaffold protein that assembles an Fe-S cluster through the mobilization of sulfur from the SufSE cysteine desulfurase and the FADH2-dependent reductive mobilization of iron.

Published
2010
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49. Correction to: Contribution of Mössbauer spectroscopy to the investigation of Fe/S biogenesis

Author

Martin Clémancey, Jean-Marc Latour, Ricardo Garcia-Serres, and Geneviève Blondin

Subjects
Iron-Sulfur Proteins, Fe/S biogenesis, Mössbauer spectroscopy, Iron–sulfur cluster, Chemistry, Iron, Correction, Internet portal, Library science, Biochemistry, Inorganic Chemistry, Spectroscopy, Mossbauer, Humans, Histidine, Minireview, Iron trafficking, Biogenesis
Abstract

Fe/S cluster biogenesis involves a complex machinery comprising several mitochondrial and cytosolic proteins. Fe/S cluster biosynthesis is closely intertwined with iron trafficking in the cell. Defects in Fe/S cluster elaboration result in severe diseases such as Friedreich ataxia. Deciphering this machinery is a challenge for the scientific community. Because iron is a key player, 57Fe-Mössbauer spectroscopy is especially appropriate for the characterization of Fe species and monitoring the iron distribution. This minireview intends to illustrate how Mössbauer spectroscopy contributes to unravel steps in Fe/S cluster biogenesis. Studies were performed on isolated proteins that may be present in multiple protein complexes. Since a few decades, Mössbauer spectroscopy was also performed on whole cells or on isolated compartments such as mitochondria and vacuoles, affording an overview of the iron trafficking. Graphical abstract This minireview aims at presenting selected applications of 57Fe-Mössbauer spectroscopy to Fe/S cluster biogenesis

Published
2018
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50. Post-translational Modification of Ribosomal Proteins

Author

John F. Hunt, Gaetano T. Montelione, Etienne Mulliez, Jean-Marc Latour, Martin Clémancey, Mohamed G. Atta, Simon Arragain, Farhad Forouhar, Thierry Douki, Marc Fontecave, Ricardo Garcia-Serres, Helen Neely, and Geneviève Blondin

Subjects
0303 health sciences, biology, TRNA Methyltransferase, Cell Biology, Isomerase, 010402 general chemistry, biology.organism_classification, 01 natural sciences, Biochemistry, 0104 chemical sciences, Structural genomics, 03 medical and health sciences, Protein structure, Ribosomal protein, Thermotoga maritima, Transfer RNA, TIM barrel, Molecular Biology, 030304 developmental biology
Abstract

Post-translational modifications of ribosomal proteins are important for the accuracy of the decoding machinery. A recent in vivo study has shown that the rimO gene is involved in generation of the 3-methylthio derivative of residue Asp-89 in ribosomal protein S12 (Anton, B. P., Saleh, L., Benner, J. S., Raleigh, E. A., Kasif, S., and Roberts, R. J. (2008) Proc. Natl. Acad. Sci. U. S. A. 105, 1826-1831). This reaction is formally identical to that catalyzed by MiaB on the C2 of adenosine 37 near the anticodon of several tRNAs. We present spectroscopic evidence that Thermotoga maritima RimO, like MiaB, contains two [4Fe-4S] centers, one presumably bound to three invariant cysteines in the central radical S-adenosylmethionine (AdoMet) domain and the other to three invariant cysteines in the N-terminal UPF0004 domain. We demonstrate that holo-RimO can specifically methylthiolate the aspartate residue of a 20-mer peptide derived from S12, yielding a mixture of mono- and bismethylthio derivatives. Finally, we present the 2.0 A crystal structure of the central radical AdoMet and the C-terminal TRAM (tRNA methyltransferase 2 and MiaB) domains in apo-RimO. Although the core of the open triose-phosphate isomerase (TIM) barrel of the radical AdoMet domain was conserved, RimO showed differences in domain organization compared with other radical AdoMet enzymes. The unusually acidic TRAM domain, likely to bind the basic S12 protein, is located at the distal edge of the radical AdoMet domain. The basic S12 protein substrate is likely to bind RimO through interactions with both the TRAM domain and the concave surface of the incomplete TIM barrel. These biophysical results provide a foundation for understanding the mechanism of methylthioation by radical AdoMet enzymes in the MiaB/RimO family.

Published
2010
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