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6 results on '"Bottin, H"'

1. Electron transfer in photosystem I reaction centers follows a linear pathway in which iron-sulfur cluster F(subB) is the immediate electron donor to soluble ferredoxin

Author

Diaz-Quintana, A., Leibl, W., Bottin, H., and Setif, P.

Subjects
Oxidation-reduction reaction -- Analysis, Cyanobacteria -- Genetic aspects, Biological sciences, Chemistry
Abstract

A study was conducted to measure the kinetics of electron transfer in PSI from the cyanobacterium, Synechocystis sp PCC 6803. The cynobacterium's cluster F(subB) was inactivated by treating it with mercury chloride and Photovoltage measurements were also utilized. Results revealed that in the absence of the cluster F(subB), the reduction of the cluster F(subA) by F(subX) remained faster than the rate of F(subX) reduction and the affinity of the ferredoxin for mercury chloride-treated PSI was deceased by a factor of 3-4 as compared to untreated photosystem.

Published
1998

2. A new non-heme iron environment in Paracoccus denitrificans adenylate kinase studied by electron paramagnetic resonance and electron spin echo envelope modulation spectroscopy

Author

Octavian Bârzu, Boussac A, Anne-Marie Gilles, Perrier, Bottin H, and Deligiannakis Y

Subjects
Absorption spectroscopy, Dimer, Molecular Sequence Data, Analytical chemistry, Adenylate kinase, chemistry.chemical_element, Zinc, Biochemistry, Ferric Compounds, Spectral line, law.invention, chemistry.chemical_compound, law, Rubredoxin, Amino Acid Sequence, Electron paramagnetic resonance, Paracoccus denitrificans, Binding Sites, biology, Sequence Homology, Amino Acid, Chemistry, Adenylate Kinase, Electron Spin Resonance Spectroscopy, biology.organism_classification, Recombinant Proteins, Crystallography
Abstract

Adenylate kinase from the Gram-negative bacterium Paracoccus denitrificans (AKden) has structural features highly similar to those of the enzyme from Gram-positive organisms. Atomic absorption spectroscopy of the recombinant protein, which is a dimer, revealed the presence of two metals, zinc and iron, each binding most probably to one monomer. Under oxidizing conditions, the electron paramagnetic resonance (EPR) spectrum of AKden at 4.2 K consists of features at g = 9.23, 4.34, 4.21, and 3.68. These features are absent in the ascorbate-reduced protein and are characteristic of a S = 5/2 spin system in a rhombic environment with E/D = 0.24 and are assigned to a non-heme Fe3+ (S = 5/2) center. The zero-field splitting parameter D (D = 1.4 +/- 0.2 cm-1) was estimated from the temperature dependence of the EPR spectra. These EPR characteristic as well as the difference absorption spectrum (oxidized minus reduced) of AKden are similar to those reported for the non-heme iron protein rubredoxin. Nevertheless, the redox potential of the Fe2+/Fe3+ couple in AKden was measured at +230 +/- 30 mV, which is more positive than the redox potential of the non-heme iron in rubredoxin. Binding of cyanide converts the iron from the high-spin (S = 5/2) to the low-spin (S = 1/2) spin state. The EPR spectrum of the non-heme Fe3+(S = 1/2) in the presence of cyanide has g values of 2.45, 2.18, and 1.92 and spin-Hamiltonian parameters R/lambda = 7. 4 and R/mu = 0.56. The conversion of the non-heme iron to the low-spin (S = 1/2) state allowed the study of its local environment by electron spin echo envelope modulation spectroscopy (ESEEM). The ESEEM data revealed the existence of 14N or 15N nuclei coupled to the low-spin iron after addition of KC14N or KC15N respectively. This demonstrated that iron in AKden has at least one labile coordination position that can be easily occupied by cyanide. Other possible magnetic interactions with nitrogen(s) from the protein are discussed.

Published
1997

3. Mechanism of O2 diffusion and reduction in FeFe hydrogenases

Author

Philippe Soucaille, Matteo Sensi, Christophe Léger, Isabelle Meynial-Salles, Charles Gauquelin, Carole Baffert, Jochen Blumberger, Laure Saujet, Robert B. Best, David De Sancho, Adam Kubas, Christophe Orain, Hervé Bottin, Vincent Fourmond, Kubas, A, Orain, C, Sancho, D, Saujet, L, Sensi, M, Gauquelin, C, Meynial-Salles, I, Soucaille, P, Bottin, H, Baffert, C, Fourmond, V, Best, R, Blumberger, J, Léger, C, Department of Physics and Astronomy [UCL London], University College of London [London] ( UCL ), Bioénergétique et Ingénierie des Protéines ( BIP ), Aix Marseille Université ( AMU ) -Centre National de la Recherche Scientifique ( CNRS ), Department of Chemistry [Cambridge, UK], University of Cambridge [UK] ( CAM ), 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 Biologie et de Technologies de Saclay ( IBITECS ), Université Paris-Saclay-Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ), Laboratoire d'Ingénierie des Systèmes Biologiques et des Procédés ( LISBP ), Institut National de la Recherche Agronomique ( INRA ) -Institut National des Sciences Appliquées - Toulouse ( INSA Toulouse ), Institut National des Sciences Appliquées ( INSA ) -Institut National des Sciences Appliquées ( INSA ) -Centre National de la Recherche Scientifique ( CNRS ), and Institut de Microbiologie de la Méditerranée ( IMM )

Subjects
Hydrogenase, General Chemical Engineering, Mutant, Nanotechnology, Molecular Dynamics Simulation, Molecular Dynamics, 010402 general chemistry, Electrochemistry, [ CHIM ] Chemical Sciences, 01 natural sciences, Catalysis, Diffusion, Molecular dynamics, Metalloproteins, Site-Directed, Clostridium, CHIM/03 - CHIMICA GENERALE E INORGANICA, chemistry.chemical_classification, biology, 010405 organic chemistry, Chemistry, Mutagenesis, Active site, Electrochemical Techniques, General Chemistry, 0104 chemical sciences, Oxygen, CHIM/02 - CHIMICA FISICA, Enzyme mecanisms, Enzyme, Hydrogen, Mutagenesis, Site-Directed, Oxidation-Reduction, Quantum Theory, Density functional theory, Electrocatalysis, Enzyme mechanisms, Metalloproteins, Molecular dynamics, Density functional theory, Biophysics, biology.protein, Electrocatalysis, Cysteine
Abstract

International audience; FeFe hydrogenases are the most efficient H2-producing enzymes. However, inactivation by O2 remains an obstacle that prevents them being used in many biotechnological devices. Here, we combine electrochemistry, site-directed mutagenesis, molecular dynamics and quantum chemical calculations to uncover the molecular mechanism of O2 diffusion within the enzyme and its reactions at the active site. We propose that the partial reversibility of the reaction with O2 results from the four-electron reduction of O2 to water. The third electron/proton transfer step is the bottleneck for water production, competing with formation of a highly reactive OH radical and hydroxylated cysteine. The rapid delivery of electrons and protons to the active site is therefore crucial to prevent the accumulation of these aggressive species during prolonged O2 exposure. These findings should provide important clues for the design of hydrogenase mutants with increased resistance to oxidative damage.

Published
2016
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4. Reactivity of the Excited States of the H-Cluster of FeFe Hydrogenases

Author

Carole Baffert, Claudio Greco, Luca Bertini, Souvik Roy, Charles Gauquelin, Isabelle Meynial-Salles, Matteo Sensi, Vincent Artero, Hervé Bottin, Luca De Gioia, Marc Fontecave, Laure Saujet, Christophe Léger, Philippe Soucaille, Vincent Fourmond, Giorgio Caserta, Bioénergétique et Ingénierie des Protéines (BIP ), Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS), Department of Biotechnologies and Biosciences, University of Milano-Bicocca, Department of Earth and Environmental Sciences [Milano], Università degli Studi di Milano-Bicocca [Milano] (UNIMIB), Laboratoire de Chimie des Processus Biologiques (LCPB), Centre National de la Recherche Scientifique (CNRS)-Collège de France (CdF)-Université Pierre et Marie Curie - Paris 6 (UPMC), Laboratoire d'Ingénierie des Systèmes Biologiques et des Procédés (LISBP), Centre National de la Recherche Scientifique (CNRS)-Institut National des Sciences Appliquées - Toulouse (INSA Toulouse), Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Institut National de la Recherche Agronomique (INRA), Institut de Biologie Intégrative de la Cellule (I2BC), Université Paris-Sud - Paris 11 (UP11)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-Université Paris-Saclay, Institut de Biologie et de Technologies de Saclay (IBITECS), Université Paris-Saclay-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Laboratoire de Chimie et Biologie des Métaux (LCBM - UMR 5249), Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes (UGA)-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), Bioénergétique et Ingénierie des Protéines ( BIP ), Aix Marseille Université ( AMU ) -Centre National de la Recherche Scientifique ( CNRS ), Department of Earth and Environmental Sciences, Università degli Studi di Milano-Bicocca [Milano], Laboratoire de Chimie des Processus Biologiques ( LCPB ), Université Pierre et Marie Curie - Paris 6 ( UPMC ) -Collège de France ( CdF ) -Centre National de la Recherche Scientifique ( CNRS ), Laboratoire d'Ingénierie des Systèmes Biologiques et des Procédés ( LISBP ), Institut National de la Recherche Agronomique ( INRA ) -Institut National des Sciences Appliquées - Toulouse ( INSA Toulouse ), Institut National des Sciences Appliquées ( INSA ) -Institut National des Sciences Appliquées ( INSA ) -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 ), Institut de Biologie et de Technologies de Saclay ( IBITECS ), Université Paris-Saclay-Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ), 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 ), Università degli Studi di Milano-Bicocca = University of Milano-Bicocca (UNIMIB), Collège de France - Chaire Chimie des processus biologiques, Collège de France (CdF (institution))-Institut de Chimie du CNRS (INC)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Collège de France (CdF (institution))-Institut de Chimie du CNRS (INC)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS), Institut National de la Recherche Agronomique (INRA)-Institut National des Sciences Appliquées - Toulouse (INSA Toulouse), Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-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, 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), CNRS, Aix Marseille Universite, INSA, CEA, ANR-12-BS08-0014,ECCHYMOSE,Etudes d'hydrogénases à Fer par électrochimie: mécanisme et optimisation pour la photoproduction d'hydrogène(2012), ANR-14-CE05-0010,HEROS,Hydrogénases résistantes à l'Oxygène(2014), ANR-11-LABX-0003,ARCANE,Grenoble, une chimie bio-motivée(2011), ANR-11-IDEX-0001,Amidex,INITIATIVE D'EXCELLENCE AIX MARSEILLE UNIVERSITE(2011), Chaire Chimie des processus biologiques, Université Pierre et Marie Curie - Paris 6 (UPMC)-Collège de France (CdF)-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), Sensi, M, Baffert, C, Greco, C, Caserta, G, Gauquelin, C, Saujet, L, Fontecave, M, Roy, S, Artero, V, Soucaille, P, Meynial Salles, I, Bottin, H, DE GIOIA, L, Fourmond, V, Léger, C, and Bertini, L

Subjects
Hydrogenase, 010402 general chemistry, Photochemistry, 01 natural sciences, Biochemistry, [ CHIM ] Chemical Sciences, Catalysis, [ CHIM.CATA ] Chemical Sciences/Catalysis, Colloid and Surface Chemistry, Cluster (physics), [CHIM]Chemical Sciences, Reactivity (chemistry), Hydrogen, hydrogenase, biology, 010405 organic chemistry, Chemistry, Active site, General Chemistry, Time-dependent density functional theory, [CHIM.CATA]Chemical Sciences/Catalysis, 0104 chemical sciences, [ PHYS.PHYS.PHYS-CHEM-PH ] Physics [physics]/Physics [physics]/Chemical Physics [physics.chem-ph], Covalent bond, Excited state, biology.protein
Abstract

International audience; FeFe hydrogenases catalyze H-2 oxidation and formation at an inorganic active site (the "H-cluster"), which consists of a [Fe-2(CO)(3)(CN)(2)(dithiomethylamine)] subcluster covalently attached to a Fe4S4 subcluster. This active site is photosensitive: visible light has been shown to induce the release of exogenous CO (a reversible inhibitor of the enzyme), shuffle the intrinsic CO ligands, and even destroy the H-cluster. These reactions must be understood because they may negatively impact the Use of hydrogenase for the photoproduction of H-2. Here, we explore in great detail the reactivity of the excited states of the H-duster under catalytic conditions by examining, both experimentally and using TDDFT calculations, the simplest photochemical reaction: the binding and release of exogenous CO. A simple dyad model can be used to predict which excitations are active. This could be used for probing other, aspects of the photoreactivity of the H-cluster.

Published
2016
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5. The oxidative inactivation of FeFe hydrogenase reveals the flexibility of the H-cluster

Author

Isabelle Meynial-Salles, Jochen Blumberger, Vincent Fourmond, Carole Baffert, Marco Montefiori, Luca De Gioia, Pierre Ezanno, Claudio Greco, Philippe Soucaille, Kateryna Sybirna, Po-hung Wang, Hervé Bottin, Christophe Léger, Maurizio Bruschi, Bioénergétique et Ingénierie des Protéines (BIP ), Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS), Department of Earth and Environmental Sciences [Milano], Università degli Studi di Milano-Bicocca = University of Milano-Bicocca (UNIMIB), Service de Bioénergétique, Biologie Stucturale, et Mécanismes (SB2SM), 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)-Centre National de la Recherche Scientifique (CNRS), Institut de Biologie et de Technologies de Saclay (IBITECS), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay, Department of Physics and Astronomy [UCL London], University College of London [London] (UCL), Laboratoire d'Ingénierie des Systèmes Biologiques et des Procédés (LISBP), Institut National de la Recherche Agronomique (INRA)-Institut National des Sciences Appliquées - Toulouse (INSA Toulouse), Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS), Department of Biotechnologies and Biosciences, Centre National de la Recherche Scientifique, Aix-Marseille Universite, Agence Nationale de la Recherche [ANR-12-BS08-0014, ANR-2010-BIOE-004], Ministero dell'Istruzione, dell'Universita e della Ricerca [Prin 2010M2JARJ], Ministry of Education, Republic of China (Taiwan), Engineering and Physical Sciences Research Council [EP/J015571/1, EP/F067496], Royal Society, Università degli Studi di Milano-Bicocca [Milano] (UNIMIB), 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), Université Paris-Saclay-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Centre National de la Recherche Scientifique (CNRS), Université Paris-Sud - Paris 11 (UP11)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-Université Paris-Saclay-Université Paris-Sud - Paris 11 (UP11)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-Université Paris-Saclay, Centre National de la Recherche Scientifique (CNRS)-Institut National des Sciences Appliquées - Toulouse (INSA Toulouse), Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Institut National de la Recherche Agronomique (INRA), University of Milano-Bicocca, Fourmond, V, Greco, C, Sybirna, K, Baffert, C, Wang, P, Ezanno, P, Montefiori, M, Bruschi, M, Meynial Salles, I, Soucaille, P, Blumberger, J, Bottin, H, DE GIOIA, L, Léger, C, Bioénergétique et Ingénierie des Protéines ( BIP ), Aix Marseille Université ( AMU ) -Centre National de la Recherche Scientifique ( CNRS ), Department of Earth and Environmental Sciences ( DEES ), Service de Bioénergétique, Biologie Stucturale, et Mécanismes ( SB2SM ), 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 ), Institut de Biologie et de Technologies de Saclay ( IBITECS ), Université Paris-Saclay-Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ), University College of London [London] ( UCL ), Laboratoire d'Ingénierie des Systèmes Biologiques et des Procédés ( LISBP ), Institut National de la Recherche Agronomique ( INRA ) -Institut National des Sciences Appliquées - Toulouse ( INSA Toulouse ), and Institut National des Sciences Appliquées ( INSA ) -Institut National des Sciences Appliquées ( INSA ) -Centre National de la Recherche Scientifique ( CNRS )

Subjects
Iron-Sulfur Proteins, Hydrogenase, Coordination sphere, Protein Conformation, General Chemical Engineering, Phenylalanine, Oxidative phosphorylation, Hydrogenase mimic, Photochemistry, Electrocatalyst, [ CHIM ] Chemical Sciences, Catalysis, Oxidizing agent, [CHIM]Chemical Sciences, chemistry.chemical_classification, General Chemistry, Combinatorial chemistry, Kinetics, Enzyme, chemistry, Mutation, Enzyme mechanisms, Tyrosine, hydrogenases, hydrogen, density functional theory, molecular dynamics, Electrocatalysis, Oxidation-Reduction, Hydrogen
Abstract

Nature is a valuable source of inspiration in the design of catalysts, and various approaches are used to elucidate the mechanism of hydrogenases, the enzymes that oxidize or produce H 2. In FeFe hydrogenases, H 2 oxidation occurs at the H-cluster, and catalysis involves H 2 binding on the vacant coordination site of an iron centre. Here, we show that the reversible oxidative inactivation of this enzyme results from the binding of H 2 to coordination positions that are normally blocked by intrinsic CO ligands. This flexibility of the coordination sphere around the reactive iron centre confers on the enzyme the ability to avoid harmful reactions under oxidizing conditions, including exposure to O 2. The versatile chemistry of the diiron cluster in the natural system might inspire the design of novel synthetic catalysts for H 2 oxidation. © 2014 Macmillan Publishers Limited.

Published
2014
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6. CO Disrupts the Reduced H-Cluster of FeFe Hydrogenase. A Combined DFT and Protein Film Voltammetry Study

Author

Emilien Etienne, Claudio Greco, Philippe Soucaille, Kateryna Sybirna, Christophe Léger, Luca Bertini, Thomas Lautier, Patrick Bertrand, Hervé Bottin, Luca De Gioia, Pierre Ezanno, Isabelle Meynial-Salles, Carole Baffert, Centre National de la Recherche Scientifique (CNRS), Università degli Studi di Milano [Milano] (UNIMI), Laboratoire d'Ingénierie des Systèmes Biologiques et des Procédés (LISBP), Institut National de la Recherche Agronomique (INRA)-Institut National des Sciences Appliquées - Toulouse (INSA Toulouse), Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Centre National de la Recherche Scientifique (CNRS), Commissariat à l'énergie atomique et aux énergies alternatives (CEA), ANR, Pole de competitivite Capenergies, European Commission [SolarH2 212508], Università degli Studi di Milano = University of Milan (UNIMI), Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS), Baffert, C, Bertini, L, Lautier, T, Greco, C, Sybirna, K, Ezanno, P, Etienne, E, Philippe Soucaille, P, Bertrand, P, Bottin, H, Meynial Salles, I, DE GIOIA, L, and Leger, C

Subjects
Hydrogenase, Stereochemistry, In silico, [SDV]Life Sciences [q-bio], Chlamydomonas reinhardtii, 010402 general chemistry, 01 natural sciences, Biochemistry, Catalysis, CHLAMYDOMONAS-REINHARDTII, CARBON-MONOXIDE BINDING, chemistry.chemical_compound, Colloid and Surface Chemistry, ONLY HYDROGENASE, Catalytic Domain, [SDV.IDA]Life Sciences [q-bio]/Food engineering, Electrochemistry, Cluster (physics), Protein Film Voltammetry, [SPI.GPROC]Engineering Sciences [physics]/Chemical and Process Engineering, Density Functional theory, CO binding, CHIM/03 - CHIMICA GENERALE E INORGANICA, Carbon Monoxide, ANALOGS, biology, 010405 organic chemistry, ACTIVE-SITE, Active site, General Chemistry, biology.organism_classification, 0104 chemical sciences, CHIM/02 - CHIMICA FISICA, chemistry, Iron-hydrogenasi, Protein film voltammetry, biology.protein, Quantum Theory, Carbon monoxide binding, CLOSTRIDIUM-PASTEURIANUM, Oxidation-Reduction, ENZYMES, Carbon monoxide
Abstract

International audience; Carbon monoxide is often described as a competitive inhibitor of FeFe hydrogenases, and it is used for probing H-2 binding to synthetic or in silico models of the active site H-cluster. Yet it does not always behave as a simple inhibitor. Using an original approach which combines accurate electrochemical measurements and theoretical calculations, we elucidate the mechanism by which, under certain conditions, CO binding can cause permanent damage to the H-cluster. Like in the case of oxygen inhibition, the reaction with CO engages the entire H-cluster, rather than only the Fe-2 subsite.

Published
2011
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