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716 results on '"Mansuy, D."'

8. Oxidation of cyclohexane by molecular oxygen photoassisted by meso-tetraarylporphyrin iron(III)-hydroxo complexes

Author

Maldotti, A., Bartocci, C., Varani, G., Molinari, A., Battioni, P., and Mansuy, D.

Subjects
Cyclohexane -- Research, Oxygen -- Research, Iron compounds -- Research, Porphyrins -- Research, Radicals (Chemistry) -- Research, Ligands -- Research, Halogens -- Research, Chemistry
Abstract

The meso-tetraaryl iron porphyrins with an OH- axial ligand and halogen substituents in the pyrrole beta-positions were irradiated at 365 nanometer without dioxygen to produce Fe(super II) and OH radicals. The reduction of Fe(III) involved the transfer of the electron from the ligand to the metal center. The photoreduction quantum yields were affected by the OH- axial ligand and the various substituents in the beta-positions. The photoexcitation method can also oxidize cyclohexane to cyclohexanone by O2 with the formation of OH radicals.

Published
1996

9. Synthesis of pyrroloquinolinequinone analogs. Molecular structure and Mossbauer and magnetic properties of their iron complexes

Author

Tommasi, L., Shechter-Barloy, L., Varech, D., Battioni, J.-P., Donnadieu, B., Verelst, M., Bousseksou, A., Mansuy, D., and Tuchagues, J.P.

Subjects
Complex compounds -- Spectra, Quinone -- Research, Molecular structure -- Analysis, Chemistry
Abstract

A study of Mossbauer spectrum and molecular structure of iron complexes of pyrroloquinolinequinone (PPQ) analogs, synthesized by cycloaddition methods, reveals that stoichiometry and pH of the reactions influence the nuclearity and structure of these complexes. Chelation of oxidized PPQ with iron occurs via the quinonic site, while that of reduced PPQ proceeds through the tridentate state. Fe(II) is present in a distorted octahedral geometry.

Published
1995

10. Metabolism of polychlorinated phenols by Pseudomonas cepacia AC1100:determination of the first two steps and specific inhibitory effect of methimazole

Author

Tomasi, I., Artaud, I., Bertheau, Y., and Mansuy, D.

Subjects
Pseudomonas -- Research, Phenols -- Physiological aspects, Microbial metabolism -- Analysis, Biological sciences
Abstract

A study of the metabolism of polychlorinated phenols by Pseudomonas cepacia AC1100 using the inhibitory effect of methimazole reveals that the metabolism proceeds via two hydroxylation steps. The first involves a flavoprotein and positions the OH group para to the starting phenol, irrespective of the substituent present. The hydroquinone metabolite from the first step undergoes spontaneous oxidation producing quinone, a substrate for the second hydroxylation step.

Published
1995

11. Phenylhydrazones as new good substrates for the dioxygenase and peroxidase reactions of prostaglandin synthase: formation of iron(III)-sigma-phenyl complexes

Author

Mahy, J.P., Gaspard, S., and Mansuy, D.

Subjects
Prostaglandins -- Synthesis, Biological sciences, Chemistry
Abstract

Phenylhydrazones as substrates of prostaglandin synthase (PGHS) were reported. It was shown that phenylhydrazones constitute a new class of good substrates for the dioxygenase function of PGHS and that the hydroperoxides derived from this raection act as substrates for the peroxidase function of PGHS. It was also shown that Fe(III)-sigma-phenyl complexes of PGHS are formed during this oxidation of phenylhydrazones catalyzed by PGHS, which could be the cause of the inhibitory effects previously described for phenylhydrazones.

Published
1993

12. Beta-halogenated-pyrrole porphyrins. Molecular structures of 2,3,7,8,12,13,17, 18-octabromo-5,10,15,20-tetramesitylporphyrin, nickel(II) 2,3,7,8,12,13,17,18- octabromo-5,10,15,20-tetramesitylporphyrin, and nickel(II) 2,3,7,8,12,13,17,18 -octabromo-5,10,15,20-tetrakis(pentafluorophenyl)porphyrin

Author

Mandon, D., Ochsenbein, P., Fischer, J., Weiss, R., Jayaraj, K., Austin, R.N., Gold, A., White, P.S., Brigaud, O., Battioni, P., and Mansuy, D.

Subjects
Porphyrins -- Research, Nickel compounds -- Research, Molecular structure -- Research, Chemistry
Abstract

Three beta-halogenated-pyrrole porphyrins of the type H2TMOBP, NiTMOBP and NiTPFPOBP.1/2CH2Cl2 were successfully prepared and characterized. These three compounds subsequently underwent X-ray crystallography. The genrated images showed that the molecular formation of the compounds featured a nonplanar, saddle-shaped structure which reduced the intramolecular steric effects within the molecule. This generally made the metal oxo units of the compound more accessible than the non-halogenated forms.

Published
1992

16. New Recognition Elements in Biosensing

Author

SCHELLER, FRIEDER W., KLEINJUNG, FRANK, BIER, FRANK F., MAKOWER, ALEXANDER, NEUMANN, BARBARA, WOLLENBERGER, ULLA, KUROCHKIN, ILIYA, EREMENKO, ARKADI, BARMIN, ANATOLI, KLUMANN, SVEN, FÜRSTE, JENS-PETER, ERDMANN, VOLKER A., and MANSUY, D.

Published
1998

30. Predictive toxicology: the paths of the future

Author

Detilleux, Ph, Vallier, L, Legallais, C, Leclerc, E, Prot J, M, Choucha, L, Baudoin, R, Dufresne, M, Gautier, A, Carpentier, B, Mansuy, D, Pery, Alexandre R.R., Brochot, C, Manivet, Ph, Rabilloud, Thierry, Spire, C, Coumoul, Xavier, Junot, Ch, Laprevote, O, Le Pape, A, Tourneur, E, Ben Mkaddem, S, Chassin, C, Aloulou, M, Goujon J, M, Hertif, A, Ouali, N, Vimont, S, Monteiro, R, Rondeau, E, Elbim, C, Werts, C, Vandewalle, A, Pedruzzi, E, Coant, N, Bens, M, Cluzeaud, F, Ogier-Denis, E, Pongnimitprasert, N, Babin-Chevaye, C, Fay, M, Bernard, M, Dupuy, C, Ei Benna, J, Gougerot-Pocidale M, A, Braut-Boucher, F, Pinton, Philippe, Lucioli, Joelma, Tsybulskyy, D, Joly, Baptiste, Laffitte, J, Bourges-Abella, N, Oswald, Isabelle P., Kolf-Clauw, Martine, Pierre, St, Bats A, S, Chevalier, Aline, Bui L, Ch, Ambolet-Camoit, A, Garlatti, M, Aggerbeck, M, Barouki, R, Al Khansa, I, Blanck, O, Guillouzo, A, Bars, R, Rouas, C, Bensoussan, H, Suhard, D, Tessier, C, Grandcolas, L, Pallardy, M, Gueguen, Y, Sparfel, L, Pinel-Marie M, L, Boize, M, Koscielny, S, Desmots, S, Fardel, O, Alvergnas, M, Rouleau, A, Lucchi, G, Mantion, G, Heyd, B, Richert, L, Ducoroy, P, Martin, H, Val, St, Martinon, L, Cachier, H, Yahyaoui, A, Marfaing, H, Baeza-Squiban, A, Martin-Chouly, Corinne, Bonvallet, M, Morzadec, C, Vernhet, L, Baverel, G, El Hage, M, Nazaret, R, Conjard-Duplany, A, Ferrier, B, Martin, G, Legendre, A, Lecomte, Anthony, Froment, P, Habert, R, Lemazurier, E, Robinel, F, Dupont, O, Sanfins, E, Dairou, J, Chaffotte A, F, Busi, F, Rodrigues Lima, F, Dupret J, M, Mayati, A, Le Ferrec, Eric, Levoin, N, Paris, H, Uriac, Ph, N'Diaye, M, Lagadic-Gossmann, D, Assemat, E, Boublil, L, Borot M, C, Marano, F, Martiny V, Y, Moroy, G, Badel, A, Miteva M, A, Hussain, S, Ferecatu, I, Borot, C, Andreau, K, Boland, S, Leroux, M, Zucchini-Pascal, Nathalie, Peyre, L, Rahmani, Roger, Buron, N, Porcedou, M, Fromenty, B, Borgne-Sanchez, A, Rogue, A, Claude, N, Le Guével, Rémy, Institut National de l'Environnement Industriel et des Risques (INERIS), Laboratoire pharmaceutique Biologie Servier, Biologie Servier, Pharmacologie, toxicologie et signalisation cellulaire (U747), Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Faculté de Médecine Xavier Bichat, Centre de recherche biomédicale Bichat-Beaujon (CRB3), Université Paris Diderot - Paris 7 (UPD7)-Institut National de la Santé et de la Recherche Médicale (INSERM), Unité de recherche Pharmacologie-Toxicologie (UPT), Institut National de la Recherche Agronomique (INRA), Toxicité environnementale, cibles thérapeutiques, signalisation cellulaire (T3S - UMR_S 1124), Cytokines, chimiokines et immunopathologie, Université Paris-Sud - Paris 11 (UP11)-Institut National de la Santé et de la Recherche Médicale (INSERM), Service de biostatistique et d'épidémiologie (SBE), Direction de la recherche clinique [Gustave Roussy], Institut Gustave Roussy (IGR)-Institut Gustave Roussy (IGR), Institut de recherche en santé, environnement et travail (Irset), Université d'Angers (UA)-Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES)-École des Hautes Études en Santé Publique [EHESP] (EHESP)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique ), Fonctions et dysfonctions épithéliales - UFC (EA 4267) (FDE), Université de Franche-Comté (UFC), Plate-forme Protéomique CLIPP - Clinical and Innovation Proteomic Platform [Dijon] (CLIPP), Franche-Comté Électronique Mécanique, Thermique et Optique - Sciences et Technologies (UMR 6174) (FEMTO-ST), Université de Franche-Comté (UFC)-Centre National de la Recherche Scientifique (CNRS)-Ecole Nationale Supérieure de Mécanique et des Microtechniques (ENSMM)-Université de Technologie de Belfort-Montbeliard (UTBM)-Université de Franche-Comté (UFC)-Centre National de la Recherche Scientifique (CNRS)-Ecole Nationale Supérieure de Mécanique et des Microtechniques (ENSMM)-Université de Technologie de Belfort-Montbeliard (UTBM)-Institut de Chimie Moléculaire de l'Université de Bourgogne [Dijon] (ICMUB), Université de Bourgogne (UB)-Centre National de la Recherche Scientifique (CNRS)-Université de Bourgogne (UB)-Centre National de la Recherche Scientifique (CNRS), Laboratoire des Sciences du Climat et de l'Environnement [Gif-sur-Yvette] (LSCE), Université Paris-Saclay-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université de Versailles Saint-Quentin-en-Yvelines (UVSQ)-Centre National de la Recherche Scientifique (CNRS), Cellules Souches et Radiations (SCSR (U967 / UMR-E_008)), Institut National de la Santé et de la Recherche Médicale (INSERM)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris Diderot - Paris 7 (UPD7)-Université Paris-Sud - Paris 11 (UP11), Laboratoire Bioprojet, Institut des Sciences Chimiques de Rennes (ISCR), Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES)-Institut National des Sciences Appliquées - Rennes (INSA Rennes), Institut National des Sciences Appliquées (INSA)-Université de Rennes (UNIV-RENNES)-Institut National des Sciences Appliquées (INSA)-Ecole Nationale Supérieure de Chimie de Rennes-Centre National de la Recherche Scientifique (CNRS), Unité de Biologie Fonctionnelle et Adaptative (BFA (UMR_8251 / U1133)), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Diderot - Paris 7 (UPD7), Mitologics SAS, Hôpital Robert Debré, Biomécanique et Bioingénierie (BMBI), Université de Technologie de Compiègne (UTC)-Centre National de la Recherche Scientifique (CNRS), Laboratoire de radiotoxicologie expérimentale (IRSN/DRPH/SRBE/LRTOX), Service de RadioBiologie et d'Epidémiologie (IRSN/DRPH/SRBE), Institut de Radioprotection et de Sûreté Nucléaire (IRSN)-Institut de Radioprotection et de Sûreté Nucléaire (IRSN), Université d'Angers (UA)-Université de Rennes (UR)-École des Hautes Études en Santé Publique [EHESP] (EHESP)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique ), Université Bourgogne Franche-Comté [COMUE] (UBFC)-Université Bourgogne Franche-Comté [COMUE] (UBFC), Université de Technologie de Belfort-Montbeliard (UTBM)-Ecole Nationale Supérieure de Mécanique et des Microtechniques (ENSMM)-Centre National de la Recherche Scientifique (CNRS)-Université de Franche-Comté (UFC), Université Bourgogne Franche-Comté [COMUE] (UBFC)-Université Bourgogne Franche-Comté [COMUE] (UBFC)-Université de Technologie de Belfort-Montbeliard (UTBM)-Ecole Nationale Supérieure de Mécanique et des Microtechniques (ENSMM)-Centre National de la Recherche Scientifique (CNRS)-Université de Franche-Comté (UFC), Université Bourgogne Franche-Comté [COMUE] (UBFC)-Université Bourgogne Franche-Comté [COMUE] (UBFC)-Institut de Chimie Moléculaire de l'Université de Bourgogne [Dijon] (ICMUB), Université de Bourgogne (UB)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université de Bourgogne (UB)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Université de Versailles Saint-Quentin-en-Yvelines (UVSQ)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut national des sciences de l'Univers (INSU - CNRS)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Stabilité génétique, Cellules Souches et Radiations (SCSR (U_967)), Université Paris-Sud - Paris 11 (UP11)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Paris Cité (UPCité), Université de Rennes (UR)-Institut National des Sciences Appliquées - Rennes (INSA Rennes), Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Ecole Nationale Supérieure de Chimie de Rennes (ENSCR)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Université Paris Diderot - Paris 7 (UPD7)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Université Paris Descartes - Paris 5 (UPD5)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Paris-Sud - Paris 11 (UP11), Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique )-Institut National de la Santé et de la Recherche Médicale (INSERM)-École des Hautes Études en Santé Publique [EHESP] (EHESP)-Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES)-Université d'Angers (UA), Université de Technologie de Belfort-Montbeliard (UTBM)-Ecole Nationale Supérieure de Mécanique et des Microtechniques (ENSMM)-Université de Franche-Comté (UFC), Université Bourgogne Franche-Comté [COMUE] (UBFC)-Université Bourgogne Franche-Comté [COMUE] (UBFC)-Centre National de la Recherche Scientifique (CNRS)-Université de Technologie de Belfort-Montbeliard (UTBM)-Ecole Nationale Supérieure de Mécanique et des Microtechniques (ENSMM)-Université de Franche-Comté (UFC), Université Bourgogne Franche-Comté [COMUE] (UBFC)-Université Bourgogne Franche-Comté [COMUE] (UBFC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie Moléculaire de l'Université de Bourgogne [Dijon] (ICMUB), Institut national des sciences de l'Univers (INSU - CNRS)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université de Versailles Saint-Quentin-en-Yvelines (UVSQ), Université Paris-Sud - Paris 11 (UP11)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Paris (UP), Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC)-Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES)-Ecole Nationale Supérieure de Chimie de Rennes (ENSCR)-Institut National des Sciences Appliquées - Rennes (INSA Rennes), Institut National des Sciences Appliquées (INSA)-Université de Rennes (UNIV-RENNES)-Institut National des Sciences Appliquées (INSA), Université Paris-Sud - Paris 11 (UP11)-Université Paris Diderot - Paris 7 (UPD7)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de la Santé et de la Recherche Médicale (INSERM), Institut National des Sciences Appliquées - Rennes (INSA Rennes), Institut National des Sciences Appliquées (INSA)-Université de Rennes (UNIV-RENNES)-Institut National des Sciences Appliquées (INSA)-Université de Rennes (UNIV-RENNES)-Centre National de la Recherche Scientifique (CNRS)-Ecole Nationale Supérieure de Chimie de Rennes-Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES), Institut National de l'Environnement Industriel et des Risques ( INERIS ), Physiologie Cellulaire des Regulations Hormonales, Nutritionnelles et Pharmacologiques, Université Paris Descartes - Paris 5 ( UPD5 ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ) -Centre National de la Recherche Scientifique ( CNRS ), Centre de recherche biomédicale Bichat-Beaujon ( CRB3 ), Université Paris Diderot - Paris 7 ( UPD7 ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ), Unité de recherche Pharmacologie-Toxicologie ( UPT ), Institut National de la Recherche Agronomique ( INRA ), Toxicologie, Pharmacologie et Signalisation Cellulaire ( U1124 ), Institut National de la Santé et de la Recherche Médicale ( INSERM ) -Université Paris Descartes - Paris 5 ( UPD5 ) -Centre National de la Recherche Scientifique ( CNRS ), Université Paris-Sud - Paris 11 ( UP11 ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ), Service de biostatistique et d'épidémiologie ( SBE ), Institut Gustave Roussy ( IGR ) -Institut Gustave Roussy ( IGR ), Institut de recherche, santé, environnement et travail ( Irset ), Université d'Angers ( UA ) -Université de Rennes 1 ( UR1 ), Université de Rennes ( UNIV-RENNES ) -Université de Rennes ( UNIV-RENNES ) -École des Hautes Études en Santé Publique [EHESP] ( EHESP ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ) -Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique ) -Université des Antilles ( UA ), Fonctions et dysfonctions épithéliales - UFC (EA 4267) ( FDE ), Université de Franche-Comté ( UFC ), Plate-forme Protéomique CLIPP - Clinical and Innovation Proteomic Platform [Dijon] ( CLIPP ), Franche-Comté Électronique Mécanique, Thermique et Optique - Sciences et Technologies (UMR 6174) ( FEMTO-ST ), Université de Franche-Comté ( UFC ) -Centre National de la Recherche Scientifique ( CNRS ) -Ecole Nationale Supérieure de Mécanique et des Microtechniques ( ENSMM ) -Université de Technologie de Belfort-Montbeliard ( UTBM ) -Université de Franche-Comté ( UFC ) -Centre National de la Recherche Scientifique ( CNRS ) -Ecole Nationale Supérieure de Mécanique et des Microtechniques ( ENSMM ) -Université de Technologie de Belfort-Montbeliard ( UTBM ) -Institut de Chimie Moléculaire de l'Université de Bourgogne [Dijon] ( ICMUB ), Université de Bourgogne ( UB ) -Centre National de la Recherche Scientifique ( CNRS ) -Université de Bourgogne ( UB ) -Centre National de la Recherche Scientifique ( CNRS ), Laboratoire des Sciences du Climat et de l'Environnement [Gif-sur-Yvette] ( LSCE ), Université Paris-Saclay-Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Université de Versailles Saint-Quentin-en-Yvelines ( UVSQ ) -Centre National de la Recherche Scientifique ( CNRS ), Cellules Souches et Radiations ( SCSR - U 967 ), Université Paris-Sud - Paris 11 ( UP11 ) -Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Université Paris Diderot - Paris 7 ( UPD7 ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ), Institut des Sciences Chimiques de Rennes ( ISCR ), Université de Rennes 1 ( UR1 ), Université de Rennes ( UNIV-RENNES ) -Université de Rennes ( UNIV-RENNES ) -Ecole Nationale Supérieure de Chimie de Rennes-Institut National des Sciences Appliquées ( INSA ) -Centre National de la Recherche Scientifique ( CNRS ), Biologie Fonctionnelle et Adaptative ( BFA ), and Université Paris Diderot - Paris 7 ( UPD7 ) -Centre National de la Recherche Scientifique ( CNRS )

Subjects
[ SDV ] Life Sciences [q-bio], [SDV.TOX]Life Sciences [q-bio]/Toxicology, [SDV]Life Sciences [q-bio], ComputingMilieux_MISCELLANEOUS
Abstract

National audience

Published
2010

31. Toxicologie predictive: les voies du futur

Author

Ph Detilleux, Vallier, L., Legallais, C., Leclerc, E., M Prot J, Choucha, L., Baudoin, R., Dufresne, M., Gautier, A., Carpentier, B., Mansuy, D., Pery, Alexandre R. R., Brochot, C., Ph Manivet, Thierry Rabilloud, Spire, C., Xavier Coumoul, Ch Junot, Laprevote, O., Le Pape, A., Ronan Le Guével, Tourneur, E., Ben Mkaddem, S., Chassin, C., Aloulou, M., M Goujon J, Hertif, A., Ouali, N., Vimont, S., Monteiro, R., Rondeau, E., Elbim, C., Werts, C., Vandewalle, A., Pedruzzi, E., Coant, N., Bens, M., Cluzeaud, F., Ogier-Denis, E., Pongnimitprasert, N., Babin-Chevaye, C., Fay, M., Bernard Fromenty, Dupuy, C., Ei Benna, J., A Gougerot-Pocidale M, Braut-Boucher, F., Ph Pinton, Lucioli, J., Tsybulskyy, D., Baptiste Joly, Laffitte, J., Bourges-Abella, N., P Oswald I, Kolf-Clauw, M., St Pierre, S Bats A, Aline Chevalier, Ch Bui L, Ambolet-Camoit, A., Garlatti, M., Aggerbeck, M., Barouki, R., Al Khansa, I., Blanck, O., Guillouzo, A., Bars, R., Rouas, C., Bensoussan, H., Suhard, D., Tessier, C., Grandcolas, L., Pallardy, M., Gueguen, Y., Sparfel, L., L Pinel-Marie M, Boize, M., Koscielny, S., Desmots, S., Fardel, O., Alvergnas, M., Rouleau, A., Lucchi, G., Mantion, G., Heyd, B., Richert, L., Ducoroy, P., Martin, H., St Val, Martinon, L., Cachier, H., Yahyaoui, A., Marfaing, H., Baeza-Squiban, A., Corinne Martin-Chouly, Bonvallet, M., Morzadec, C., Vernhet, L., Baverel, G., El Hage, M., Nazaret, R., Conjard-Duplany, A., Ferrier, B., Martin, G., Legendre, A., Lecomte, A., Froment, P., Habert, R., Lemazurier, E., Robinel, F., Dupont, O., Sanfins, E., Dairou, J., F Chaffotte A, Busi, F., Rodrigues Lima, F., M Dupret J, Mayati, A., Eric Le Ferrec, Levoin, N., Paris, H., Ph Uriac, Diaye, M. N., Lagadic-Gossmann, D., Assemat, E., Boublil, L., C Borot M, Marano, F., Y Martiny V, Moroy, G., Badel, A., A Miteva M, Hussain, S., Ferecatu, I., Borot, C., Andreau, K., Boland, S., Leroux, M., Zucchini-Pascal, N., Peyre, L., Rahmani, R., Buron, N., Porcedou, M., Fromenty, B., Borgne-Sanchez, A., Rogue, A., Claude, N., and Jonchère, Laurent

Subjects
[SDV] Life Sciences [q-bio], [SDV.TOX] Life Sciences [q-bio]/Toxicology
Published
2010

32. LIST OF CONTRIBUTORS

Author

Alazard, J.P., primary, Amin, S.G., additional, Andrus, A., additional, ApSimon, J.W., additional, Armstrong, V.W., additional, Au-Yeung, B.-W., additional, Avram, M., additional, Ayer, W.A., additional, Babin, D., additional, Backinowsky, L.V., additional, Baldwin, J.E., additional, Bally, I., additional, Balsetan, A.T., additional, Bamezai, S., additional, Bandara, B.M.R., additional, Barth, G., additional, Barton, D.H.R., additional, Beaujean, M., additional, Beeley, N.R.A., additional, Berke, C.M., additional, Besselièvre, R., additional, Betaneli, V.I., additional, Beugelmans, R., additional, Birch, A.J., additional, Bose, A.K., additional, Brambilla, R., additional, Braun-Keller, E., additional, Brown, E., additional, Brownbridge, P., additional, Caspi, E., additional, Chamberlain, K., additional, Chan, T.H., additional, Chauncy, B., additional, Chottard, J.C., additional, Clardy, J., additional, Clark, B.C., additional, Collins, J.B., additional, Coulton, S., additional, Crouse, G.D., additional, Dadoun, H., additional, Dahler, P., additional, Day, A.I., additional, De Ville, G., additional, Dinulescu, I.G., additional, Djerassi, C., additional, von E. Doering, W., additional, Drâghici, C., additional, Elian, M., additional, Factor, R.E., additional, Faulkner, D.J., additional, Fernandez, I.F., additional, Finer-Moore, J., additional, Fleming, I., additional, Florent, J.-C., additional, Fourneron, J.-D., additional, Friary, R., additional, Fuhrer, H., additional, Fukuyama, T., additional, Funke, P.T., additional, Furmanova, N.G., additional, Fürst, A., additional, Furuhata, K., additional, Gala, K., additional, Ganguly, A., additional, Georgescu, E.G., additional, Gheorghiu, M.D., additional, Girard, P., additional, Gneuss, K.D., additional, Greaves, A.M., additional, Grier, D., additional, Gruska, R., additional, Guilhem, J., additional, Hangauer, D.G., additional, Hendrickson, J.B., additional, Hillenbrand, G.F., additional, Holohan, J.J., additional, Huber, C.P., additional, Huffman, J.W., additional, Husson, H.-P., additional, Iacobucci, G.A., additional, Ireland, C., additional, Irwin, A.J., additional, Janousek, Z., additional, Jenkins, I.D., additional, Johnson, M.A., additional, Jones, B.B., additional, Julia, M., additional, Kagan, H.B., additional, Kägi, D., additional, Kalvoda, J., additional, Kapur, J.C., additional, Katritzky, A.R., additional, Kaufmann, H., additional, Kelly, L.P., additional, Khajavi, M.S., additional, Khor, T.-C., additional, Kishi, Y., additional, Kitchin, J.P., additional, Kochetkov, N.K., additional, Kreder, J., additional, Kretschmer, G., additional, Kriemler, H.-P., additional, Ksander, G.M., additional, Kuwano, H., additional, Lansbury, P.T., additional, Lester, D.J., additional, Lewis, M., additional, Ley, S.V., additional, Liepa, A.J., additional, Lindley, M., additional, Lusinchi, X., additional, Mahanty, M.K., additional, Mallion, K.B., additional, Manhas, M.S., additional, Mansuy, D., additional, Mastrocola, A.R., additional, McMurry, J.E., additional, McPhail, A.T., additional, Meerholz, C.A., additional, Merenyi, R., additional, Metlushenko, V.P., additional, Mignani, S., additional, Minkin, V.I., additional, Mohr, P., additional, Monneret, C., additional, Motherwell, W.B., additional, Mukkavilli, L., additional, Müller, G., additional, Müller, M., additional, Mulliez, E., additional, Musser, J.H., additional, Naegeli, P., additional, Nakatsuka, S.-I., additional, Namy, J.L., additional, Narula, A.S., additional, Ogura, H., additional, Olekhnovich, L.P., additional, Onan, K.D., additional, Ovchinnikov, M.V., additional, Papoula, M.T.B., additional, Paquette, L.A., additional, Parker, W.L., additional, Pârvulescu, L., additional, Patel, R.C., additional, Peel, R., additional, Pickett, J.E., additional, Piper, J.U., additional, Puar, M.S., additional, Ragault, M., additional, Ram, B., additional, Ramachandran, P.V., additional, Ramage, R., additional, Ranganathan, D., additional, Ranganathan, S., additional, Rathnum, M.L., additional, Raverty, W.D., additional, Reed, N.V., additional, Rizzardo, E., additional, Roussi, G., additional, Saeedi-Ghomi, M.H., additional, Saito, I., additional, Scheuer, P.J., additional, Schriver, G.W., additional, Schwartz, R.E., additional, Scott, A.I., additional, Sell, C., additional, Sependa, G.J., additional, Shapiro, S., additional, Sing, L.Y., additional, Smith, K.M., additional, Sondheimer, F., additional, Soulié, J., additional, Stanescu, L., additional, Stephenson, G.R., additional, Stiller, K., additional, Streitwieser, A., additional, Sugiura, M., additional, Sum, F.W., additional, Sundararaman, P., additional, Sunday, B.R., additional, Sutherland, J.K., additional, Suzuki, M., additional, Tagle, B., additional, Tamm, Ch., additional, Tho, N.-D., additional, Thomas, E.J., additional, Thompson, D.J., additional, Toczko, G.A., additional, Van Engen, D., additional, van der Veen, J.M., additional, Viehe, H.G., additional, Vincent, J.E., additional, Wasserman, H.H., additional, Watson, W.H., additional, Weiler, L., additional, Wetli, M., additional, Wiley, D.C., additional, Williamson, D.H., additional, Wolff, M.S., additional, Wong, H.N.C., additional, Wright, J.J., additional, Zabel, V., additional, and Zimmerman, H.E., additional

Published
1982
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37. Synthesis and evaluation of new omega-borono-alpha-amino acids as rat liver arginase inhibitors

Author

Busnel, O., Carreaux, F., Carboni, B., Pethe, S., Goff, Sv, Mansuy, D., Boucher, Jl, and Deleage, Gilbert

Subjects
[SDV.BBM] Life Sciences [q-bio]/Biochemistry, Molecular Biology
Abstract

Recent studies have demonstrated that arginase plays important roles in pathologies such as asthma or erectile dysfunctions. We have synthesized new omega-borono-alpha-amino acids that are analogues of the previously known arginase inhibitors S-(2-boronoethyl)-l-cysteine (BEC) and 2-amino-6-boronohexanoic acid (ABH) and evaluated them as inhibitors of purified rat liver arginase (RLA). In addition to the distance between the B(OH)(2) and the alpha-amino acid functions, the position of the sulfur atom in the side chain also appears as a key determinant for the interaction with the active site of RLA. Furthermore, substitution of the alkyl side chain of BEC by methyl groups and conformational restriction of ABH by incorporation of its side chain in a phenyl ring led to inactive compounds. These results suggest that subtle interactions govern the affinity of inhibitors for the active site of RLA.Recent studies have demonstrated that arginase plays important roles in pathologies such as asthma or erectile dysfunctions. We have synthesized new omega-borono-alpha-amino acids that are analogues of the previously known arginase inhibitors S-(2-boronoethyl)-l-cysteine (BEC) and 2-amino-6-boronohexanoic acid (ABH) and evaluated them as inhibitors of purified rat liver arginase (RLA). In addition to the distance between the B(OH)(2) and the alpha-amino acid functions, the position of the sulfur atom in the side chain also appears as a key determinant for the interaction with the active site of RLA. Furthermore, substitution of the alkyl side chain of BEC by methyl groups and conformational restriction of ABH by incorporation of its side chain in a phenyl ring led to inactive compounds. These results suggest that subtle interactions govern the affinity of inhibitors for the active site of RLA.

Published
2005

41. Oxidations of N(omega)-hydroxyarginine analogues and various N-hydroxyguanidines by NO synthase II: key role of tetrahydrobiopterin in the reaction mechanism and substrate selectivity

Author

Moali, C., Boucher, Jl, Renodon-Corniere, A., Stuehr, Dj, Mansuy, D., and Deleage, Gilbert

Subjects
[SDV.BBM] Life Sciences [q-bio]/Biochemistry, Molecular Biology
Abstract

Oxidations of L-arginine 2, homo-L-arginine 1, their N(omega)-hydroxy derivatives 4 and 3 (NOHA and homo-NOHA, respectively), and four N-hydroxyguanidines, N(omega)-hydroxynor-L-arginine 5 (nor-NOHA), N(omega)-hydroxydinor-L-arginine 6 (dinor-NOHA), N-(4-chlorophenyl)-N'-hydroxyguanidine (8), and N-hydroxyguanidine (7) itself, by either NOS II or (6R)-5,6,7,8-tetrahydro-L-biopterin (BH4)-free NOS II, have been studied in a comparative manner. Recombinant BH4-free NOS II catalyzes the oxidation of all N-hydroxyguanidines by NADPH and O2, with formation of NO2(-) and NO3(-) at rates between 20 and 80 nmol min(-1) (mg of protein)(-1). In the case of compound 8, formation of the corresponding urea and cyanamide was also detected besides that of NO2(-) and NO3(-). These BH4-free NOS II-dependent reactions are inhibited by modulators of electron transfer in NOS such as thiocitrulline (TC) or imidazole (ImH), but not by Arg, and are completely suppressed by superoxide dismutase (SOD). They exhibit characteristics very similar to those previously reported for microsomal cytochrome P450-catalyzed oxidation of N-hydroxyguanidines. Both P450 and BH4-free NOS II reactions appear to be mainly performed by O2(.-) derived from the oxidase function of those heme proteins. In the presence of increasing concentrations of BH4, these nonselective oxidations progressively disappear while a much more selective monooxygenation takes place only with the N-hydroxyguanidines that are recognized well by NOS II, NOHA, homo-NOHA, and 8. These monooxygenations are much more chemoselective (8 being selectively transformed into the corresponding urea and NO) and are inhibited by Arg but not by SOD, as expected for reactions performed by the NOS Fe(II)-O2 species. Altogether, these results provide a further clear illustration of the key role of BH4 in regulating the monooxygenase/oxidase ratio in NOS. They also suggest a possible implication of NOSs in the oxidative metabolism of certain classes of xenobiotics such as N-hydroxyguanidines, not only via their monooxygenase function but also via their oxidase function.Oxidations of L-arginine 2, homo-L-arginine 1, their N(omega)-hydroxy derivatives 4 and 3 (NOHA and homo-NOHA, respectively), and four N-hydroxyguanidines, N(omega)-hydroxynor-L-arginine 5 (nor-NOHA), N(omega)-hydroxydinor-L-arginine 6 (dinor-NOHA), N-(4-chlorophenyl)-N'-hydroxyguanidine (8), and N-hydroxyguanidine (7) itself, by either NOS II or (6R)-5,6,7,8-tetrahydro-L-biopterin (BH4)-free NOS II, have been studied in a comparative manner. Recombinant BH4-free NOS II catalyzes the oxidation of all N-hydroxyguanidines by NADPH and O2, with formation of NO2(-) and NO3(-) at rates between 20 and 80 nmol min(-1) (mg of protein)(-1). In the case of compound 8, formation of the corresponding urea and cyanamide was also detected besides that of NO2(-) and NO3(-). These BH4-free NOS II-dependent reactions are inhibited by modulators of electron transfer in NOS such as thiocitrulline (TC) or imidazole (ImH), but not by Arg, and are completely suppressed by superoxide dismutase (SOD). They exhibit characteristics very similar to those previously reported for microsomal cytochrome P450-catalyzed oxidation of N-hydroxyguanidines. Both P450 and BH4-free NOS II reactions appear to be mainly performed by O2(.-) derived from the oxidase function of those heme proteins. In the presence of increasing concentrations of BH4, these nonselective oxidations progressively disappear while a much more selective monooxygenation takes place only with the N-hydroxyguanidines that are recognized well by NOS II, NOHA, homo-NOHA, and 8. These monooxygenations are much more chemoselective (8 being selectively transformed into the corresponding urea and NO) and are inhibited by Arg but not by SOD, as expected for reactions performed by the NOS Fe(II)-O2 species. Altogether, these results provide a further clear illustration of the key role of BH4 in regulating the monooxygenase/oxidase ratio in NOS. They also suggest a possible implication of NOSs in the oxidative metabolism of certain classes of xenobiotics such as N-hydroxyguanidines, not only via their monooxygenase function but also via their oxidase function.

Published
2001

43. Recognition of alpha-amino acids bearing various C=NOH functions by nitric oxide synthase and arginase involves very different structural determinants

Author

Moali, C., Brollo, M., Custot, J., Sari, Ma, Boucher, Jl, Stuehr, Dj, Mansuy, D., and Deleage, Gilbert

Subjects
[SDV.BBM] Life Sciences [q-bio]/Biochemistry, Molecular Biology
Abstract

Several alpha-amino acids bearing a C=NOH function separated from the Calpha carbon by two to five atoms have been synthesized and tested as substrates or inhibitors of recombinant nitric oxide synthases (NOS) I and II and as inhibitors of rat liver arginase (RLA). These include four N-hydroxyguanidines, N(omega)-hydroxy-L-arginine (NOHA) and its analogues homo-NOHA, nor-NOHA, and dinor-NOHA, two amidoximes bearing the -NH-C(CH(3))=NOH group, and two amidoximes bearing the -CH(2)-C(NH(2))=NOH group. Their behavior toward NOS and RLA was compared to that of the corresponding compounds bearing a C=NH function instead of the C=NOH function. The results obtained clearly show that efficient recognition of these alpha-amino acids by NOS and RLA involves very different structural determinants. NOS favors molecules bearing a -NH-C(R)=NH motif separated from Calpha by three or four CH(2) groups, such as arginine itself, with the necessary presence of delta-NH and omega-NH groups and a more variable R substituent. The corresponding molecules with a C=NOH function exhibit a much lower affinity for NOS. On the contrary, RLA best recognizes molecules bearing a C=NOH function separated from Calpha by three or four atoms, the highest affinity being observed in the case of three atoms. The presence of two omega-nitrogen atoms is important for efficient recognition, as in the two best RLA inhibitors, N(omega)-hydroxynorarginine and N(omega)-hydroxynorindospicine, which exhibit IC(50) values at the micromolar level. However, contrary to what was observed in the case of NOS, the presence of a delta-NH group is not important. These different structural requirements of NOS and RLA may be directly linked to the position of crucial residues that have been identified from crystallographic data in the active sites of both enzymes. Thus, binding of arginine analogues to NOS particularly relies on strong interactions of their delta-NH and omega-NH(2) groups with glutamate 371 (of NOS II), whereas binding of C=NOH molecules to RLA is mainly based on interactions of their terminal OH group with the binuclear Mn(II).Mn(II) cluster of the enzyme and on possible additional bonds between their omega-NH(2) group with histidine 141, glutamate 277, and one Mn(II) ion. The different modes of interaction displayed by both enzymes depend on their different catalytic functions and give interesting opportunities to design useful molecules to selectively regulate NOS and arginase.Several alpha-amino acids bearing a C=NOH function separated from the Calpha carbon by two to five atoms have been synthesized and tested as substrates or inhibitors of recombinant nitric oxide synthases (NOS) I and II and as inhibitors of rat liver arginase (RLA). These include four N-hydroxyguanidines, N(omega)-hydroxy-L-arginine (NOHA) and its analogues homo-NOHA, nor-NOHA, and dinor-NOHA, two amidoximes bearing the -NH-C(CH(3))=NOH group, and two amidoximes bearing the -CH(2)-C(NH(2))=NOH group. Their behavior toward NOS and RLA was compared to that of the corresponding compounds bearing a C=NH function instead of the C=NOH function. The results obtained clearly show that efficient recognition of these alpha-amino acids by NOS and RLA involves very different structural determinants. NOS favors molecules bearing a -NH-C(R)=NH motif separated from Calpha by three or four CH(2) groups, such as arginine itself, with the necessary presence of delta-NH and omega-NH groups and a more variable R substituent. The corresponding molecules with a C=NOH function exhibit a much lower affinity for NOS. On the contrary, RLA best recognizes molecules bearing a C=NOH function separated from Calpha by three or four atoms, the highest affinity being observed in the case of three atoms. The presence of two omega-nitrogen atoms is important for efficient recognition, as in the two best RLA inhibitors, N(omega)-hydroxynorarginine and N(omega)-hydroxynorindospicine, which exhibit IC(50) values at the micromolar level. However, contrary to what was observed in the case of NOS, the presence of a delta-NH group is not important. These different structural requirements of NOS and RLA may be directly linked to the position of crucial residues that have been identified from crystallographic data in the active sites of both enzymes. Thus, binding of arginine analogues to NOS particularly relies on strong interactions of their delta-NH and omega-NH(2) groups with glutamate 371 (of NOS II), whereas binding of C=NOH molecules to RLA is mainly based on interactions of their terminal OH group with the binuclear Mn(II).Mn(II) cluster of the enzyme and on possible additional bonds between their omega-NH(2) group with histidine 141, glutamate 277, and one Mn(II) ion. The different modes of interaction displayed by both enzymes depend on their different catalytic functions and give interesting opportunities to design useful molecules to selectively regulate NOS and arginase.

Published
2000

44. The new alpha-amino acid Nomega-hydroxy-nor-L-arginine:a high-affinity inhibitor of arginase well adapted to bind to its manganese cluster

Author

Custot, J., Moali, C., Brollo, M., Bouvher, J.L., Delaforge, M., Mansuy, D., Tenu, J. P., and Zimmerman, J. L.

Subjects
Amino acids -- Research, Arginine -- Research, Electron paramagnetic resonance spectroscopy -- Research, Enzyme inhibitors -- Research, Chemistry
Abstract

The synthesis of Nomega-hydroxy-nor-L-arginine and its homolog Nw-hydroxy-homo-L-arginine was reported. The inhibitory effects of NOHA, homo-NOHA, and nor-NOHA on arginases were compared. Electron paramagnetic resonance studies of NOHA compounds interaction with purified rat liver arginase showed that only nor-NOHA as the best arginase inhibitor and the only one capable of modifying the arginase EPR spectrum.

Published
1997

46. Detection of a nitric oxide synthase possibly involved in the regulation of the Rhodococcus sp R312 nitrile hydratase

Author

Sari, Ma, Moali, C., Boucher, Jl, Jaouen, M., Mansuy, D., and Deleage, Gilbert

Subjects
[SDV.BBM] Life Sciences [q-bio]/Biochemistry, Molecular Biology
Abstract

Crude homogenates from Rhodococcus sp 312 catalyze the conversion of L-arginine into L-citrulline and NO2-, the usual oxidation product of NO under aerobic conditions. They also catalyze the conversion of N omega-hydroxy-L-arginine (NOHA) into L-citrulline and NO2- with similar rates (10-15 and 100-150 nmol of product.min-1.(mg of protein)-1 respectively for the crude homogenate and for a fraction obtained from ammonium sulfate precipitation). L-citrulline formation is strongly inhibited by classical inhibitors of mammalian nitric oxide synthases (NOSs) such as N omega-methyl-L-arginine (NMA) and thio-L-citrulline (TC). Finally, the lack of inhibitory effects of EGTA, a classical inhibitor of constitutive mammalian NOSs, and the specific immunodetection of a 100 kD protein from Rhodococcus cytosol by an antibody raised against human inducible NOS, is in favor of the presence of a NOS similar to inducible mammalian NOSs in Rhodococcus sp 312. This NOS should be responsible for the NO-dependent inactivation of Rhodococcus Nitrile Hydratase (NHase) in the absence of light; it could regulate the activity of the latter enzyme.Crude homogenates from Rhodococcus sp 312 catalyze the conversion of L-arginine into L-citrulline and NO2-, the usual oxidation product of NO under aerobic conditions. They also catalyze the conversion of N omega-hydroxy-L-arginine (NOHA) into L-citrulline and NO2- with similar rates (10-15 and 100-150 nmol of product.min-1.(mg of protein)-1 respectively for the crude homogenate and for a fraction obtained from ammonium sulfate precipitation). L-citrulline formation is strongly inhibited by classical inhibitors of mammalian nitric oxide synthases (NOSs) such as N omega-methyl-L-arginine (NMA) and thio-L-citrulline (TC). Finally, the lack of inhibitory effects of EGTA, a classical inhibitor of constitutive mammalian NOSs, and the specific immunodetection of a 100 kD protein from Rhodococcus cytosol by an antibody raised against human inducible NOS, is in favor of the presence of a NOS similar to inducible mammalian NOSs in Rhodococcus sp 312. This NOS should be responsible for the NO-dependent inactivation of Rhodococcus Nitrile Hydratase (NHase) in the absence of light; it could regulate the activity of the latter enzyme.

Published
1998

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