Detoxification of superoxide without production of H2O2: antioxidant activity of superoxide reductase complexed with ferrocyanide
| Autor: | Catherine Berthomieu, Vincent Nivière, Emilie Tremey, Fernando P. Molina-Heredia, Vincent Favaudon, Virgile Adam, Danièle Touati, Chantal Houée-Levin |
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| Přispěvatelé: | 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 Physique D'Orsay (LCPO), Université Paris-Sud - Paris 11 (UP11)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Interactions Protéine Métal (IPM), Institut de Biosciences et Biotechnologies d'Aix-Marseille (ex-IBEB) (BIAM), Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS)-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)-Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Institut Jacques Monod (IJM (UMR_7592)), Université Paris Diderot - Paris 7 (UPD7)-Centre National de la Recherche Scientifique (CNRS), Génotoxicologie, signalisation et radiothérapie expérimentale, Institut Curie [Paris]-Institut National de la Santé et de la Recherche Médicale (INSERM), European Synchrotron Radiation Facility (ESRF), Toxicologie Nucléaire program from the Commissariat à l'Energie Atomique (CEA), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS), Chimie et biochimie des centres redox biologiques (CBCRB), Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Joseph Fourier - Grenoble 1 (UJF), Biologie cellulaire et moléculaire des plantes et des bactéries (BCMPB), Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université de la Méditerranée - Aix-Marseille 2, Université Joseph Fourier - Grenoble 1 (UJF)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), Université de la Méditerranée - Aix-Marseille 2-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS) |
| Jazyk: | angličtina |
| Rok vydání: | 2015 |
| Předmět: |
Deltaproteobacteria
MESH: Hydrogen-Ion Concentration MESH: Pulse Radiolysis Antioxidant medicine.medical_treatment MESH: Escherichia coli Proteins MESH: Superoxides Crystallography X-Ray Photochemistry MESH: Research Support Non-U.S. Gov't 01 natural sciences Medicinal chemistry Antioxidants chemistry.chemical_compound dismutase Superoxides Spectroscopy Fourier Transform Infrared Spectroscopy 0303 health sciences Multidisciplinary MESH: Oxidative Stress Crystallography biology Superoxide MESH: Escherichia coli Escherichia coli Proteins Hydrogen-Ion Concentration Biological Sciences Aerobiosis Hydrogen-Ion Concentration Models Solutions Superoxide reductase MESH: Hydrogen Peroxide pyrococcus-furiosus Ferrocyanide Oxidoreductases Pulse Radiolysis MESH: Mutation Non-U.S. Gov't Solutions MESH: Ferrocyanides mechanism FOS: Physical sciences hydrogen peroxide superoxide radical MESH: Solutions 010402 general chemistry Research Support Models Biological Redox Biological Mutation Oxidative Stress MESH: Spectroscopy Fourier Transform Infrared Ferrous Superoxide dismutase 03 medical and health sciences MESH: Aerobiosis Physics - Chemical Physics medicine Escherichia coli [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology MESH: Oxidoreductases [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biochemistry [q-bio.BM] MESH: Deltaproteobacteria 030304 developmental biology Chemical Physics (physics.chem-ph) Binding Sites MESH: Antioxidants MESH: Models Biological Active site Biomolecules (q-bio.BM) [SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biology Hydrogen Peroxide MESH: Gamma Rays MESH: Crystallography X-Ray 0104 chemical sciences Oxidative Stress chemistry MESH: Binding Sites Quantitative Biology - Biomolecules Fourier Transform Infrared Gamma Rays FOS: Biological sciences Mutation biology.protein X-Ray desulfoarculus-baarsii Ferrocyanides |
| Zdroj: | Proceedings of the National Academy of Sciences of the United States of America Proceedings of the National Academy of Sciences of the United States of America, 2006, 103 (40), pp.14750-5. ⟨10.1073/pnas.0510828103⟩ HAL Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2006, pp.14750-5 Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2006, 103 (40), pp.14750-5. ⟨10.1073/pnas.0510828103⟩ |
| ISSN: | 0027-8424 1091-6490 |
| Popis: | The superoxide radical O 2 ·̅ is a toxic by-product of oxygen metabolism. Two O 2 ·̅ detoxifying enzymes have been described so far, superoxide dismutase and superoxide reductase (SOR), both forming H 2 O 2 as a reaction product. Recently, the SOR active site, a ferrous iron in a [Fe 2+ (N-His) 4 (S-Cys)] pentacoordination, was shown to have the ability to form a complex with the organometallic compound ferrocyanide. Here, we have investigated in detail the reactivity of the SOR–ferrocyanide complex with O 2 ·̅ by pulse and γ-ray radiolysis, infrared, and UV-visible spectroscopies. The complex reacts very efficiently with O 2 ·̅ . However, the presence of the ferrocyanide adduct markedly modifies the reaction mechanism of SOR, with the formation of transient intermediates different from those observed for SOR alone. A one-electron redox chemistry appears to be carried out by the ferrocyanide moiety of the complex, whereas the SOR iron site remains in the reduced state. Surprisingly, the toxic H 2 O 2 species is no longer the reaction product. Accordingly, in vivo experiments showed that formation of the SOR–ferrocyanide complex increased the antioxidant capabilities of SOR expressed in an Escherichia coli sodA sodB recA mutant strain. Altogether, these data describe an unprecedented O 2 ·̅ detoxification activity, catalyzed by the SOR–ferrocyanide complex, which does not conduct to the production of the toxic H 2 O 2 species. |
| Databáze: | OpenAIRE |
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