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5 results on '"Soucaille, Philippe"'

2. Mechanism of O2 diffusion and reduction in FeFe hydrogenases

Author

Kubas, Adam, primary, Orain, Christophe, additional, De Sancho, David, additional, Saujet, Laure, additional, Sensi, Matteo, additional, Gauquelin, Charles, additional, Meynial-Salles, Isabelle, additional, Soucaille, Philippe, additional, Bottin, Hervé, additional, Baffert, Carole, additional, Fourmond, Vincent, additional, Best, Robert B., additional, Blumberger, Jochen, additional, and Léger, Christophe, additional

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

Author

Fourmond, Vincent, primary, Greco, Claudio, additional, Sybirna, Kateryna, additional, Baffert, Carole, additional, Wang, Po-Hung, additional, Ezanno, Pierre, additional, Montefiori, Marco, additional, Bruschi, Maurizio, additional, Meynial-Salles, Isabelle, additional, Soucaille, Philippe, additional, Blumberger, Jochen, additional, Bottin, Hervé, additional, De Gioia, Luca, additional, and Léger, Christophe, additional

Published
2014
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4. Mechanism of O2diffusion and reduction in FeFe hydrogenases

Author

Kubas, Adam, Orain, Christophe, De Sancho, David, Saujet, Laure, Sensi, Matteo, Gauquelin, Charles, Meynial-Salles, Isabelle, Soucaille, Philippe, Bottin, Hervé, Baffert, Carole, Fourmond, Vincent, Best, Robert B., Blumberger, Jochen, and Léger, Christophe

Abstract

FeFe hydrogenases are the most efficient H2-producing enzymes. However, inactivation by O2remains 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 O2diffusion within the enzyme and its reactions at the active site. We propose that the partial reversibility of the reaction with O2results from the four-electron reduction of O2to 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 O2exposure. These findings should provide important clues for the design of hydrogenase mutants with increased resistance to oxidative damage.

Published
2017
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5. Mechanism of O 2 diffusion and reduction in FeFe hydrogenases.

Author

Kubas A, Orain C, De Sancho D, Saujet L, Sensi M, Gauquelin C, Meynial-Salles I, Soucaille P, Bottin H, Baffert C, Fourmond V, Best RB, Blumberger J, and Léger C

Subjects
Catalysis, Clostridium enzymology, Diffusion, Electrochemical Techniques, Hydrogenase genetics, Molecular Dynamics Simulation, Mutagenesis, Site-Directed, Oxidation-Reduction, Quantum Theory, Hydrogen chemistry, Hydrogenase chemistry, Oxygen chemistry
Abstract

FeFe hydrogenases are the most efficient H 2 -producing enzymes. However, inactivation by O 2 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 O 2 diffusion within the enzyme and its reactions at the active site. We propose that the partial reversibility of the reaction with O 2 results from the four-electron reduction of O 2 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 O 2 exposure. These findings should provide important clues for the design of hydrogenase mutants with increased resistance to oxidative damage.

Published
2017
Full Text
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