CO disrupts the reduced H-cluster of FeFe hydrogenase. A combined DFT and protein film voltammetry study |
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Authors: | Baffert Carole Bertini Luca Lautier Thomas Greco Claudio Sybirna Kateryna Ezanno Pierre Etienne Emilien Soucaille Philippe Bertrand Patrick Bottin Hervé Meynial-Salles Isabelle De Gioia Luca Léger Christophe |
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Institution: | Bioenergetics and Engineering of Proteins, CNRS, UPR 9036, 31 chemin Joseph Aiguier, 13402 Marseille Cedex 20, France. |
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Abstract: | 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. |
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