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

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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Submitted on : Friday, May 29, 2020 - 6:29:56 PM
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Carole Baffert, Luca Bertini, Thomas Lautier, Claudio Greco, Kateryna Sybirna, et al.. CO Disrupts the Reduced H-Cluster of FeFe Hydrogenase. A Combined DFT and Protein Film Voltammetry Study. Journal of the American Chemical Society, American Chemical Society, 2011, 133 (7), pp.2096 - 2099. ⟨10.1021/ja110627b⟩. ⟨hal-02652182⟩

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