CO disrupts the reduced H-cluster of FeFe hydrogenase. A combined DFT and PFV study

Baffert C, Bertini L, Lautier T, Greco C, Sybirna K, Ezanno P, Etienne E, Soucaille P, Bertrand P, Bottin H, Meynial-Salles I, De Gioia L, Léger C.

J Am Chem Soc. 2011 Feb 23;133(7):2096-9. doi: 10.1021/ja110627b. Epub 2011 Jan 27.

Carbon monoxide is often described as a competitive inhibitor of FeFe hydrogenases, and it is used for probing H2 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 Fe2 subsite.

See the animated gif here.

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One thought on “CO disrupts the reduced H-cluster of FeFe hydrogenase. A combined DFT and PFV study

  1. Pingback: ANR Ecchymose | Movie: the Hred-CO state of hydrogenase breaking down over the course of DFT optimization

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