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Issue 2, 2014
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FeFe hydrogenase reductive inactivation and implication for catalysis

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Abstract

We show that FeFe hydrogenases inactivate at low potential, in a complex process that is mostly reversible. A form of the enzyme that is produced slowly and reversibly under reductive conditions has no proton activity under reductive conditions, although it can still oxidize H2 under oxidative conditions. This suggests that the so-called “super-reduced” state of the active site H-cluster is not part of the normal catalytic cycle. We also discuss our findings in relation to the optimization of H2-photoproduction devices based on FeFe hydrogenases that receive electrons from low potential photosensitizers.

Graphical abstract: FeFe hydrogenase reductive inactivation and implication for catalysis

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Supplementary files

Article information


Submitted
20 Jun 2013
Accepted
04 Nov 2013
First published
06 Nov 2013

Energy Environ. Sci., 2014,7, 715-719
Article type
Paper

FeFe hydrogenase reductive inactivation and implication for catalysis

V. Hajj, C. Baffert, K. Sybirna, I. Meynial-Salles, P. Soucaille, H. Bottin, V. Fourmond and C. Léger, Energy Environ. Sci., 2014, 7, 715
DOI: 10.1039/C3EE42075B

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