Inhibition of [FeFe]-hydrogenases by formaldehyde and wider mechanistic implications for biohydrogen activation

Carina E Foster, Tobias Krämer, Annemarie F Wait, Alison Parkin, David P Jennings, Thomas Happe, John E McGrady, Fraser A Armstrong

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Formaldehyde-a rapid and reversible inhibitor of hydrogen evolution by [FeFe]-hydrogenases-binds with a strong potential dependence that is almost complementary to that of CO. Whereas exogenous CO binds tightly to the oxidized state known as H(ox) but very weakly to a state two electrons more reduced, formaldehyde interacts most strongly with the latter. Formaldehyde thus intercepts increasingly reduced states of the catalytic cycle, and density functional theory calculations support the proposal that it reacts with the H-cluster directly, most likely targeting an otherwise elusive and highly reactive Fe-hydrido (Fe-H) intermediate.
Original languageEnglish
Pages (from-to)7553-7
Number of pages5
JournalJournal of the American Chemical Society
Issue number17
Publication statusPublished - 2 May 2012

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