Peer-Reviewed Journal Details
Mandatory Fields
Foster CE;Krämer T;Wait AF;Parkin A;Jennings DP;Happe T;McGrady JE;Armstrong FA;
2012
May
Journal of the American Chemical Society
Inhibition of [FeFe]-hydrogenases by formaldehyde and wider mechanistic implications for biohydrogen activation.
Published
()
Optional Fields
134
17
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.
1520-5126
10.1021/ja302096r
Grant Details