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From the same journal

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

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Published copy (DOI)

Author(s)

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

Department/unit(s)

Publication details

JournalJournal of the American Chemical Society
DatePublished - 2 May 2012
Issue number17
Volume134
Number of pages5
Pages (from-to)7553-7
Original languageEnglish

Abstract

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.

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