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    Inhibition of [FeFe]-Hydrogenases by Formaldehyde and Wider Mechanistic Implications for Biohydrogen Activation

    Foster, Carina E. and Krämer, Tobias and Wait, Annemarie F. and Parkin, Alison and Jennings, David P. and Happe, Thomas and McGrady, John E. and Armstrong, Fraser A. (2012) Inhibition of [FeFe]-Hydrogenases by Formaldehyde and Wider Mechanistic Implications for Biohydrogen Activation. Journal of the American Chemical Society, 134 (17). pp. 7553-7557. ISSN 0002-7863

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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 Hox 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.

    Item Type: Article
    Keywords: Inhibition; [FeFe]-Hydrogenases; Formaldehyde; Wider Mechanistic Implications; Biohydrogen Activation;
    Academic Unit: Faculty of Science and Engineering > Computer Science
    Faculty of Science and Engineering > Research Institutes > Hamilton Institute
    Item ID: 15515
    Identification Number:
    Depositing User: Tobias Kraemer
    Date Deposited: 15 Feb 2022 16:51
    Journal or Publication Title: Journal of the American Chemical Society
    Publisher: American Chemical Society
    Refereed: Yes
    Use Licence: This item is available under a Creative Commons Attribution Non Commercial Share Alike Licence (CC BY-NC-SA). Details of this licence are available here

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