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    Hydride bridge in [NiFe]-hydrogenase observed by nuclear resonance vibrational spectroscopy


    Ogata, Hideaki, Krämer, Tobias, Wang, Hongxin, Schilter, David, Pelmenschikov, Vladimir, van Gastel, Maurice, Neese, Frank, Rauchfuss, Thomas B., Gee, Leland B., Scott, Aubrey D., Yoda, Yoshitaka, Tanaka, Yoshihito, Lubitz, Wolfgang and Cramer, Stephen P. (2015) Hydride bridge in [NiFe]-hydrogenase observed by nuclear resonance vibrational spectroscopy. Nature Communications, 6 (1). ISSN 2041-1723

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    Abstract

    The metabolism of many anaerobes relies on [NiFe]-hydrogenases, whose characterization when bound to substrates has proven non-trivial. Presented here is direct evidence for a hydride bridge in the active site of the 57Fe-labelled fully reduced Ni-R form of Desulfovibrio vulgaris Miyazaki F [NiFe]-hydrogenase. A unique ‘wagging’ mode involving H- motion perpendicular to the Ni(m-H)57Fe plane was studied using 57Fe-specific nuclear resonance vibrational spectroscopy and density functional theory (DFT) calculations. On Ni(m-D)57Fe deuteride substitution, this wagging causes a characteristic perturbation of Fe–CO/CN bands. Spectra have been interpreted by comparison with Ni(m-H/D)57Fe enzyme mimics [(dppe)Ni(m-pdt)(m-H/D)57Fe(CO)3] þ and DFT calculations, which collectively indicate a low-spin Ni(II)(m-H)Fe(II) core for Ni-R, with H- binding Ni more tightly than Fe. The present methodology is also relevant to characterizing Fe–H moieties in other important natural and synthetic catalysts.
    Item Type: Article
    Keywords: Hydride bridge; NiFe-hydrogenase; observed; nuclear resonance; vibrational; spectroscopy;
    Academic Unit: Faculty of Science and Engineering > Chemistry
    Faculty of Science and Engineering > Research Institutes > Hamilton Institute
    Item ID: 15494
    Identification Number: 10.1038/ncomms8890
    Depositing User: Tobias Kraemer
    Date Deposited: 15 Feb 2022 12:13
    Journal or Publication Title: Nature Communications
    Publisher: Nature Research
    Refereed: Yes
    Related URLs:
    URI: https://mu.eprints-hosting.org/id/eprint/15494
    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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