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

Author

Listed:
  • Hideaki Ogata

    (Max Planck Institute for Chemical Energy Conversion)

  • Tobias Krämer

    (Max Planck Institute for Chemical Energy Conversion)

  • Hongxin Wang

    (University of California
    Lawrence Berkeley National Laboratory)

  • David Schilter

    (University of Illinois
    Present address: IBS Center for Multidimensional Carbon Materials, Ulsan National Institute of Science and Technology, Ulsan 689-798, Republic of Korea)

  • Vladimir Pelmenschikov

    (Institut für Chemie, Technische Universität Berlin)

  • Maurice van Gastel

    (Max Planck Institute for Chemical Energy Conversion)

  • Frank Neese

    (Max Planck Institute for Chemical Energy Conversion)

  • Thomas B. Rauchfuss

    (University of Illinois)

  • Leland B. Gee

    (University of California)

  • Aubrey D. Scott

    (University of California)

  • Yoshitaka Yoda

    (SPring-8/JASRI)

  • Yoshihito Tanaka

    (Materials Dynamics Laboratory
    Present address: Graduate School of Material Science, University of Hyogo, Hyogo 678-1297, Japan)

  • Wolfgang Lubitz

    (Max Planck Institute for Chemical Energy Conversion)

  • Stephen P. Cramer

    (University of California
    Lawrence Berkeley National Laboratory)

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(μ-H)57Fe plane was studied using 57Fe-specific nuclear resonance vibrational spectroscopy and density functional theory (DFT) calculations. On Ni(μ-D)57Fe deuteride substitution, this wagging causes a characteristic perturbation of Fe–CO/CN bands. Spectra have been interpreted by comparison with Ni(μ-H/D)57Fe enzyme mimics [(dppe)Ni(μ-pdt)(μ-H/D)57Fe(CO)3]+ and DFT calculations, which collectively indicate a low-spin Ni(II)(μ-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.

Suggested Citation

  • Hideaki Ogata & Tobias Krämer & Hongxin Wang & David Schilter & Vladimir Pelmenschikov & Maurice van Gastel & Frank Neese & Thomas B. Rauchfuss & Leland B. Gee & Aubrey D. Scott & Yoshitaka Yoda & Yos, 2015. "Hydride bridge in [NiFe]-hydrogenase observed by nuclear resonance vibrational spectroscopy," Nature Communications, Nature, vol. 6(1), pages 1-8, November.
    • Handle: RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms8890
    DOI: 10.1038/ncomms8890
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