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

Ogata, H., Krämer, T., Wang, H., Schilter, D., Pelmenschikov, V., van Gastel, M., et al. (2015). Hydride bridge in [NiFe]-hydrogenase observed by nuclear resonance vibrational spectroscopy. Nature Communications, 6: 7890. doi:10.1038/ncomms8890.

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 Creators:
Ogata, Hideaki1, Author              
Krämer, Tobias2, Author              
Wang, Hongxin3, 4, Author
Schilter, David5, Author
Pelmenschikov, Vladimir6, Author
van Gastel, Maurice2, Author              
Neese, Frank2, Author              
Rauchfuss, Thomas B.5, Author
Gee, Leland B.3, Author
Scott, Aubrey D.3, Author
Yoda, Yoshitaka7, Author
Tanaka, Yoshihito8, Author
Lubitz, Wolfgang1, Author              
Cramer, Stephen P.3, 4, Author
Affiliations:
1Research Department Lubitz, Max Planck Institute for Chemical Energy Conversion, Max Planck Society, ou_3023873              
2Research Department Neese, Max Planck Institute for Chemical Energy Conversion, Max Planck Society, ou_3023886              
3Department of Chemistry, University of California, Davis, 95616, California, USA, ou_persistent22              
4Division of Physical Biosciences, Lawrence Berkeley National Laboratory, Berkeley, 94720, California, USA, ou_persistent22              
5Department of Chemistry, University of Illinois, Urbana, 61801, Illinois, USA, ou_persistent22              
6Institut für Chemie, Technische Universität Berlin, Berlin, 10623, Germany, ou_persistent22              
7Division of Research and Utilization, SPring-8/JASRI, Hyogo, 679-5198, Japan, ou_persistent22              
8Materials Dynamics Laboratory, RIKEN SPring-8, Hyogo, 679-5148, Japan, ou_persistent22              

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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(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.

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Language(s): eng - English
 Dates: 2015-02-042015-06-182015-08-10
 Publication Status: Published online
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1038/ncomms8890
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Title: Nature Communications
  Abbreviation : Nat. Commun.
Source Genre: Journal
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Publ. Info: London : Nature Publishing Group
Pages: - Volume / Issue: 6 Sequence Number: 7890 Start / End Page: - Identifier: ISSN: 2041-1723
CoNE: https://pure.mpg.de/cone/journals/resource/2041-1723