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

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, Yoshihito Tanaka, Wolfgang Lubitz and Stephen P. Cramer ()
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Hideaki Ogata: Max Planck Institute for Chemical Energy Conversion
Tobias Krämer: Max Planck Institute for Chemical Energy Conversion
Hongxin Wang: University of California
David Schilter: University of Illinois
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
Wolfgang Lubitz: Max Planck Institute for Chemical Energy Conversion
Stephen P. Cramer: University of California

Nature Communications, 2015, vol. 6, issue 1, 1-8

Abstract: 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.

Date: 2015
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DOI: 10.1038/ncomms8890

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