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, Stephen P. Cramer

Research output: Contribution to journalArticlepeer-review


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 57 Fe-labelled fully reduced Ni-R form of Desulfovibrio vulgaris Miyazaki F [NiFe]-hydrogenase. A unique ' wagging' mode involving H- motion perpendicular to the Ni(μ1/4-H)57 Fe plane was studied using 57 Fe-specific nuclear resonance vibrational spectroscopy and density functional theory (DFT) calculations. On Ni(μ1/4-D) 57 Fe deuteride substitution, this wagging causes a characteristic perturbation of Fe-CO/CN bands. Spectra have been interpreted by comparison with Ni(μ1/4-H/D) 57 Fe enzyme mimics [(dppe)Ni(μ1/4-pdt)(μ1/4-H/D) 57 Fe(CO)3 ]+ and DFT calculations, which collectively indicate a low-spin Ni(II)(μ1/4-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.

Original languageEnglish (US)
Article number7890
JournalNature communications
StatePublished - Aug 10 2015

ASJC Scopus subject areas

  • Chemistry(all)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Physics and Astronomy(all)

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