Journal
NATURE COMMUNICATIONS
Volume 6, Issue -, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/ncomms8890
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Funding
- DOE Office of Biological and Environmental Research
- NIH [GM-65440]
- DOE grant [DEFG02-90ER14146]
- BMBF [03SF0355C]
- EU/Energy Network project SOLAR-H2 (FP7) [212508]
- DFG-funded Cluster of Excellence RESOLV [EXC1069]
- Max Planck Society
- DFG-funded 'Unifying Concepts in Catalysis' (UniCat) initiative
- JASRI [2012A0032-2014B1032]
- RIKEN [20120107, 20130022, 20140033]
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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 Fe-57-labelled fully reduced Ni-R form of Desulfovibrio vulgaris Miyazaki F [NiFe]-hydrogenase. A unique 'wagging' mode involving H- motion perpendicular to the Ni(mu-H)Fe-57 plane was studied using Fe-57-specific nuclear resonance vibrational spectroscopy and density functional theory (DFT) calculations. On Ni(mu-D)Fe-57 deuteride substitution, this wagging causes a characteristic perturbation of Fe-CO/CN bands. Spectra have been interpreted by comparison with Ni(mu-H/D)Fe-57 enzyme mimics [(dppe)Ni(mu-pdt)(mu-H/D)Fe-57(CO) 3](+) and DFT calculations, which collectively indicate a low-spin Ni(II)(mu-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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