title: Hydride bridge in [NiFe]-hydrogenase observed by nuclear resonance vibrational spectroscopy.
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 (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(μ-H)(57)Fe plane was studied using (57)Fe-specific nuclear resonance vibrational spectroscopy and density functional theory (DFT) calculations. On Ni(μ-D)(57)Fe deuteride substitution, this wagging causes a characteristic perturbation of Fe-CO/CN bands. Spectra have been interpreted by comparison with Ni(μ-H/D)(57)Fe enzyme mimics [(dppe)Ni(μ-pdt)(μ-H/D)(57)Fe(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.
authors.affiliation: Max Planck Institute for Chemical Energy Conversion, Mülheim an der Ruhr 45470, Germany.
authors.forename: Hideaki
authors.initials: H
authors.lastname: Ogata
authors.affiliation: Max Planck Institute for Chemical Energy Conversion, Mülheim an der Ruhr 45470, Germany.
authors.forename: Tobias
authors.initials: T
authors.lastname: Krämer
authors.affiliation: 1] Department of Chemistry, University of California, Davis, California 95616, USA [2] Division of Physical Biosciences, Lawrence Berkeley National Laboratory, Berkeley, California 94720, USA.
authors.forename: Hongxin
authors.initials: H
authors.lastname: Wang
authors.affiliation: Department of Chemistry, University of Illinois, Urbana, Illinois 61801, USA.
authors.forename: David
authors.identifier: 0000000257206806
authors.initials: D
authors.lastname: Schilter
authors.affiliation: Institut für Chemie, Technische Universität Berlin, Berlin 10623, Germany.
authors.forename: Vladimir
authors.initials: V
authors.lastname: Pelmenschikov
authors.affiliation: Max Planck Institute for Chemical Energy Conversion, Mülheim an der Ruhr 45470, Germany.
authors.forename: Maurice
authors.initials: M
authors.lastname: van Gastel
authors.affiliation: Max Planck Institute for Chemical Energy Conversion, Mülheim an der Ruhr 45470, Germany.
authors.forename: Frank
authors.initials: F
authors.lastname: Neese
authors.affiliation: Department of Chemistry, University of Illinois, Urbana, Illinois 61801, USA.
authors.forename: Thomas B
authors.initials: TB
authors.lastname: Rauchfuss
authors.affiliation: Department of Chemistry, University of California, Davis, California 95616, USA.
authors.forename: Leland B
authors.identifier: 0000000258173997
authors.initials: LB
authors.lastname: Gee
authors.affiliation: Department of Chemistry, University of California, Davis, California 95616, USA.
authors.forename: Aubrey D
authors.initials: AD
authors.lastname: Scott
authors.affiliation: Division of Research and Utilization, SPring-8/JASRI, Hyogo 679-5198, Japan.
authors.forename: Yoshitaka
authors.initials: Y
authors.lastname: Yoda
authors.affiliation: Materials Dynamics Laboratory, RIKEN SPring-8, Hyogo 679-5148, Japan.
authors.forename: Yoshihito
authors.initials: Y
authors.lastname: Tanaka
authors.affiliation: Max Planck Institute for Chemical Energy Conversion, Mülheim an der Ruhr 45470, Germany.
authors.forename: Wolfgang
authors.initials: W
authors.lastname: Lubitz
authors.affiliation: 1] Department of Chemistry, University of California, Davis, California 95616, USA [2] Division of Physical Biosciences, Lawrence Berkeley National Laboratory, Berkeley, California 94720, USA.
authors.forename: Stephen P
authors.initials: SP
authors.lastname: Cramer
mesh_terms: D016969:Desulfovibrio vulgaris / Q000201:enzymology*; D006864:Hydrogenase / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy
chemical_list: C043296:nickel-iron hydrogenase; D006864:Hydrogenase