English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

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

MPS-Authors
/persons/resource/persons237664

Ogata,  Hideaki
Research Department Lubitz, Max Planck Institute for Chemical Energy Conversion, Max Planck Society;

/persons/resource/persons237625

Krämer,  Tobias
Research Department Neese, Max Planck Institute for Chemical Energy Conversion, Max Planck Society;

/persons/resource/persons216842

van Gastel,  Maurice
Research Department Neese, Max Planck Institute for Chemical Energy Conversion, Max Planck Society;

/persons/resource/persons216825

Neese,  Frank
Research Department Neese, Max Planck Institute for Chemical Energy Conversion, Max Planck Society;

/persons/resource/persons237637

Lubitz,  Wolfgang
Research Department Lubitz, Max Planck Institute for Chemical Energy Conversion, Max Planck Society;

External Ressource
No external resources are shared
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available
Citation

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.


Cite as: http://hdl.handle.net/21.11116/0000-0007-8942-4
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.