Ogata, Hideaki and Krämer, Tobias and Wang, Hongxin and Schilter, David and Pelmenschikov, Vladimir and van Gastel, Maurice and Neese, Frank and Rauchfuss, Thomas B. and Gee, Leland B. and Scott, Aubrey D. and Yoda, Yoshitaka and Tanaka, Yoshihito and Lubitz, Wolfgang and Cramer, Stephen P. (2015) Hydride bridge in [NiFe]-hydrogenase observed by nuclear resonance vibrational spectroscopy. Nature Communications, 6 (1). ISSN 2041-1723

Preview

Download (1MB) | Preview

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(m-H)57Fe plane was studied using 57Fe-specific nuclear resonance vibrational spectroscopy and density functional theory (DFT) calculations. On Ni(m-D)57Fe deuteride substitution, this wagging causes a characteristic perturbation of Fe–CO/CN bands. Spectra have been interpreted by comparison with Ni(m-H/D)57Fe enzyme mimics [(dppe)Ni(m-pdt)(m-H/D)57Fe(CO)3] þ and DFT calculations, which collectively indicate a low-spin Ni(II)(m-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.

Item Type:	Article
Keywords:	Hydride bridge; NiFe-hydrogenase; observed; nuclear resonance; vibrational; spectroscopy;
Academic Unit:	Faculty of Science and Engineering > Chemistry Faculty of Science and Engineering > Research Institutes > Hamilton Institute
Item ID:	15494
Identification Number:	https://doi.org/10.1038/ncomms8890
Depositing User:	Tobias Kraemer
Date Deposited:	15 Feb 2022 12:13
Journal or Publication Title:	Nature Communications
Publisher:	Nature Research
Refereed:	Yes
URI:	Publisher
Use Licence:	This item is available under a Creative Commons Attribution Non Commercial Share Alike Licence (CC BY-NC-SA). Details of this licence are available here

Repository Staff Only(login required)

Item control page

Downloads

Origin of downloads