An S-Oxygenated [NiFe] Complex Modelling Sulfenate Intermediates of an O2 -Tolerant Hydrogenase

Angew Chem Int Ed Engl. 2017 Feb 13;56(8):2208-2211. doi: 10.1002/anie.201611069. Epub 2017 Jan 12.

Abstract

To understand the molecular details of O2 -tolerant hydrogen cycling by a soluble NAD+ -reducing [NiFe] hydrogenase, we herein present the first bioinspired heterobimetallic S-oxygenated [NiFe] complex as a structural and vibrational spectroscopic model for the oxygen-inhibited [NiFe] active site. This compound and its non-S-oxygenated congener were fully characterized, and their electronic structures were elucidated in a combined experimental and theoretical study with emphasis on the bridging sulfenato moiety. Based on the vibrational spectroscopic properties of these complexes, we also propose novel strategies for exploring S-oxygenated intermediates in hydrogenases and similar enzymes.

Keywords: IR spectroscopy; [NiFe] hydrogenases; enzyme models; resonance Raman spectroscopy; spectroscopic models.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Catalytic Domain
  • Crystallography, X-Ray
  • Cupriavidus necator / chemistry
  • Cupriavidus necator / enzymology*
  • Hydrogenase / chemistry*
  • Models, Molecular
  • Oxygen / chemistry*
  • Spectrophotometry, Infrared
  • Spectrum Analysis, Raman

Substances

  • nickel-iron hydrogenase
  • Hydrogenase
  • Oxygen