Transient FTIR spectroelectrochemical and stopped-flow detection of a mixed valence (Fe(I)-Fe(II)) bridging carbonyl intermediate with structural elements and spectroscopic characteristics of the di-iron sub-site of all-iron hydrogenase

Chem Commun (Camb). 2002 Apr 7:(7):700-1. doi: 10.1039/b111613b.

Abstract

Iron(I) in biology?: one-electron oxidation of an (Fe(I)-Fe(I)) carbonyl cyanide precursor bearing a proximal thioether group leads to an (Fe(I)-Fe(II)) bridging carbonyl transient with spectral features similar to the di-iron sub-site of the CO inhibited paramagnetic centre of all-iron hydrogenase.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry
  • Binding Sites
  • Electrochemistry
  • Hydrogenase / chemistry*
  • Iron-Sulfur Proteins / chemistry*
  • Ligands
  • Metalloproteins / chemistry
  • Molecular Structure
  • Nitriles / chemistry
  • Oxidation-Reduction
  • Spectroscopy, Fourier Transform Infrared / instrumentation
  • Spectroscopy, Fourier Transform Infrared / methods

Substances

  • Bacterial Proteins
  • Iron-Sulfur Proteins
  • Ligands
  • Metalloproteins
  • Nitriles
  • mesoxalonitrile
  • iron hydrogenase
  • Hydrogenase