Fe-S complexes containing five-membered heterocycles: novel models for the active site of hydrogenases with unusual low reduction potential

Dalton Trans. 2007 Feb 28:(8):896-902. doi: 10.1039/b615037c. Epub 2007 Jan 24.

Abstract

Three biomimetic 2Fe2S complexes [{(micro-SCH2)2NCH2(2-C4H3O)}](Fe2(CO)6), [{(micro-SCH2)2 NCH2(2-C4H3S)}](Fe2(CO)6) and [{(micro-SCH2)2NCH2(5-Br-2-C4H2S)}Fe2(CO)6] were prepared as models for the active site of Fe-only hydrogenase by the convergent process from [(micro-S2)Fe2(CO)6] and N,N-bis(hydromethyl)-2-furan and thiophene. The structures of these complexes were identified spectroscopically and crystallographically. The electrochemical behavior of the complexes and was unique as they showed catalytic proton reduction with a low reduction potential at -1.13 and -1.09 V vs Fc/Fc+, respectively, in the presence of HClO4.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Binding Sites
  • Electrochemistry
  • Ferrous Compounds / chemical synthesis
  • Ferrous Compounds / chemistry*
  • Hydrogenase / chemistry*
  • Iron-Sulfur Proteins / chemistry*
  • Models, Molecular*
  • Molecular Structure
  • Oxidation-Reduction
  • Protons

Substances

  • Ferrous Compounds
  • Iron-Sulfur Proteins
  • Protons
  • iron hydrogenase
  • Hydrogenase