High-valent iron(IV)-oxo complexes of heme and non-heme ligands in oxygenation reactions

Acc Chem Res. 2007 Jul;40(7):522-31. doi: 10.1021/ar700027f. Epub 2007 May 1.

Abstract

High-valent iron(IV)-oxo species have been implicated as the key reactive intermediates in the catalytic cycles of dioxygen activation by heme and non-heme iron enzymes. Our understanding of the enzymatic reactions has improved greatly via investigation of spectroscopic and chemical properties of heme and non-heme iron(IV)-oxo complexes. In this Account, reactivities of synthetic iron(IV)-oxo porphyrin pi-cation radicals and mononuclear non-heme iron(IV)-oxo complexes in oxygenation reactions have been discussed as chemical models of cytochrome P450 and non-heme iron enzymes. These results demonstrate how mechanistic developments in biomimetic research can help our understanding of dioxygen activation and oxygen atom transfer reactions in nature.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Biomimetic Materials / chemistry*
  • Cytochrome P-450 Enzyme System / chemistry
  • Iron / chemistry*
  • Ligands
  • Models, Molecular
  • Nonheme Iron Proteins / chemistry*
  • Oxidation-Reduction
  • Oxygen / chemistry
  • Oxygen / metabolism
  • Oxygenases / chemistry*
  • Porphyrins / chemistry
  • Substrate Specificity

Substances

  • Ligands
  • Nonheme Iron Proteins
  • Porphyrins
  • ferryl iron
  • Cytochrome P-450 Enzyme System
  • Iron
  • Oxygenases
  • Oxygen