Carboxylate as the protonation site in (Peroxo)diiron(III) model complexes of soluble methane monooxygenase and related diiron proteins

J Am Chem Soc. 2010 Feb 3;132(4):1273-5. doi: 10.1021/ja909718f.

Abstract

Addition of H(+) to a synthetic (mu-1,2-peroxo)diiron(III) model complex results in protonation of a carboxylate rather than the peroxo ligand. This conclusion is based on spectroscopic evidence from UV-vis, (57)Fe Mossbauer, resonance Raman, infrared, and (1)H/(19)F NMR studies. These results suggest a similar role for protons in the dioxygen activation reactions in soluble methane monooxygenase and related carboxylate-bridged diiron enzymes.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Carboxylic Acids / chemistry*
  • Catalytic Domain
  • Ferric Compounds / chemistry*
  • Models, Biological
  • Oxygen / chemistry*
  • Oxygenases / chemistry*
  • Protons*

Substances

  • Carboxylic Acids
  • Ferric Compounds
  • Protons
  • Oxygenases
  • methane monooxygenase
  • Oxygen