Nature of the peroxo intermediate of the W48F/D84E ribonucleotide reductase variant: implications for O2 activation by binuclear non-heme iron enzymes

J Am Chem Soc. 2004 Jul 21;126(28):8842-55. doi: 10.1021/ja049106a.

Abstract

Analysis of the spectroscopic signatures of the R2-W48F/D84E biferric peroxo intermediate identifies a cis mu-1,2 peroxo coordination geometry. DFT geometry optimizations on both R2-W48F/D84E and R2-wild-type peroxo intermediate models including constraints imposed by the protein also identify the cis mu-1,2 peroxo geometry as the most stable peroxo intermediate structure. This study provides significant insight into the electronic structure and reactivity of the R2-W48F/D84E peroxo intermediate, structurally related cis mu-1,2 peroxo model complexes, and other enzymatic biferric peroxo intermediates.

Publication types

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

MeSH terms

  • Binding Sites / genetics
  • Binding Sites / physiology
  • Computer Simulation
  • Ferrous Compounds / chemistry
  • Models, Chemical
  • Models, Molecular
  • Mutagenesis, Site-Directed
  • Nonheme Iron Proteins / chemistry*
  • Oxygen / chemistry*
  • Peroxides / chemistry
  • Ribonucleotide Reductases / analysis
  • Ribonucleotide Reductases / chemistry*
  • Spectrum Analysis, Raman / methods

Substances

  • Ferrous Compounds
  • Nonheme Iron Proteins
  • Peroxides
  • Ribonucleotide Reductases
  • ribonucleotide reductase R2 subunit
  • Oxygen