Kinetic, structural and electrostatic aspects of the reduction of pentacyanoferrate(III) complexes by myoglobin

J Biol Inorg Chem. 1999 Jun;4(3):302-10. doi: 10.1007/s007750050316.

Abstract

The mechanism of the reduction of pentacyanoferrate(III) complexes by oxymyoglobin has been studied by conventional and high-pressure kinetic methods, and also by structural modelling. The results of this and an earlier study show that an outer-sphere mechanism is operating for electron transfer between oxymyoglobin and FeIII(CN)5Ln-, independent of the lability of the ligand L. The electron transfer process is preceded by precursor formation at a specific site on the protein close to the protein heme pocket.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Electrons
  • Ferric Compounds / chemistry*
  • Ferric Compounds / metabolism*
  • Ferricyanides / chemistry*
  • Ferricyanides / metabolism*
  • Horses
  • Kinetics
  • Models, Chemical
  • Models, Molecular
  • Myoglobin / chemistry*
  • Myoglobin / metabolism*
  • Oxidation-Reduction
  • Protein Conformation

Substances

  • Ferric Compounds
  • Ferricyanides
  • Myoglobin
  • oxymyoglobin
  • pentacyanoferrate (III)