Kinetic, structural and electrostatic aspects of the reduction of pentacyanoferrate(III) complexes by myoglobin.
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.
Ilkowska
E
E
Faculty of Chemistry, Jagiellonian University, Kraków, Poland.
Lewiński
K
K
van Eldik
R
R
Stochel
G
G
D000818:Animals; D004583:Electrons; D005290:Ferric Compounds / Q000737:chemistry* / Q000378:metabolism*; D005292:Ferricyanides / Q000737:chemistry* / Q000378:metabolism*; D006736:Horses; D007700:Kinetics; D008956:Models, Chemical; D008958:Models, Molecular; D009211:Myoglobin / Q000737:chemistry* / Q000378:metabolism*; D010084:Oxidation-Reduction; D011487:Protein Conformation
D005290:Ferric Compounds; D005292:Ferricyanides; D009211:Myoglobin; C017595:oxymyoglobin; C121008:pentacyanoferrate (III)