One-electron reduction of the oxy form of cobalt-substituted hemoproteins.
The reduction of oxy forms in cobalt-substituted hemoproteins by the hydrated electron (e(aq)-) was investigated by pulse radiolysis. The hydrated electron (e(aq)-) reacted with the oxy form of cobalt horseradish peroxidase (CoHRP) to form CoHRP. On the other hand, the initial product observed in the reaction of the oxy form of cobalt myoglobin (CoMb) with e(aq)- is neither CoMb nor Co3+ Mb. Subsequently, the product was found to convert to another form, the irreversible change in the porphyrin. In contrast to e(aq)-, both oxy forms of CoMb and CoHRP were reduced by various electron donors to form the cobaltic forms.
Kobayashi
K
K
Institute of Scientific and Industrial Research, Osaka University, Japan.
Amano
M
M
Hayashi
K
K
D003035:Cobalt; D004583:Electrons; D006735:Horseradish Peroxidase / Q000378:metabolism*; D007700:Kinetics; D009211:Myoglobin / Q000378:metabolism*; D010084:Oxidation-Reduction; D010544:Peroxidases / Q000378:metabolism*; D011675:Pulse Radiolysis; D013053:Spectrophotometry
D009211:Myoglobin; D003035:Cobalt; D006735:Horseradish Peroxidase; D010544:Peroxidases