[Oxygenase activity of cytochrome P-450 electrochemically reduced in the presence of methylviologen].
An electrochemical system of cytochrome P-450 reduction in the presence of the water-soluble redox carrier methylviologen has been developed. In this system cytochrome P-450 effectuates a steady-state demethylation of dimethylaniline and hydroxylation of aniline. The results of control experiments suggest that the above reactions are mediated by cytochrome P-450. The effect of the peroxidase reaction is excluded by an addition of high concentrations of catalase to the incubation mixture. At the same time the hydroxylation of these substrates is accompanied by methylviologen demethylation.
Remizov
V A
VA
Archakov
A I
AI
Kariakin
A V
AV
Byzova
N A
NA
D000818:Animals; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism*; D004563:Electrochemistry; D008297:Male; D008862:Microsomes, Liver / Q000201:enzymology; D010084:Oxidation-Reduction; D010105:Oxygenases; D010269:Paraquat / Q000378:metabolism*; D011817:Rabbits; D013379:Substrate Specificity
D003577:Cytochrome P-450 Enzyme System; D010105:Oxygenases; D010269:Paraquat
Oksigenaznaia aktivnost' tsitokhroma P-450, vosstanovlennogo élektrokhimicheski v prisutstvii metilviologena.