Demethylation of tertiary amines by a reconstituted cytochrome P-450 enzyme system: kinetics of oxygen consumption and hydrogen peroxide formation.
Initial reaction rates of oxygen consumption and hydrogen peroxide formation in a cytochrome P-450 catalyzed reaction are practically independent of the nature of tertiary amines that were used as substrates. From the kinetic studies and the substrate conversion results that the amount of water formed in a side reaction is determined by the substrate specificity. Both hydrogen peroxide and water formation lower the efficiency of the monooxygenatic activity of cytochrome P-450.
Ristau
O
O
Central Institute of Molecular Biology, Academy of Sciences of the GDR, Berlin-Buch.
Wagnerova
D M
DM
Rein
H
H
Ruckpaul
K
K
D000588:Amines / Q000378:metabolism*; D000818:Animals; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism*; D006861:Hydrogen Peroxide / Q000378:metabolism; D007700:Kinetics; D008297:Male; D008745:Methylation; D010084:Oxidation-Reduction; D010101:Oxygen Consumption; D011817:Rabbits
D000588:Amines; D003577:Cytochrome P-450 Enzyme System; D006861:Hydrogen Peroxide