Study of H2O2-supported N-demethylations catalyzed by cytochrome P-450 and horseradish peroxidase.
H2O2-supported oxidative demethylation reactions catalyzed by cytochrome P-450 and horseradish peroxidase have been compared. In contrast to peroxidase catalyzed reactions no free substrate radicals could be detected by EPR stopped flow measurements in demethylation reactions catalyzed by highly purified cytochrome P-450 although the rate of product formation for both enzyme systems was identical. These findings cause doubts in a general peroxide dependent demethylation mechanism valid for all hemoproteins and in the hypothesis that free substrate radicals are principally formed during cytochrome P-450 catalysis.
D000632:Aminopyrine / Q000378:metabolism; D000818:Animals; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism*; D004578:Electron Spin Resonance Spectroscopy; D006735:Horseradish Peroxidase / Q000378:metabolism*; D006861:Hydrogen Peroxide / Q000378:metabolism*; D008099:Liver / Q000201:enzymology; D010089:Oxidoreductases, N-Demethylating / Q000378:metabolism*; D010544:Peroxidases / Q000378:metabolism*; D011817:Rabbits
D000632:Aminopyrine; D003577:Cytochrome P-450 Enzyme System; D006861:Hydrogen Peroxide; D006735:Horseradish Peroxidase; D010544:Peroxidases; D010089:Oxidoreductases, N-Demethylating