Comparison of the peroxidatic activity of cytochrome P-450 with other hemoproteins and model compounds.
The H2O2 dependent catalysis of cytochrome P-450 was compared with the catalytic mechanism of horse radish peroxidase, methemoglobin and iron protoporphyrin complexes. A relatively stable intermediate being comparable to compound I of horse radish peroxidase is formed in the case of iron porphyrin complexes, methemoglobin and probably cytochrome P-450. In the case of peroxidase compound II is the more stable intermediate. This could be the reason for the different catalytic properties of peroxidase on the one hand and iron porphyrin complexes, methemoglobin and cytochrome P-450 on the other hand.
D000818:Animals; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism*; D004578:Electron Spin Resonance Spectroscopy; D006735:Horseradish Peroxidase / Q000378:metabolism*; D007700:Kinetics; D008297:Male; D008862:Microsomes, Liver / Q000187:drug effects / Q000378:metabolism*; D010544:Peroxidases / Q000378:metabolism*; D010545:Peroxides; D010634:Phenobarbital / Q000494:pharmacology; D011048:Polarography; D011817:Rabbits
D010545:Peroxides; D003577:Cytochrome P-450 Enzyme System; D006735:Horseradish Peroxidase; D010544:Peroxidases; D010634:Phenobarbital