Abstract
When incorporated into phospholipid vesicles containing NADPH-cytochrome P-450 reductase and P-450 LM 2, cytochrome b 5 enhanced the rate of NADPH-supported hydroxylation of 7-ethoxycoumarin or p -nitroanisole about 5-fold. Cytochrome b 5 did not affect the rate of NADPH-oxidation, nor the rate of NADPH-supported formation of the ferrous CO-complex of cytochrome P-450. However, the cytochrome b 5-mediated increase in product formation was found to be correlated with concomitant decreases in the production of H 2O 2 or O 2 − in the system, thus strongly indicating cytochrome b 5 being a more efficient donor of the second electron to cytochrome P-450 than is NADPH-cytochrome P-450 reductase.
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