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Biochemical pharmacology

Interactions of diethylphenylphosphine with purified, reconstituted mouse liver cytochrome P-450 monooxygenase systems.


PMID 3707601

Abstract

Purified mouse liver cytochrome P-450 reconstituted with purified NADPH-cytochrome P-450 reductase and phosphatidylcholine metabolized diethylphenylphosphine to diethylphenylphosphine oxide. NADPH was required for the reaction and the amount of oxide formed was time and cytochrome P-450 dependent. Purified phenobarbital-induced cytochrome P-450 produced more oxide per nmole enzyme than any of the purified uninduced cytochrome P-450s. the phosphine oxide was also formed in lesser amounts in incubation mixtures containing only NADPH-cytochrome P-450 reductase and NADPH. Diethylphenylphosphine bound to oxidized purified phenobarbital-induced cytochrome P-450 and uninduced cytochrome P-450 with Ks values of 16 microM and 11-18 microM respectively. Diethylphenylphosphine was also a competitive inhibitor of p-nitroanisole O-demethylation catalyzed by a reconstituted phenobarbital-induced cytochrome P-450-dependent monooxygenase system, with a Ki value of 5 microM. The phosphine oxide produced no observable optical difference spectrum with oxidized phenobarbital-induced cytochrome P-450 and caused no inhibition of p-nitroanisole O-demethylation.

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381241
Diethylphenylphosphine, 96%
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