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Zwitterionic detergent mediated interaction of purified cytochrome p 450l m 4 from 5 6 benzoflavone treated rabbits with nadph cytochrome p 450 reductase

, : Zwitterionic detergent mediated interaction of purified cytochrome p 450l m 4 from 5 6 benzoflavone treated rabbits with nadph cytochrome p 450 reductase. Biochemistry 26(8): 2343-2348

Hydroxylation of acetanilide catalyzed by purified cytochrome P-450Lm4 and NADPH-cytochrome P-450 reductase was reconstituted with the zwitterionic detergent 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate (CHAPS). The optimum rate of production of 4-hydroxyacetanilide was observed between 3 and 7 mM CHAPS and was about half that with 0.05 mM dilauroylglyceryl-3-phosphocholine (di-12-GPC). At higher detergent concentrations, hydroxylase activity decreased until at 15-20 mM CHAPS the system was inactive. The effect of CHAPS on the state of aggregation of P-450LM4 and on interaction between the cytochrome and P450 reductase alone and under turnover conditions was investigated by ultracentrifugation. At 4 mM CHAPS, P-450LM4 was hexameric to heptameric (Mr 369,000). Neither reductase nor reductase plus acetanilide and NADPH altered the state of P-450LM4 aggregation, suggesting that a stable 1:1 P-450/reductase complex did not form under turnover conditions. Replacing CHAPS with 0.05 mM di-12-GPC resulted in formation of heterogeneous P-450 oligomers (Mr > 480,000). At CHAPS concentrations where substrate hydroxylation did not occur (15 and 22 mM), P-450Lm4 was shown by sedimentation equilibrium measurements to be dimeric and monomeric, respectively. P-450 reductase was shown to reduce monomeric P-450LM4 in the presence of NADPH. This, the dependence of hydroxylase activity on [CHAPS] may be related to the state of aggregation of the cytochrome. An apprent correlation between P-450 aggregation state and NADPH-supported hydroxylation was also observed with phenobarbital-inducible P-450LM2 in the presence of detergents.


PMID: 3113479

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