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• W2092669210 abstract "The kinetics of NADPH-dependent reduction of cytochrome P450 LM2 in the soluble monomeric reconstituted system in the absence of any substrate is shown to be monophasic. We show that ferrous cytochrome c acts as a competitive inhibitor of the reduction. In the presence of 1 mm benzphetamine an additional extremely fast phase was observed. Under these conditions ferrous cytochrome c was found to be a competitive inhibitor of the slow phase of the reduction process, which accounted for 80% of the total reduction amplitude. Inhibition experiments yield a dissociation constant for the LM2-reductase complex of 3.0 ± 1.5 μm. This constant was the same both in the presence and in the absence of benzphetamine. Based on these data we conclude that cytochromes P450 and c bind to the same center on the NADPH-cytochrome P450 reductase molecule. Comparative analysis of the amino acid sequences reveals a detectable similarity between cytochrome c and cytochrome P450 LM2 at positions 68–87 and 121–145, respectively. In addition, a substantial similarity was shown for sequence fragments 204–224 of NADPH-cytochrome P450 reductase and 40–60 of cytochrome b5. Based on these findings a hypothesis for the location of the centers of intermolecular interactions on the molecules of cytochrome P450 LM2 and NADPH-cytochrome P450 reductase is proposed." @default.
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• W2092669210 date "1992-09-01" @default.
• W2092669210 modified "2023-09-27" @default.
• W2092669210 title "Cytochrome C (Fe2+) as a competitive inhibitor of NADPH-dependent reduction of cytochrome P450 LM2: Locating protein-protein interaction sites in microsomal electron carriers" @default.
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• W2092669210 doi "https://doi.org/10.1016/0003-9861(92)90677-o" @default.
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