The interaction of aliphatic analogs of methylene-dioxyphenyl compounds with cytochromes P-450 and P-420.
The spectra resulting from the interaction of a series of substituted dioxolanes with microsomal cytochromes P-450 or P-420, as well as purified cytochrome P-450, were measured. With the exception of dioxolane, 4-methyldioxolane and 4-ethyldioxolane, these compounds interacted with ferric cytochrome P-450 to give complexes exhibiting type I optical difference spectra, and, after incubation with NADPH, spectra with peaks at about 430 nm. These complexes, as well as those formed from dioxolanes in the presence of cumene hydroperoxide, inhibit the binding of CO to the cytochrome. Consideration of the known chemistry of dioxolanes, together with recent advances in the understanding of double Soret spectra, lead to a possible explanation for the differences between the spectra of dioxolanes and their aromatic analogs, the methylenedioxyphenyl compounds.
D000818:Animals; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism; D003580:Cytochromes / Q000378:metabolism*; D004148:Dioxolanes / Q000378:metabolism*; D004149:Dioxoles / Q000378:metabolism*; D008297:Male; D051379:Mice; D009249:NADP / Q000378:metabolism; D013053:Spectrophotometry
D003580:Cytochromes; D004148:Dioxolanes; D004149:Dioxoles; D009249:NADP; D003577:Cytochrome P-450 Enzyme System