Cytochrome P450_BM-3 and P450 11A1 retain Compound I (FeO³⁺) chemistry with electrophilic substrates poised for Compound 0 (Fe³⁺O₂^-) reactions.

ABSTRACT: The catalytic cycle of cytochrome P450 (P450) enzymes involves ferric peroxide anion (Fe³⁺O₂^-, Compound 0) and perferryl oxygen (FeO³⁺, Compound I) intermediates. Compound I is generally viewed as responsible for most P450-catalyzed oxidations, but Compound 0 has been implicated in the oxidation of some carbonyl compounds, particularly deformylation reactions. We considered the hypothesis that Compound 0 could also attack other electrophilic carbon atoms and accordingly positioned keto groups at preferred hydroxylation sites of substrates for two P450s with well-defined catalytic reactions, bacterial P450_BM-3 (102A1), and human P450 11A1. The predicted products of Compound I and Compound 0 reactions were analyzed. With the normally pre

SUBMITTER: McCarty KD 

PROVIDER: S-EPMC12332404 | biostudies-literature | 2025 Jul

REPOSITORIES: biostudies-literature