Roles of Ferric Peroxide Anion Intermediates (Fe³⁺O₂ ^-, Compound 0) in Cytochrome P450 19A1 Steroid Aromatization and a Cytochrome P450 2B4 Secosteroid Oxidation Model.

ABSTRACT: Cytochrome P450 (P450, CYP) 19A1 is the steroid aromatase, the enzyme responsible for the 3-step conversion of androgens (androstenedione or testosterone) to estrogens. The final step is C-C bond scission (removing the 19-oxo group as formic acid) that proceeds via a historically controversial reaction mechanism. The two competing mechanistic possibilities involve a ferric peroxide anion (Fe³⁺O₂ ^-, Compound 0) and a perferryl oxy species (FeO³⁺, Compound I). One approach to discern the role of each species in the reaction is with the use of oxygen-18 labeling, i.e., from ¹⁸O₂ and H₂ ¹⁸O of the reaction product formic acid. We applied this approach, using several technical improvements, to study the defo

SUBMITTER: Tateishi Y 

PROVIDER: S-EPMC11519728 | biostudies-literature | 2024 Aug

REPOSITORIES: biostudies-literature