A requirement for an active proton delivery network supports a compound I-mediated C-C bond cleavage in CYP51 catalysis.

ABSTRACT: CYP51 enzymes (sterol 14α-demethylases) are cytochromes P450 that catalyze multistep reactions. The CYP51 reaction occurs in all biological kingdoms and is essential in sterol biosynthesis. It removes the 14α-methyl group from cyclized sterol precursors by first forming an alcohol, then an aldehyde, and finally eliminating formic acid with the introduction of a Δ14-15 double bond in the sterol core. The first two steps are typical hydroxylations, mediated by an electrophilic compound I mechanism. The third step, C-C bond cleavage, has been proposed to involve either compound I (i.e. FeO₃⁺) or, alternatively, a proton transfer-independent nucleophilic ferric peroxo anion (compound 0, i.e. Fe₃⁺O₂^-). Here, using c

SUBMITTER: Hargrove TY 

PROVIDER: S-EPMC7380200 | biostudies-literature | 2020 Jul

REPOSITORIES: biostudies-literature