Enabling highly (R)-enantioselective epoxidation of styrene by engineering unique non-natural P450 peroxygenases.

ABSTRACT: Unlike the excellent (S)-enantioselective epoxidation of styrene performed by natural styrene monooxygenases (ee > 99%), the (R)-enantioselective epoxidation of styrene has not yet achieved a comparable efficiency using natural or engineered oxidative enzymes. This report describes the H₂O₂-dependent (R)-enantioselective epoxidation of unfunctionalized styrene and its derivatives by site-mutated variants of a unique non-natural P450BM3 peroxygenase, working in tandem with a dual-functional small molecule (DFSM). The observed (R)-enantiomeric excess (ee) of styrene epoxidation is up to 99% with a turnover number (TON) of 918 by the best enantioselective mutant F87A/T268I/L181Q, while the best active mutant F87A/T268I/V78A/A184L (with 98% ee)

SUBMITTER: Zhao P 

PROVIDER: S-EPMC8115292 | biostudies-literature | 2021 Mar

REPOSITORIES: biostudies-literature