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Enabling Highly (R)-Enantioselective Epoxidation of Styrene by Engineering Non-natural P450 Peroxygenase.pdf (836.81 kB)
Enabling Highly (R)-Enantioselective Epoxidation of Styrene by Engineering Unique Non-Natural P450 Peroxygenases
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submitted on 01.11.2020, 02:59 and posted on 02.11.2020, 12:08by Panxia Zhao, Jie Chen, Nana Ma, Jingfei Chen, Xiangquan Qin, Chuanfei Liu, Fuquan Yao, Lishan Yao, Longyi Jin, Zhiqi Cong
Unlike the excellent (S)-enantioselective epoxidation of
styrene performed by natural styrene monooxygenase (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 of styrene epoxidation is up to ~99%, which is unprecedented relative to
natural or engineered oxidative enzymes. The catalytic turnover number is up to
~4500 (with ~98% ee), representing
the best activity of a P450 peroxygenase towards styrene epoxidation, to date.
This study indicates that the synergistic use of protein engineering and an
exogenous DFSM constitutes an efficient strategy to control enantioselectivity
of styrene epoxidation, thus substantially expanding the chemical scope of P450
enzyme functions as useful bio-oxidative catalysts.