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Enantiocomplementary Epoxidation Reactions Catalyzed by an Engineered Cofactor‐Independent Non‐natural Peroxygenase
Author(s) -
Xu Guangcai,
Crotti Michele,
Saravanan Thangavelu,
Kataja Kim M.,
Poelarends Gerrit J.
Publication year - 2020
Publication title -
angewandte chemie
Language(s) - English
Resource type - Journals
eISSN - 1521-3757
pISSN - 0044-8249
DOI - 10.1002/ange.202001373
Subject(s) - chemistry , cofactor , biocatalysis , iminium , catalysis , enzyme , combinatorial chemistry , protein engineering , metabolic engineering , stereochemistry , organic chemistry , reaction mechanism
Abstract Peroxygenases are heme‐dependent enzymes that use peroxide‐borne oxygen to catalyze a wide range of oxyfunctionalization reactions. Herein, we report the engineering of an unusual cofactor‐independent peroxygenase based on a promiscuous tautomerase that accepts different hydroperoxides ( t ‐BuOOH and H 2 O 2 ) to accomplish enantiocomplementary epoxidations of various α,β‐unsaturated aldehydes (citral and substituted cinnamaldehydes), providing access to both enantiomers of the corresponding α,β‐epoxy‐aldehydes. High conversions (up to 98 %), high enantioselectivity (up to 98 % ee ), and good product yields (50–80 %) were achieved. The reactions likely proceed via a reactive enzyme‐bound iminium ion intermediate, allowing tweaking of the enzyme's activity and selectivity by protein engineering. Our results underscore the potential of catalytic promiscuity for the engineering of new cofactor‐independent oxidative enzymes.