Enantiocomplementary Epoxidation Reactions Catalyzed by an Engineered Cofactor‐Independent Non‐Natural PeroxygenaseXu, G., Crotti, M., Thangavelu, S., Kataja, K. & Poelarends, G. J., 22-Jun-2020, In : Angewandte Chemie International Edition. 59, 26, p. 10374-10378 5 p.
Research output: Contribution to journal › Article › Academic › peer-review
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 H2O2) 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.
|Number of pages||5|
|Journal||Angewandte Chemie International Edition|
|Publication status||Published - 22-Jun-2020|
- MICHAEL-TYPE ADDITIONS, PEROXIDE-DRIVEN HYDROXYLATION, ANTARCTICA LIPASE B, 4-OXALOCROTONATE TAUTOMERASE, ASYMMETRIC EPOXIDATION, CHLOROPEROXIDASE, ACETALDEHYDE, OXIDATIONS, ALDEHYDES, ENZYMES