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Enantiocomplementary Epoxidation Reactions Catalyzed by an Engineered Cofactor‐Independent Non‐Natural Peroxygenase
Xu, 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

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- Enantiocomplementary Epoxidation Reactions Catalyzed by an Engineered Cofactor‐Independent Non‐Natural Peroxygenase
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DOI
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.
Original language | English |
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Pages (from-to) | 10374-10378 |
Number of pages | 5 |
Journal | Angewandte Chemie International Edition |
Volume | 59 |
Issue number | 26 |
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
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