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

Guangcai Xu, Michele Crotti, Saravan Thangavelu, Kim Kataja, Gerrit J. Poelarends*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

6 Citations (Scopus)
36 Downloads (Pure)

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 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 languageEnglish
Pages (from-to)10374-10378
Number of pages5
JournalAngewandte Chemie International Edition
Volume59
Issue number26
DOIs
Publication statusPublished - 22-Jun-2020

Keywords

  • MICHAEL-TYPE ADDITIONS
  • PEROXIDE-DRIVEN HYDROXYLATION
  • ANTARCTICA LIPASE B
  • 4-OXALOCROTONATE TAUTOMERASE
  • ASYMMETRIC EPOXIDATION
  • CHLOROPEROXIDASE
  • ACETALDEHYDE
  • OXIDATIONS
  • ALDEHYDES
  • ENZYMES

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