Biocatalytic Enantioselective Oxidation of Sec-Allylic Alcohols with Flavin-Dependent Oxidases

Somayyeh Gandomkar, Etta Jost, Doris Loidolt, Alexander Swoboda, Mathias Pickl, Wael Elaily, Bastian Daniel, Marco W. Fraaije, Peter Macheroux, Wolfgang Kroutil

Research output: Contribution to journalArticleResearchpeer-review

Abstract

The oxidation of allylic alcohols is challenging to perform in a chemo- as well as stereo-selective fashion at the expense of molecular oxygen using conventional chemical protocols. Here, we report the identification of a library of flavin-dependent oxidases including variants of the berberine bridge enzyme (BBE) analogue from Arabidopsis thaliana (AtBBE15) and the 5-(hydroxymethyl)furfural oxidase (HMFO) and its variants (V465T, V465S, V465T/W466H and V367R/W466F) for the enantioselective oxidation of sec-allylic alcohols. While primary and benzylic alcohols as well as certain sugars are well known to be transformed by flavin-dependent oxidases, sec-allylic alcohols have not been studied yet except in a single report. The model substrates investigated were oxidized enantioselectively in a kinetic resolution with an E-value of up to >200. For instance HMFO V465S/T oxidized the (S)-enantiomer of (E)-oct-3-en-2-ol (1 a) and (E)-4-phenylbut-3-en-2-ol with E>200 giving the remaining (R)-alcohol with ee>99% at 50% conversion. The enantioselectivity could be decreased if required by medium engineering by the addition of cosolvents (e. g. dimethyl sulfoxide).
Original languageEnglish
Pages (from-to)5264-5271
Number of pages8
JournalAdvanced Synthesis and Catalysis
Volume361
Issue number22
DOIs
Publication statusPublished - 19 Nov 2019

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Keywords

  • Aerobic Oxidation, Asymmetric catalysis, Biocatalysis, Biotransformation, sec-Allylic alcohol

ASJC Scopus subject areas

  • Organic Chemistry
  • Biochemistry

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