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Laccase‐mediated Oxidations of Propargylic Alcohols. Application in the Deracemization of 1‐arylprop‐2‐yn‐1‐ols in Combination with Alcohol Dehydrogenases
Author(s) -
GonzálezGranda Sergio,
MéndezSánchez Daniel,
Lavandera Iván,
GotorFernández Vicente
Publication year - 2020
Publication title -
chemcatchem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.497
H-Index - 106
eISSN - 1867-3899
pISSN - 1867-3880
DOI - 10.1002/cctc.201901543
Subject(s) - chemistry , alcohol dehydrogenase , alcohol , laccase , biocatalysis , stereoselectivity , catalysis , organic chemistry , enantiomeric excess , combinatorial chemistry , enantioselective synthesis , reaction mechanism , enzyme
Abstract The catalytic system composed by the laccase from Trametes versicolor and the oxy‐radical TEMPO has been successfully applied in the sustainable oxidation of fourteen propargylic alcohols. The corresponding propargylic ketones were obtained in most cases in quantitative conversions (87–>99 % yield), demonstrating the efficiency of the chemoenzymatic methodology in comparison with traditional chemical oxidants, which usually lead to problems associated with the formation of by‐products. Also, the stereoselective reduction of propargylic ketones was studied using alcohol dehydrogenases such as the one from Ralstonia species overexpressed in E. coli or the commercially available evo‐1.1.200, allowing the access to both alcohol enantiomers mostly with complete conversions and variable selectivities depending on the aromatic pattern substitution (97–>99 % ee ). To demonstrate the compatibility of the laccase‐mediated oxidation and the alcohol dehydrogenase‐catalyzed bioreduction, a deracemization strategy starting from the racemic compounds was developed through a sequential one‐pot two‐step process, obtaining a selection of ( S )‐ or ( R )‐1‐arylprop‐2‐yn‐1‐ols with excellent yields (>98 %) and selectivities (>98 % ee ) depending on the alcohol dehydrogenase employed.