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Chloroperoxidase‐Catalyzed Achmatowicz Rearrangements
Author(s) -
Thiel Daniel,
Blume Fabian,
Jäger Christina,
Deska Jan
Publication year - 2018
Publication title -
european journal of organic chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.825
H-Index - 155
eISSN - 1099-0690
pISSN - 1434-193X
DOI - 10.1002/ejoc.201800333
Subject(s) - chemistry , enantioselective synthesis , biocatalysis , catalysis , glucose oxidase , ring (chemistry) , oxidase test , enzyme , organic chemistry , combinatorial chemistry , stereochemistry , reaction mechanism
Chloroperoxidase from Caldariomyces fumago catalyzes the selective oxidation of furfuryl alcohols in an Achmatowicz‐type ring expansion. In combination with glucose oxidase as oxygen‐activating biocatalyst, a purely enzymatic, aerobic protocol for the synthesis of 6‐hydroxypyranone building blocks is obtained. Thanks to an only modest stereochemical bias of the oxygenating heme protein, optically active alcohols of either configuration are converted without a significant mismatch opening up opportunities for enantioselective multienzymatic cascades. Balancing the oxidase‐driven aerobic activation, extended enzyme half‐lives and productive conversion of poorly soluble and slowly reacting substrates can be achieved with high yields of the six‐membered O‐heterocycles.