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Chemoenzymatic Halogenation of Phenols by using the Haloperoxidase from Curvularia inaequalis
Author(s) -
FernándezFueyo Elena,
van Wingerden Marco,
Renirie Rokus,
Wever Ron,
Ni Yan,
Holtmann Dirk,
Hollmann Frank
Publication year - 2015
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.201500862
Subject(s) - halogenation , curvularia , chemistry , vanadium , organic chemistry , catalysis , biocatalysis , electrophile , reaction mechanism , food science , penicillium
The vanadium‐dependent chloroperoxidase from Curvularia inaequalis is an efficient biocatalyst for the in situ generation of hypohalous acids and subsequent electrophilic oxidation/halogenation reactions. Especially, its superb activity and stability under operational conditions make it an attractive catalyst for organic synthesis. Herein, the efficient bromination of thymol was investigated, and turnover numbers of the enzyme were found to exceed 2 000 000. The major novelty of the work is that vanadium chloroperoxidase is more useful as a brominating enzyme than vanadium bromoperoxidase in terms of operational stability, besides being far more stable than heme‐containing peroxidases.