Halofunctionalization of alkenes by vanadium chloroperoxidase from Curvularia inaequalis

Journal article (2017)

Authors

J. Dong BT/Biocatalysis - AS
E. Fernandez Fueyo BT/Biocatalysis - AS
Jingbo Li Aarhus University
Zheng Guo Aarhus University
Rokus Renirie Universiteit van Amsterdam
Ron Wever Universiteit van Amsterdam
F. Hollmann BT/Biocatalysis - AS
Research Group
BT/Biocatalysis (AS) (TU Delft)
Copyright: © 2017 J. Dong, E. Fernandez Fueyo, Jingbo Li, Zheng Guo, Rokus Renirie, Ron Wever, F. Hollmann
DOI: https://doi.org/10.1039/C7CC03368K
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Published Date

2017-5

Language

English

Faculty

Applied Sciences

Department

BT/Biotechnologie

Research Group

BT/Biocatalysis

Abstract

The vanadium-dependent chloroperoxidase from Curvularia inaequalis is a stable and efficient biocatalyst for the hydroxyhalogenation of a broad range of alkenes into halohydrins. Up to 1 200 000 TON with 69 s−1 TOF were observed for the biocatalyst. A bienzymatic cascade to yield epoxides as reaction products is presented.