Halofunctionalization of alkenes by vanadium chloroperoxidase from Curvularia inaequalis

Journal Article (2017)
Author(s)

J. Dong (TU Delft - BT/Biocatalysis)

Elena Fernandez Fueyo (TU Delft - BT/Biocatalysis)

Jingbo Li (Aarhus University)

Zheng Guo (Aarhus University)

Rokus Renirie (Universiteit van Amsterdam)

Ron Wever (Universiteit van Amsterdam)

Frank Hollmann (TU Delft - BT/Biocatalysis)

Research Group
BT/Biocatalysis
Copyright
© 2017 J. Dong, E. Fernandez Fueyo, Jingbo Li, Zheng Guo, Rokus Renirie, Ron Wever, F. Hollmann
DOI related publication
https://doi.org/10.1039/C7CC03368K
More Info
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Publication Year
2017
Language
English
Copyright
© 2017 J. Dong, E. Fernandez Fueyo, Jingbo Li, Zheng Guo, Rokus Renirie, Ron Wever, F. Hollmann
Research Group
BT/Biocatalysis
Issue number
46
Volume number
53
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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.