Issue 46, 2017

Halofunctionalization of alkenes by vanadium chloroperoxidase from Curvularia inaequalis

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.

Graphical abstract: Halofunctionalization of alkenes by vanadium chloroperoxidase from Curvularia inaequalis

Supplementary files

Article information

Article type
Communication
Submitted
01 May 2017
Accepted
22 May 2017
First published
22 May 2017
This article is Open Access
Creative Commons BY-NC license

Chem. Commun., 2017,53, 6207-6210

Halofunctionalization of alkenes by vanadium chloroperoxidase from Curvularia inaequalis

J. J. Dong, E. Fernández-Fueyo, J. Li, Z. Guo, R. Renirie, R. Wever and F. Hollmann, Chem. Commun., 2017, 53, 6207 DOI: 10.1039/C7CC03368K

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