Issue 46, 2017
From the journal:

Chemical Communications

Halofunctionalization of alkenes by vanadium chloroperoxidase from Curvularia inaequalis†

Jia Jia Dong,‡a   Elena Fernández-Fueyo,‡a   Jingbo Li, ORCID logo b   Zheng Guo,b   Rokus Renirie,c   Ron Weverc  and  Frank Hollmann ORCID logo *a  

* Corresponding authors

a Department of Biotechnology, Delft University of Technology, Van der Maasweg 9, 2629 HZ Delft, The Netherlands
E-mail: f.hollmann@tudelft.nl
Tel: +31 (0)152 781957

b Department of Engineering, Aarhus University, Gustav Wieds Vej 10, 8000 Aarhus C, Denmark

c Van't Hoff Institute for Molecular Sciences (HIMS), Faculty of Science, University of Amsterdam, Science Park 904, 1098 XH Amsterdam, The Netherlands

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

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Article information

DOI
https://doi.org/10.1039/C7CC03368K
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

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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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