Halofunctionalization of alkenes by vanadium chloroperoxidase from Curvularia inaequalis.

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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.

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Journal

Journal ID (iso-abbrev): Chem. Commun. (Camb.)

Title: Chemical communications (Cambridge, England)

Publisher: Royal Society of Chemistry (RSC)

ISSN (Electronic): 1364-548X

ISSN (Print): 1359-7345

Publication date (Electronic): May 26 2017

Affiliations

[1 ] Department of Biotechnology, Delft University of Technology, Van der Maasweg 9, 2629 HZ Delft, The Netherlands. f.hollmann@tudelft.nl.

[2 ] Department of Engineering, Aarhus University, Gustav Wieds Vej 10, 8000 Aarhus C, Denmark.

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

Article

DOI: 10.1039/c7cc03368k

PubMed ID: 28548142

SO-VID: e0c6ac1a-2eab-49bc-8214-c090198a0bef

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Halofunctionalization of alkenes by vanadium chloroperoxidase from Curvularia inaequalis.

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Algerian Journal of Natural Products

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