Chemoenzymatic halogenation of phenols by using the haloperoxidase from Curvularia inaequalis

Authors
  • Y. Ni
  • D. Holtmann
  • F. Hollmann
Publication date 2015
Journal ChemCatChem
Volume | Issue number 7 | 24
Pages (from-to) 4035-4038
Organisations
  • Faculty of Science (FNWI) - Van 't Hoff Institute for Molecular Sciences (HIMS)
Abstract
The vanadium-​dependent chloroperoxidase from Curvularia inaequalis is an efficient biocatalyst for the in situ generation of hypohalous acids and subsequent electrophilic oxidn.​/halogenation reactions. Esp., its superb activity and stability under operational conditions make it an attractive catalyst for org. synthesis. Herein, the efficient bromination of thymol was investigated, and turnover nos. of the enzyme were found to exceed 2 000 000. The major novelty of the work is that vanadium chloroperoxidase is more useful as a brominating enzyme than vanadium bromoperoxidase in terms of operational stability, besides being far more stable than heme-​contg. peroxidases.
Document type Article
Note With supporting information
Language English
Published at https://doi.org/10.1002/cctc.201500862
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