1. Chemoenzymatic halogenation of phenols by using the haloperoxidase from Curvularia inaequalis
- Author
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Elena Fernández-Fueyo, Yan Ni, Rokus Renirie, Ron Wever, Frank Hollmann, Dirk Holtmann, Marco van Wingerden, and Biocatalysis (HIMS, FNWI)
- Subjects
biology ,Organic Chemistry ,Halogenation ,Catalysis ,Inorganic Chemistry ,chemistry.chemical_compound ,chemistry ,Biocatalysis ,Haloperoxidase ,Electrophile ,biology.protein ,Organic chemistry ,Phenols ,Physical and Theoretical Chemistry ,Vanadium bromoperoxidase ,Peroxidase - 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.
- Published
- 2015