Chemoenzymatic Halogenation of Phenols by using the Haloperoxidase from Curvularia inaequalis. Issue 24 (16th October 2015)

• Record Type: Journal Article
• Authors: Fernández‐Fueyo, Elena; van Wingerden, Marco; Renirie, Rokus; Wever, Ron; Ni, Yan; Holtmann, Dirk; Hollmann, Frank
• Is Part Of: ChemCatChem. Volume 7:Issue 24(2015:Dec.)
• Page Start: 4035
• Page End: 4038
• Publication Date: 2015-10-16
• Subjects: biocatalysis -- enzymes -- halogenation -- peroxidases -- thymol; Catalysis -- Periodicals; 541.39505
• DOI: 10.1002/cctc.201500862
• Languages: English
• ISSNs: 1867-3880

Abstract

Abstract: The vanadium‐dependent chloroperoxidase from Curvularia inaequalis is an efficient biocatalyst for the in situ generation of hypohalous acids and subsequent electrophilic oxidation/halogenation reactions. Especially, its superb activity and stability under operational conditions make it an attractive catalyst for organic synthesis. Herein, the efficient bromination of thymol was investigated, and turnover numbers 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‐containing peroxidases. Abstract : It's all in the mold ! The chloroperoxidase from Curvularia inaequalis is an exceptionally efficient and stable catalyst for the in situ generation of hypohalites. Herein, the efficient bromination of thymol is reported with turnover numbers of the enzyme exceeding 2 000 000. Ci VCPO=vanadium‐dependent chloroperoxidase from Curvularia inaequalis .