Peroxygenase‐Catalyzed Oxyfunctionalization Reactions Promoted by the Complete Oxidation of Methanol |
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Authors: | Dr. Yan Ni Dr. Elena Fernández‐Fueyo Dr. Alvaro Gomez Baraibar Dr. René Ullrich Prof. Dr. Martin Hofrichter Prof. Dr. Hideshi Yanase Prof. Dr. Miguel Alcalde Prof. Dr. Willem J. H. van Berkel Dr. Frank Hollmann |
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Affiliation: | 1. Department of Biotechnology, Delft University of Technology, Julianalaan 136, 2628BL Delft (The Netherlands);2. Department of Bio‐ and Environmental Science, Technical University of Dresden—International Institute Zittau, 02763 Zittau (Germany);3. Department of Chemistry and Biotechnology, Graduate School of Engineering, Tottori University, 4–101 Koyamacho‐Minami, Tottori, Tottori 680‐8552 (Japan);4. Department of Biocatalysis, Institute of Catalysis, CSIC, 28049 Madrid (Spain);5. Laboratory of Biochemistry, Wageningen University, Dreijenlaan 3, 6703 HA Wageningen (The Netherlands) |
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Abstract: | Peroxygenases catalyze a broad range of (stereo)selective oxyfunctionalization reactions. However, to access their full catalytic potential, peroxygenases need a balanced provision of hydrogen peroxide to achieve high catalytic activity while minimizing oxidative inactivation. Herein, we report an enzymatic cascade process that employs methanol as a sacrificial electron donor for the reductive activation of molecular oxygen. Full oxidation of methanol is achieved, generating three equivalents of hydrogen peroxide that can be used completely for the stereoselective hydroxylation of ethylbenzene as a model reaction. Overall we propose and demonstrate an atom‐efficient and easily applicable alternative to established hydrogen peroxide generation methods, which enables the efficient use of peroxygenases for oxyfunctionalization reactions. |
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Keywords: | heme proteins hydrogen peroxide hydroxylation oxidation peroxygenases |
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