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Chemoenzymatic Reduction of Conjugated C[DOUBLE BOND]C Double Bonds

Authors

  • Julie Bernard,

    1. Department of Biotechnology, Delft University of Technology, 2628BL Delft (The Netherlands), Fax: (+31) 2781415
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  • Prof. Dr. Esta van Heerden,

    1. University of the Free State, Department of Biotechnology, 9300 Bloemfontein (South Africa)
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  • Prof. Dr. Isabel W. C. E. Arends,

    1. Department of Biotechnology, Delft University of Technology, 2628BL Delft (The Netherlands), Fax: (+31) 2781415
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  • Dr. Diederik J. Opperman,

    Corresponding author
    1. University of the Free State, Department of Biotechnology, 9300 Bloemfontein (South Africa)
    • Diederik J. Opperman, University of the Free State, Department of Biotechnology, 9300 Bloemfontein (South Africa)

      Frank Hollmann, Department of Biotechnology, Delft University of Technology, 2628BL Delft (The Netherlands), Fax: (+31) 2781415

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  • Dr. Frank Hollmann

    Corresponding author
    1. Department of Biotechnology, Delft University of Technology, 2628BL Delft (The Netherlands), Fax: (+31) 2781415
    • Diederik J. Opperman, University of the Free State, Department of Biotechnology, 9300 Bloemfontein (South Africa)

      Frank Hollmann, Department of Biotechnology, Delft University of Technology, 2628BL Delft (The Netherlands), Fax: (+31) 2781415

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Abstract

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An addiction to rhodium: A nicotinamide-independent regeneration approach for enoate reductases is proposed. The transition metal complex [Cp*Rh(bpy)(H2O)]2+ can replace both the nicotinamide cofactor and a corresponding enzymatic regeneration system, which results in a simplified reaction system. This system is characterized and applied to the chemoenzymatic reduction of various conjugated C[DOUBLE BOND]C double bonds.

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