An Artificial Imine Reductase based on the Ribonuclease S Scaffold

Authors

  • Maika Genz,

    1. Center for Biotechnology and Biomedicine, Institute of Bioanalytical Chemistry, University of Leipzig, Deutscher Platz 5, 04103 Leipzig (Germany)
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  • Dr. Valentin Köhler,

    1. Department of Chemistry, University of Basel, Spitalstrasse 51, CH-4056 Basel (Switzerland)
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  • Michel Krauss,

    1. Center for Biotechnology and Biomedicine, Institute of Bioanalytical Chemistry, University of Leipzig, Deutscher Platz 5, 04103 Leipzig (Germany)
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  • Dr. David Singer,

    1. Center for Biotechnology and Biomedicine, Institute of Bioanalytical Chemistry, University of Leipzig, Deutscher Platz 5, 04103 Leipzig (Germany)
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  • Prof. Ralf Hoffmann,

    1. Center for Biotechnology and Biomedicine, Institute of Bioanalytical Chemistry, University of Leipzig, Deutscher Platz 5, 04103 Leipzig (Germany)
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  • Prof. Thomas R. Ward,

    1. Department of Chemistry, University of Basel, Spitalstrasse 51, CH-4056 Basel (Switzerland)
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  • Prof. Norbert Sträter

    Corresponding author
    1. Center for Biotechnology and Biomedicine, Institute of Bioanalytical Chemistry, University of Leipzig, Deutscher Platz 5, 04103 Leipzig (Germany)
    • Center for Biotechnology and Biomedicine, Institute of Bioanalytical Chemistry, University of Leipzig, Deutscher Platz 5, 04103 Leipzig (Germany)

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Abstract

Dative anchoring of a piano-stool complex within ribonuclease S resulted in an artificial imine reductase. The catalytic performance was modulated upon variation of the coordinating amino acid residues in the S-peptide. Binding of Cp*Ir (Cp*=C5Me5) to the native active site resulted in good conversions and moderate enantiomeric excess values for the synthesis of salsolidine.

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