摘要
Dative anchoring of a piano-stool complex within ribonucleaseS 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.
- 出版日期2014-3