2 publications

2 publications

An Artificial Imine Reductase Based on the Ribonuclease S Scaffold

Ward, T.R.

ChemCatChem 2014, 6, 736-740, 10.1002/cctc.201300995

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.


Metal: Ir
Ligand type: Amino acid; Cp*
Host protein: Ribonuclease S
Anchoring strategy: Supramolecular
Optimization: Genetic
Max TON: 4
ee: 18
PDB: ---
Notes: ---

Molecular Design of Heteroprotein Assemblies Providing a Bionanocup as a Chemical Reactor

Ueno, T.; Watanabe, Y.

Small 2008, 4, 50-54, 10.1002/smll.200700855

A bionanocup chemical reactor is constructed from a heteroprotein assembly from bacteriophage T4. The preparation of a stable iron(III) porphyrin–bionanocup composite is described. The hydrophobic cup provides a space suitable for the fixation of low‐water‐solubility iron(III) porphyrins. The application of the iron(III) porphyrin–bionanocup composites for the catalysis of sulfoxidation of thioanisoles is demonstrated (see figure).


Metal: Fe
Host protein: (gp27-gp5)3
Anchoring strategy: Cystein-maleimide
Optimization: ---
Max TON: ---
ee: ---
PDB: ---
Notes: ---