1 publication

1 publication

Improving the Enantioselectivity of Artificial Transfer Hydrogenases Based on the Biotin–Streptavidin Technology by Combinations of Point Mutations

Ward, T.R.

Inorg. Chim. Acta 2010, 363, 601-604, 10.1016/j.ica.2009.02.001

Artificial metalloenzymes based on the incorporation of biotinylated ruthenium piano–stool complexes within streptavidin can be readily optimized by chemical or genetic means. We performed genetic modifications of such artificial metalloenzymes for the transfer hydrogenation of aromatic ketones, by combining targeted point mutations of the host protein. Upon using the P64G-L124V double mutant of streptavidin in combination with the [η6-(p-cymene)Ru(Biot-p-L)Cl] complex, the enantioselectivity can be increased up to 98% ee (R) for the reduction of p-methylacetophenone, which is the highest selectivity obtained up to date with an artificial transfer hydrogenase.


Metal: Ru
Ligand type: Amino-sulfonamide; P-cymene
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Chemical & genetic
Max TON: 98
ee: 98
PDB: ---
Notes: ---

Metal: Ru
Ligand type: Amino-sulfonamide; Benzene
Host protein: Streptavidin (Sav)
Anchoring strategy: Supramolecular
Optimization: Chemical & genetic
Max TON: 24
ee: 84
PDB: 2QCB
Notes: ---