Ruthenium- and Enzyme-Catalyzed Dynamic Kinetic Resolution of Secondary Alcohols
Journal of the American Chemical Society1999Vol. 121(8), pp. 1645–1650
Citations Over TimeTop 10% of 1999 papers
Abstract
Enzymatic resolution of secondary alcohols under substrate racemizing conditions was studied using an immobilized lipase from Candida antarctica in the presence of a ruthenium catalyst. A specifically designed acyl donor, 4-chlorophenyl acetate, was found to be compatible with both catalysts and resulted in an efficient dynamic kinetic resolution. Studies of the reaction in different solvents showed that nonpolar solvents gave the best results. With this process, a variety of racemic secondary alcohols were transformed to the corresponding enantiomerically pure acetates, making efficient use of all starting material. In most cases, the reaction proceeded with >99% ee and in good yield.
Related Papers
- → Extractive Separation and Spectrophotometric Determination of Traces of Ruthenium from Mixtures Containing Excess Platinum Group Metals(2009)7 cited
- → Ligand control of metal oxidation states. Synthesis, characterization and cyclic voltammetric studies of a group of ruthenium phenolates(1996)18 cited
- THE FEATURES OF PROTEIN BINDING BY RUTHENIUM COMPLEXES: DOCKING, FORCE FIELD AND QM/MM STUDIES(2013)
- → Phosphorogenic and spontaneous formation of tris(bipyridine)ruthenium in peptide scaffolds(2019)1 cited
- → ChemInform Abstract: Synthesis, Reactivities, and Structural Studies on High‐Valent Ruthenium Oxo Complexes. Ruthenium(IV), Ruthenium(V), and Ruthenium(VI) Oxo Complexes of Tertiary Amine Ligands.(1987)