Enantiocomplementary preparation of ( S)- and ( R)-1-pyridylalkanols via ketone reduction and alkane hydroxylation using whole cells of Pseudomonas putida UV4

Abstract

A previously unreported alcohol dehydrogenase enzyme in the mutant soil bacterium Pseudomonas putida UV4 catalyses the reduction of 2-, 3- and 4-acylpyridines to afford the corresponding ( S)-1-pyridyl alkanols, with moderate to high e.e., whilst under the same conditions 2,6-diacetylpyridine is readily converted to the corresponding enantiopure C 2-symmetric ( S, S)-diol in one step. In contrast, the toluene dioxygenase enzyme in the same organism catalyses the hydroxylation of 2- and 3-alkylpyridines to ( R)-1-(2-pyridyl) and ( R)-1-(3-pyridyl)alkanols. This combination of oxidative and reductive biotransformations thus provides a method for preparing both enantiomers of chiral 1-pyridyl alkanols using one biocatalyst.