Enzymatic kinetic resolution of chiral sulfoxides-an enantiocomplementary approach
A new enzymatic assay for the preparation of chiral sulfoxides that is enantiocomplementary to the known (S)-enantiomer-reducing activity of methionine sulfoxide reductase A (MsrA) is described. To this end, we have utilized the enzyme DMSO reductase (DmsABC), recently discovered by us being highly upregulated in stationary phase E. coli bacteria.
Enantioselective Pummerer-type rearrangement by reaction of O-silylated ketene acetal with enantiopure α-substituted sulfoxides
Chiral non-racemic α-substituted sulfoxides have been allowed to react with O-silylated ketene acetals in the presence of a catalytic amount of ZnI2 in THF to give chiral non-racemic α-siloxy sulfides in >99% ee. This is the highest enantioselectivity reported to date for the Pummerer reaction.