Semisynthetic enzymes in asymmetric synthesis: Enantioselective reduction of racemic hydroperoxides catalyzed by seleno-subtilisin

The serine protease subtilisin was chemically converted into the peroxidase -active seleno-subtilisin. This semisynthetic enzyme catalyzes the enantios elective reduction of racemic hydroperoxides in the presence of thiophenols to yield optically active hydroperoxides and alcohols on the semipreparati ve scale. The kinetic parameters and enantioselectivities of seleno-subtili sin-catalyzed reduction of various chiral hydroperoxides were determined. T he catalytic efficiency of this semisynthetic enzyme is comparable to that of the native horseradish peroxidase. The sense in the enantioselectivity o f the seleno-subtilisin is opposite to the natural enzymes previously used in the synthesis of optically active hydroperoxides. Consequently, the semi synthetic enzyme selenosubtilisin complements the naturally available perox idases for the asymmetric synthesis of both enantiomers.