HORSERADISH-PEROXIDASE - A BIOCATALYST FOR THE ONE-POT SYNTHESIS OF ENANTIOMERICALLY PURE HYDROPEROXIDES AND ALCOHOLS

The kinetic resolution of racemic hydroperoxides by horseradish peroxi dase (HRP)-catalyzed reduction was investigated, with major emphasis o n catalytic efficiency and enantioselectivity. The kinetic parameters of the enzymatic reaction were determined, enantiomeric excess (ee) an d absolute configurations of hydroperoxides and alcohols were measured , and a broad spectrum of structurally different hydroperoxides were i nvestigated to assess the scope and limitation of this method. Both th e catalytic efficiency and the stereoselectivity of HRP highly depend on the structure of the hydroperoxides. The enzyme selectively recogni zes sterically unencumbered hydroperoxides, which allows kinetic resol ution by means of enantioselective reduction to yield optically active hydroperoxides and alcohols in excellent ee values (up to 99%). Funct ional groups in the hydroperoxide molecule do not affect the stereosel ectivity of the enzyme, which permits a large number of functionalized hydroperoxides to be resolved by HRP.