Abstract
The kinetic resolution of racemic hydroperoxides by horseradish peroxidase (HRP)-catalyzed reduction was investigated, with major emphasis on catalytic efficiency and enantioselectivity. The kinetic parameters of the enzymatic reaction were determined, enantiomeric excess (ee) and absolute configurations of hydroperoxides and alcohols were measured, and a broad spectrum of structurally different hydroperoxides were investigated to assess the scope and limitation of this method. Both the catalytic efficiency and the stereoselectivity of HRP highly depend on the structure of the hydroperoxides. The enzyme selectively recognizes sterically unencumbered hydroperoxides, which allows kinetic resolution by means of enantioselective reduction to yield optically active hydroperoxides and alcohols in excellent ee values (up to 99%). Functional groups in the hydroperoxide molecule do not affect the stereoselectivity of the enzyme, which permits a large number of functionalized hydroperoxides to be resolved by HRP.
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