190506-76-4Relevant academic research and scientific papers
Asymmetric synthesis with the enzyme Coprinus peroxidase: Kinetic resolution of chiral hydroperoxides and enantioselective sulfoxidation
Adam, Waldemar,Mock-Knoblauch, Cordula,Saha-Moeller, Chantu R.
, p. 4834 - 4839 (2007/10/03)
The enzyme Coprinus peroxidase (CiP) was employed for the kinetic resolution of racemic hydroperoxides 1 and the asymmetric sulfoxidation of prochiral sulfides 4. Eleven hydroperoxides 1a-k were reduced by CiP and guaiacol as reductant under conditions of kinetic resolution with enantioselectivities of up to >98% for the (S)-hydroperoxide 1 and 90% for the (R)-alcohol 2. In the absence of a reductant, the hydroperoxide 1a afforded with CiP enantiomerically enriched hydroperoxide la (ee up to 54%) and alcohol 2a (ee up to 40%), as well as ketone 3a (which is also formed simultaneously in all other reactions) and molecular oxygen. Catalase activity was established for CiP with hydrogen peroxide. When aryl alkyl sulfides 4 were used as oxygen acceptors, three products, sulfoxides 5, alcohols 2, and hydroperoxides 1, were obtained, all in enantiomerically enriched form. The highest ee value (89%) was achieved for the sulfoxide derived from naphthyl methyl sulfide (4f). Thus, CiP may be utilized for the asymmetric synthesis of optically active hydroperoxides 1, alcohols 2, and sulfoxides 5.
