A systematic study of the stereochemistry of oxidation at sulfur catalyzed by cyclohexanone monooxygenase from Acinetobacter using as the substrates numerous alkyl aryl sulfides, dialkyl sulfides and dialkyl disulfides has been carried out. It was found that the structure of the sulfide dramatically influenced the enantioselectivity of the enzyme which yielded sulfoxides with optical purities ranging from 99% ee and R-configuration to 93% ee and S-configuration.
Effects of substrate structure on the enantioselectivity and stereochemical course of sulfoxidation catalyzed by cyclohexanone monooxygenase / G. Carrea, B. Redigolo, S. Riva, S. Colonna, N. Gaggero, E. Battistel, D. Bianchi. - In: TETRAHEDRON-ASYMMETRY. - ISSN 0957-4166. - 3:8(1992), pp. 1063-1068. [10.1016/S0957-4166(00)86040-1]
Effects of substrate structure on the enantioselectivity and stereochemical course of sulfoxidation catalyzed by cyclohexanone monooxygenase
S. Colonna;N. Gaggero;
1992
Abstract
A systematic study of the stereochemistry of oxidation at sulfur catalyzed by cyclohexanone monooxygenase from Acinetobacter using as the substrates numerous alkyl aryl sulfides, dialkyl sulfides and dialkyl disulfides has been carried out. It was found that the structure of the sulfide dramatically influenced the enantioselectivity of the enzyme which yielded sulfoxides with optical purities ranging from 99% ee and R-configuration to 93% ee and S-configuration.Pubblicazioni consigliate
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