The ee values of lactone 3, and not of lactone 2, obtained from the enantiodivergent oxidation of racemic bicyclo[3.2.0]hept-2-en-6-one 1, catalyzed by cyclohexanone monooxygenase from Acinetobacter calcoaceticus, were found to be markedly dependent on the degree of conversion and substrate concentration. The results are rationalized on the basis of a model which hypothesizes the binding of a second substrate molecule to an enzyme site distinct from the catalytic site.
Effect of substrate concentration on the enantioselectivity of cyclohexanone monooxygenase from Acinetobacter calcoaceticus and its rationalization / F. Zambianchi, P. Pasta, G. Ottolina, G. Carrea, S. Colonna, N. Gaggero, J. M. Ward. - In: TETRAHEDRON-ASYMMETRY. - ISSN 0957-4166. - 11:18(2000), pp. 3653-3657. [10.1016/S0957-4166(00)00354-2]
Effect of substrate concentration on the enantioselectivity of cyclohexanone monooxygenase from Acinetobacter calcoaceticus and its rationalization
S. Colonna;N. GaggeroPenultimo
;
2000
Abstract
The ee values of lactone 3, and not of lactone 2, obtained from the enantiodivergent oxidation of racemic bicyclo[3.2.0]hept-2-en-6-one 1, catalyzed by cyclohexanone monooxygenase from Acinetobacter calcoaceticus, were found to be markedly dependent on the degree of conversion and substrate concentration. The results are rationalized on the basis of a model which hypothesizes the binding of a second substrate molecule to an enzyme site distinct from the catalytic site.
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