CYCLOHEXANONE OXYGENASE: STEREOCHEMISTRY, ENANTIOSELECTIVITY, AND REGIOSELECTIVITY OF AN ENZYME-CATALYZED BAEYER-VILLIGER REACTION.

Article abstract of DOI:10.1021/ja00352a044

Cyclohexane oxygenase, from Acinetobacter NCIB 9871, has been incubated with (2S,6S)- left bracket 2,6-**2H//2 right bracket - and (2R)- left bracket 2-**2H//1 right bracket cyclohexanone. The resulting labeled epsilon -caprolactone (2-oxepanone) samples were degraded to 1-pentanol, which was esterified by using ( minus )-camphanyl chloride. Analysis of the camphanates by deuterium NMR spectroscopy, using Eu(dpm)//3, showed that the conversion of ketone to lactone had in each case proceeded with complete retention of configuration at the migrating carbon center. A similar degradation of (2R)- left bracket 2-**2H//1 right bracket cyclohexanone itself showed that reduction of left bracket 2-**2H//1 right bracket -cyclohex-2-enone by Beauveria bassiana ATCC 7159 is also completely stereoselective. A method has been developed for assessing the enantioselectivity of enzymes toward racemic substrate mixtures.