MODEL FOR THE FUNCTIONAL ACTIVE-SITE OF BAEYER-VILLIGERASES - X-RAY CRYSTAL DATA FOR (1S,2R,5R,8S,1'R)-8-ENDO-BENZOYLOXY-N-(1'-PHENYLETHYL)BICYCLO[3.3.0]OCTANE-2-ENDO-CARBOXAMIDE

An active-site model for enzyme-catalysed Baeyer-Villiger reactions is proposed and tested by transformation of the tricyclic ketone 6 to the lactone 7 (> 98% ee) using purified enzymes from Acinetobacter sp. NCIMB 9871 and Pseudomonas putida NCIMB 10 007 (M01). The absolute stereochemistry of the lactone 7 was determined by a single-crystal X-ray diffraction structure determination of the (1R')-alpha-methylbenzylamide benzoate derivative 11b. Baeyer-Villiger reactions (and Baeyer-Villigerases) are classified by the stereochemistry of the active site and the hydroxy peroxide intermediates.