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

Abstract

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 (MO1). The absolute stereochemistry of the lactone 7 was determined by a single-crystal X-ray diffraction structure determination of the (1R′)-α-methylbenzylamide benzoate derivative 11b. Baeyer–Villiger reactions (and Baeyer–Villigerases) are classified by the stereochemistry of the active site and the hydroxy peroxide intermediates.