FUNCTIONAL GROUP DIVERSITY IN ENZYMATIC OXYGENATION REACTIONS CATALYZED BY BACTERIAL FLAVIN-CONTAINING CYCLOHEXANONE OXYGENASE

Article abstract of DOI:10.1021/ja00293a054

The bacterial flavoprotein monooxygenase cyclohexanone oxygenase was found by spectrophotometric NADPH consumption assays and product analysis to perform oxygenation reaction on ketones, aldehydes, sulfides, selenides, boronic acids, a phophite ester, and an iodide ion.Kinetic parameters (K_m, V_max) are reported for these substrates.The relevance of these results to possible active oxygen-transfer species in this enzyme is discussed.The potential utility of boronic acids as general probes for nucleophilic oxygen-transfer capability in oxygenases and in model chemistry is analyzed.The potential utility of cyclohexanone oxygenase as a n enantioselective and/or chemoselective oxidant for organic molecules is assessed.Unsuccessful attempts at exploiting the 2,3-sigmatropic rearrangement of allyl sulfoxides and allyl selen oxides for mechanism-based inactivation of cyclohexanone oxygenase are reported.The use of the facile 2,3-sigmatropic rearrengement of allyl selenoxides to generate electrophilic allyl selenates for the design of mechanism-based inactivators for other enzymes is proposed.