BIOMIMETIC OXIDATION STUDIES .10. CYCLOHEXANE OXIDATION REACTIONS WITH ACTIVE-SITE METHANE MONOOXYGENASE ENZYME MODELS AND T-BUTYL HYDROPEROXIDE IN AQUEOUS MICELLES - MECHANISTIC INSIGHTS AND THE ROLE OF T-BUTOXY RADICALS IN THE C-H FUNCTIONALIZATION REACTION

The oxidation of cyclohexane (CyH) in an aqueous micelle system with t -butyl hydroperoxide (TBHP) in the presence of biomimetic methane mono oxygenase enzyme complexes, [Fe2O(eta(1)-H2O)(eta(1)-OAc)(TPA)(2)](3+) , 1, [Fe2O(eta(1)-H2O)(eta(1)-OAc)(BPIA)(2)](3+), 2, and O-2, was stud ied and found to provide cyclohexanol (CyOH), cyclohexanone (CyONE), a nd cyclohexyl-t-butyl peroxide (CyOOt-Bu). The mechanistic aspects of this oxidation reaction in aqueous micelles were studied and included the effects of the surfactant concentration, cetyltrimethylammonium hy drosulfate; concentration of CyH and TBHP; and a trapping reagent, CCl 4. Several factors allowed us to conclude that a t-butoxy radical (t-B uO(.)) was generated from the favorable redox chemistry of the biomime tic complexes with TBHP, and was responsible for the free radical init iation process with CyH in the aqueous micelle system.