MODEL COMPOUND STUDIES RELATED TO PEROXIDASES-II THE CHEMICAL REACTIVITY OF A HIGH VALENT PROTOHEMIN COMPOUND

Article abstract of DOI:10.1016/0040-4020(84)85061-9

The chemical reactivity of the model analog to compound I of the peroxidases resulting from the reaction of "chelated protohemin" and m-chloroperbenzoic acid is examined.The model intermediate shows no H-atom abstraction or O insertion activity and substrate reactivity depends only on the E_1/2 value of the substrate.A Marcus theory treatment of the available kinetic data for HRP suggests that the oxidative pathway for substrate oxidations is an outer-sphere electron transfer.From the results of the model catalyzed oxidation of 1,4-cyclohexadiene to benzene, an alternate mechanism for cytochrome P-450 catalyzed hydroxylations is suggested.