Mechanism of catalyst activation in iron(porphyrin)-catalysed aerobic oxidative cleavage of 2,3-dimethylindole

Abstract

Ferric porphyrins catalyse the aerobic oxidative cleavage of 2,3-dimethylindole, mimicking dioxygenase enzymes. The data herein suggest that the indole reduces the Fe^III(porphyrin) to Fe^II(porphyrin) via a proton-coupled electron transfer mechanism. Subsequently, Fe^II(porphyrin) binds O₂ and generates the critical superoxo intermediate, which oxidatively cleaves a second equivalent of substrate.