Oxidation of Sulfide, Phosphine, and Benzyl Substrates Tethered to N-Donor Pyridine Ligands in Carboxylate-Bridged Diiron(II) Complexes

摘要

Bacterial multicomponent monooxygenases, including soluble methane monooxygenase (sMMO) and toluene/o-xylene monooxygenase (ToMO), catalyze the selective conversion of hydrocarbons to alcohols and can oxidize other substrates including methane derivatives, olefins, amines, and sulfides. A carboxylate-bridged non-heme diiron active site, housed in the hydroxylase components (MMOH; ToMOH) of sMMO and ToMO, is responsible for the binding and reductive activation of dioxygen in the enzymes. A goal of many laboratories is to create functional models of these diiron centers to provide insight into the mechanisms of their oxidation chemistry.