Aerobic alcohol oxidation and oxygen atom transfer reactions catalyzed by a nonheme iron(ii)–α-keto acid complex

α-Ketoglutarate-dependent enzymes catalyze many important biological oxidation/oxygenation reactions. Iron(iv)–oxo intermediates have been established as key oxidants in these oxidation reactions. While most reported model iron(ii)–α-keto acid complexes exhibit stoichiometric reactivity, selective oxidation of substrates with dioxygen catalyzed by biomimetic iron(ii)–α-keto acid complexes remains unexplored. In this direction, we have investigated the ability of an iron(ii) complex [(Tp(Ph,Me))Fe(II)(BF)] (1) (Tp(Ph,Me) = hydrotris(3-phenyl-5-methylpyrazolyl)borate and BF = monoanionic benzoylformate) to catalyze the aerobic oxidation of organic substrates. An iron–oxo oxidant, intercepted in the reaction of 1 with O(2), selectively oxidizes sulfides to sulfoxides, alkenes to epoxides, and alcohols to the corresponding carbonyl compounds. The oxidant from 1 is able to hydroxylate the benzylic carbon of phenylacetic acid to afford mandelic acid with the incorporation of one oxygen atom from O(2) into the product. The iron(ii)–benzoylformate complex oxidatively converts phenoxyacetic acids to the corresponding phenols, thereby mimicking the function of iron(ii)–α-ketoglutarate-dependent 2,4-dichlorophenoxyacetate dioxygenase (TfdA). Furthermore, complex 1 exhibits catalytic aerobic oxidation of alcohols and oxygen atom transfer reactions with multiple turnovers.