Mononuclear nonheme iron enzymes catalyze a wide variety of reactions in nature, from C-H bond activation to oxygen insertion. All contain the same active site of an iron bound by the 2-His-1-carboxylate facial triad. An iron(IV)-oxo species has been proposed to be the active intermediate in many of these enzymes. Synthetic model complexes elucidate possible reaction mechanisms and facilitate systematic variance in ligand environment. [Fe(IV)(O)(TMC)(NCMe)]2+ (TMC = Tetramethylcyclam) has been used as a model of the iron(IV)-oxo reactive intermediate with the added advantage of having a labile site trans to the oxo group, where reactivity based on electronics was tested through anion substitution. Based on this electronic tuning, a series of Fe(IV)(O)(TMC) complexes has been synthesized with carboxylates, a more enzymatically relevant ligand, trans to the oxo. This variability in the trans ligand helps tune the reactivity of the oxoiron(IV) toward C�H bond cleavage, oxygen transfer, and electron transfer.

Effects of trans ligands on the reactivity of synthetic nonheme iron enzyme model complexes

245th National Meeting (2013)

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