Biological oxidation reactions are often catalyzed by metalloenzymes via high-valent iron centers generated by dioxygen activation. Key nonheme iron examples are the mononuclear oxoiron(IV) oxidants associated with TauD and related oxygenases and halogenases and the FeIV2O2 diamond core found for intermediate Q of soluble methane monooxygenase. In both types, the high-valent iron center has an S = 2 ground spin state. Our recent efforts have led to the generation of S = 2 FeIV=O species that exhibit high rates of cyclohexane oxidation that are comparable to those associated with enzymatic FeIV=O intermediates. Extension of this effort to modeling the corresponding nonheme iron halogenases has resulted in the generation and spectroscopic characterization of [FeIV(O)(L)(Cl/Br)] complexes. These complexes can halogenate hydrocarbon substrates, and both oxygenated and halogenated products are observed, thereby shedding light on the factors that control the relative rates of oxygen and halogen rebound.

Amazing nonheme high-valent iron-oxo reactivity landscape

251st National Meeting (2016)

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.