Dioxygenase enzymes are able to catalyze the hydroxylation of strong C-H bonds through high valent iron oxo species derived from O2. The primary sphere within dioxygenase enzymes have been modeled with heme and non-heme model systems, but little is known about the role of the secondary sphere in these systems. Expansive hydrogen bonding networks support enzymatic active sites and facilitate chemical transformations, but the underlying roles of outer-sphere acidic groups on enzymatic reactivity needs further study. Our lab has been working to develop fundamental structure-function relationships between substrate activation and secondary sphere groups by using appended Brønsted and/or Lewis acids. This talk will present our recent efforts on the characterization and reactivity of an O2 derived high valent iron center supported by a tris(pyridylmethyl)amine (TPA) ligand bearing three appended hydrogen bonding groups in the secondary sphere. We will describe the preferences of this high valent species to undergo H-atom transfer (HAT) or oxygen atom transfer (OAT) events and will compare rates of reaction to previously characterized high valent TPA-based iron systems.

Characterization and reactivity of an O2 derived high-valent non-heme iron species with hydrogen bonds in the outer sphere

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ACS Fall 2022

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