This presentation will focus on our recent results with iron and manganese complexes prepared from a highly sterically encumbered corrole ligand (tris(triphenyl)phenyl corrole, ttppcH<sub>3</sub>). The ligand environment stabilizes high-valent metal-oxo and metal-hydroxo species that serve as models for key intermediates in heme monooxygenases and related enzymes, and allows us to access and study reactions of fundamental importance to the mechanism of both heme enzymes and synthetic oxidation catalysts. Results regarding H-atom transfer (or PCET) reactivity will be described, including the finding that the lower-valent M(OH) complex can be a relatively potent H-atom abstractor compared to its higher-valent M(O) partner in certain cases. Access to the rare terminal hydroxide complexes have allowed us to study radical recombination reactions to give new C-X bonds, in direct relationship with the heme “rebound” mechanism proposed for oxygenases such as Cytochrome P450. These studies provide new, fundamental insights regarding the mechanism of HAT/PCET and rebound pathways with isolable, structurally well-defined model complexes.

Metal-oxo and metal-hydroxo (Fe, Mn) corrole model complexes: Insights regarding H-atom abstraction and radical rebound processes

ACS Spring Meeting 2021

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