Abstract
A high-valent iron(IV)-oxo porphyrin radical cation (Fe(IV)(O)(porph(+•)) serves as a key, reactive intermediate for a range of heme enzymes, including cytochrome P450 (CYP), horseradish peroxidase (HRP), and catalase (CAT). Synthetic analogs of this intermediate, known as Compound-I (Cpd-I) in the heme enzyme literature, have been generated with different tetrapyrrolic, macrocyclic ligands, including porphyrin derivatives, and the closely related ring-contracted macrocycles, corroles and corrolazines. These synthetic analogs have been useful for assigning and understanding structural and spectroscopic features and examining the reactivity of Cpd-I-like species in controlled and well-defined environments. This review focuses on summarizing recent developments in the synthesis and reactivity of high-valent iron-oxo porphyrinoid complexes in two main classes of reactions, proton-coupled electron transfer (PCET) and oxygen atom transfer (OAT). The relationship between the structure of the complexes and their reactivity is emphasized, including the influence of axial ligation and peripheral macrocyclic substitution, as well as the effects of solvent and secondary coordination spheres on the reactivity of the Cpd-I analogs. In bringing together the latest findings on Cpd-I analogs, this review intends to broaden our current understanding of the factors that control the stability and reactivity of Cpd-I species. This new knowledge should, in turn, point toward new synthetic strategies for constructing catalysts that rely on Cpd-I-like reactive intermediates.