title: High-valent iron(IV)-oxo complexes of heme and non-heme ligands in oxygenation reactions.
abstract: High-valent iron(IV)-oxo species have been implicated as the key reactive intermediates in the catalytic cycles of dioxygen activation by heme and non-heme iron enzymes. Our understanding of the enzymatic reactions has improved greatly via investigation of spectroscopic and chemical properties of heme and non-heme iron(IV)-oxo complexes. In this Account, reactivities of synthetic iron(IV)-oxo porphyrin pi-cation radicals and mononuclear non-heme iron(IV)-oxo complexes in oxygenation reactions have been discussed as chemical models of cytochrome P450 and non-heme iron enzymes. These results demonstrate how mechanistic developments in biomimetic research can help our understanding of dioxygen activation and oxygen atom transfer reactions in nature.
authors.affiliation: Department of Chemistry, Division of Nano Sciences, and Center for Biomimetic Systems, Ewha Womans University, Seoul 120-750, Korea. wwnam@ewha.ac.kr
authors.forename: Wonwoo
authors.initials: W
authors.lastname: Nam
mesh_terms: D040761:Biomimetic Materials / Q000737:chemistry*; D003577:Cytochrome P-450 Enzyme System / Q000737:chemistry; D007501:Iron / Q000737:chemistry*; D008024:Ligands; D008958:Models, Molecular; D019159:Nonheme Iron Proteins / Q000737:chemistry*; D010084:Oxidation-Reduction; D010100:Oxygen / Q000737:chemistry / Q000378:metabolism; D010105:Oxygenases / Q000737:chemistry*; D011166:Porphyrins / Q000737:chemistry; D013379:Substrate Specificity
chemical_list: D008024:Ligands; D019159:Nonheme Iron Proteins; D011166:Porphyrins; C066317:ferryl iron; D003577:Cytochrome P-450 Enzyme System; D007501:Iron; D010105:Oxygenases; D010100:Oxygen