2007/05/01 by Wonwoo Nam · 1 citation
Chemistry · Biochemistry, Genetics and Molecular Biology · Materials Science · #Metal-Catalyzed Oxygenation Mechanisms #Heme Oxygenase-1 and Carbon Monoxide #Porphyrin and Phthalocyanine Chemistry
paper · doi:10.1021/ar700027f
openalex publication_date 2007/05/01 · openalex created_date 2025/10/10 · openalex updated_date 2026/07/30
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.