Crystallographic and Spectroscopic Characterization of a Nonheme Fe(IV)=O Complex

2003/02/13 by Jan‐Uwe Rohde, Jun-Hee In, Mi Hee Lim +6 · 6 citations
Biochemistry, Genetics and Molecular Biology · Chemistry · Materials Science · #Hemoglobin structure and function #Metal-Catalyzed Oxygenation Mechanisms #Porphyrin and Phthalocyanine Chemistry

paper · doi:10.1126/science.299.5609.1037

openalex publication_date 2003/02/13 · openalex created_date 2025/10/10 · openalex updated_date 2026/08/01

Abstract

Following the heme paradigm, it is often proposed that dioxygen activation by nonheme monoiron enzymes involves an iron(IV)=oxo intermediate that is responsible for the substrate oxidation step. Such a transient species has now been obtained from a synthetic complex with a nonheme macrocyclic ligand and characterized spectroscopically. Its high-resolution crystal structure reveals an iron-oxygen bond length of 1.646(3) angstroms, demonstrating that a terminal iron(IV)=oxo unit can exist in a nonporphyrin ligand environment and lending credence to proposed mechanisms of nonheme iron catalysis.

Citations

• Structure of dipotassium ferrate(VI)

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• Transition Metal Complexes and the Activation of Dioxygen
• High-Valent Iron(IV)–Oxo Complexes of Heme and Non-Heme Ligands in Oxygenation Reactions
• High-valent iron [wikipedia]