Crystallographic and spectroscopic characterization of a Nonheme Fe(IV)=O complex

Jan Uwe Rohde, Jun Hee In, Mi Hee Lim, William W. Brennessel, Michael R. Bukowski, Audria Stubna, Eckard Münck, Wonwoo Nam, Lawrence Que

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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.

Original languageEnglish
Pages (from-to)1037-1039
Number of pages3
Issue number5609
StatePublished - 14 Feb 2003


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