Crystallographic and spectroscopic characterization of a nonheme Fe(IV)-O complex |
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Authors: | Rohde Jan-Uwe In Jun-Hee Lim Mi Hee Brennessel William W Bukowski Michael R Stubna Audria Münck Eckard Nam Wonwoo Que Lawrence |
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Institution: | Department of Chemistry and Center for Metals in Biocatalysis, University of Minnesota, 207 Pleasant Street SE, Minneapolis, MN 55455, USA. |
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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. |
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