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

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Science  14 Feb 2003:
Vol. 299, Issue 5609, pp. 1037-1039
DOI: 10.1126/science.299.5609.1037

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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.

  • * These authors contributed equally to this work.

  • To whom correspondence should be addressed. E-mail: emunck{at}cmu.edu (E.M.); wwnam{at}ewha.ac.kr (W.N.); que{at}chem.umn.edu (L.Q.)

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