Report

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

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

You are currently viewing the abstract.

View Full Text

Via your Institution

Log in through your institution

Log in through your institution


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.)

View Full Text

Related Content