Journal
SCIENCE
Volume 299, Issue 5609, Pages 1037-1039Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.299.5609.1037
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Funding
- NIGMS NIH HHS [GM-38767, GM-33162, GM-22701] Funding Source: Medline
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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 [ending credence to proposed mechanisms of nonheme iron catalysis.
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