Crystal Structures of Fe2+ Dioxygenase Superoxo, Alkylperoxo, and Bound Product Intermediates.
From: Department of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, Minneapolis, MN 55455, USA.
Science (New York, N.Y.)
- Publish Date: Apr 2007
- ISSN: 1095-9203
- Volume: 316
- Issue: 5823
- Pages: 453-7
- Medium: Internet
- Language: English
- Citation (JAMA): Kovaleva Elena G, Lipscomb John D, et al. Crystal Structures of Fe2+ Dioxygenase Superoxo, Alkylperoxo, and Bound Product Intermediates.. Science Apr 2007;316:453-7
Abstract
We report the structures of three intermediates in the O2 activation and insertion reactions of an extradiol ring-cleaving dioxygenase. A crystal of Fe2+-containing homoprotocatechuate 2,3-dioxygenase was soaked in the slow substrate 4-nitrocatechol in a low O2 atmosphere. The x-ray crystal structure shows that three different intermediates reside in different subunits of a single homotetrameric enzyme molecule. One of these is the key substrate-alkylperoxo-Fe2+ intermediate, which has been predicted, but not structurally characterized, in an oxygenase. The intermediates define the major chemical steps of the dioxygenase mechanism and point to a general mechanistic strategy for the diverse 2-His-1-carboxylate enzyme family.
Mesh Headings (Keywords): Binding Sites, Brevibacterium, Catalysis, Catechols, Crystallization, Crystallography, X-Ray, Dioxygenases, Ferric Compounds, Ferrous Compounds, Ligands, Models, Chemical, Models, Molecular, Oxygen, Protein Conformation, Protein Subunits, Superoxides
Check for Full Text / PubMed Unique Identifier (PMID): 17446402
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