Publication Date:
2007-04-21
Description:
Iron-peroxide intermediates are central in the reaction cycle of many iron-containing biomolecules. We trapped iron(III)-(hydro)peroxo species in crystals of superoxide reductase (SOR), a nonheme mononuclear iron enzyme that scavenges superoxide radicals. X-ray diffraction data at 1.95 angstrom resolution and Raman spectra recorded in crystallo revealed iron-(hydro)peroxo intermediates with the (hydro)peroxo group bound end-on. The dynamic SOR active site promotes the formation of transient hydrogen bond networks, which presumably assist the cleavage of the iron-oxygen bond in order to release the reaction product, hydrogen peroxide.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Katona, Gergely -- Carpentier, Philippe -- Niviere, Vincent -- Amara, Patricia -- Adam, Virgile -- Ohana, Jeremy -- Tsanov, Nikolay -- Bourgeois, Dominique -- New York, N.Y. -- Science. 2007 Apr 20;316(5823):449-53.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut de Biologie Structurale (IBS) Jean-Pierre Ebel, Commissariat a l'Energie Atomique (CEA), Centre National de la Recherche Scientifique (CNRS), Universite Joseph Fourier, 41 rue Jules Horowitz, F-38027 Grenoble, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17446401" target="_blank"〉PubMed〈/a〉
Keywords:
Crystallization
;
Crystallography, X-Ray
;
Deltaproteobacteria/*enzymology
;
Ferric Compounds/chemistry/metabolism
;
Hydrogen Bonding
;
Hydrogen Peroxide/*chemistry/metabolism
;
Iron/*chemistry
;
Ligands
;
Models, Chemical
;
Models, Molecular
;
Oxidation-Reduction
;
Oxidoreductases/*chemistry/*metabolism
;
Oxygen/chemistry
;
Peroxides/*chemistry
;
Protein Conformation
;
Protons
;
Spectrum Analysis, Raman
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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