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Título

The crystal structure of an eukaryotic iron superoxide dismutase suggests intersubunit cooperation during catalysis

AutorMuñoz, Inés G.; Morán, José F. ; Becana Ausejo, Manuel ; Montoya Blanco, Guillermo
Palabras claveantioxidants
iron superoxide dismutase
manganese superoxide dismutase
X-ray crystallography
protein–protein interaction
Fecha de publicaciónfeb-2005
EditorJohn Wiley & Sons
CitaciónProtein Science 14(2): 387–394 (2005)
ResumenSuperoxide dismutases (SODs) are a family of metalloenzymes that catalyze the dismutation of superoxide anion radicals into molecular oxygen and hydrogen peroxide. Iron superoxide dismutases (FeSODs) are only expressed in some prokaryotes and plants. A new and highly active FeSOD with an unusual subcellular localization has recently been isolated from the plant Vigna unguiculata (cowpea). This protein functions as a homodimer and, in contrast to the other members of the SOD family, is localized to the cytosol. The crystal structure of the recombinant enzyme has been solved and the model refined to 1.97 Å resolution. The superoxide anion binding site is located in a cleft close to the dimer interface. The coordination geometry of the Fe site is a distorted trigonal bipyramidal arrangement, whose axial ligands are His43 and a solvent molecule, and whose in-plane ligands are His95, Asp195, and His199. A comparison of the structural features of cowpea FeSOD with those of homologous SODs reveals subtle differences in regard to the metal–protein interactions, and confirms the existence of two regions that may control the traffic of substrate and product: one located near the Fe binding site, and another in the dimer interface. The evolutionary conservation of reciprocal interactions of both monomers in neighboring active sites suggests possible subunit cooperation during catalysis.
DescripciónThe definitive version is available at: http://www.proteinscience.org/ http://www3.interscience.wiley.com/journal/121502357/home This article is open access through PubMed Central.
Versión del editorhttp://dx.doi.org/10.1110/ps.04979505
URIhttp://hdl.handle.net/10261/12189
DOI10.1110/ps.04979505
ISSN0961-8368
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