The superoxide reductase from the early diverging eukaryote Giardia intestinalis (Articolo in rivista)

Type
Label
  • The superoxide reductase from the early diverging eukaryote Giardia intestinalis (Articolo in rivista) (literal)
Anno
  • 2011-01-01T00:00:00+01:00 (literal)
Alternative label
  • Testa F; Mastronicola D, Cabelli DE, Bordi E, Pucillo P, Sarti P, Saraiva LM, Giuffrè A, Teixeira M. (2011)
    The superoxide reductase from the early diverging eukaryote Giardia intestinalis
    in Free radical biology & medicine
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Testa F; Mastronicola D, Cabelli DE, Bordi E, Pucillo P, Sarti P, Saraiva LM, Giuffrè A, Teixeira M. (literal)
Pagina inizio
  • 1567 (literal)
Pagina fine
  • 1574 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 51 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Department of Biochemical Sciences, CNR Institute of Molecular Biology and Pathology, and Istituto Pasteur-Fondazione Cenci Bolognetti, Sapienza Università di Roma, I-00185 Rome, Italy; Chemistry Department, Brookhaven National Laboratory, Upton, NY 11973-5000, USA; Clinical Chemistry and Microbiology Laboratory, Istituto Nazionale per le Malattie Infettive IRCCS \"Lazzaro Spallanzani,\" Rome, Italy; Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, 2780-157 Oeiras, Portugal. (literal)
Titolo
  • The superoxide reductase from the early diverging eukaryote Giardia intestinalis (literal)
Abstract
  • Unlike superoxide dismutases (SODs), superoxide reductases (SORs) eliminate superoxide anion (O2 o-) not through its dismutation, but via reduction to hydrogen peroxide (H2O2) in the presence of an electron donor. The microaerobic protist Giardia intestinalis, responsible for a common intestinal disease in humans, though lacking SOD and other canonical reactive oxygen species-detoxifying systems, is among the very few eukaryotes encoding a SOR yet identified. In this study, the recombinant SOR from Giardia (SORGi) was purified and characterized by pulse radiolysis and stopped-flow spectrophotometry. The protein, isolated in the reduced state, after oxidation by superoxide or hexachloroiridate(IV), yields a resting species (Tfinal) with Fe3+ ligated to glutamate or hydroxide depending on pH (apparent pKa=8.7). Although showing negligible SOD activity, reduced SORGi reacts with O2 o- with a pH-independent second-order rate constant k1=1.0×109 M-1 s-1 and yields the ferric-(hydro)peroxo intermediate T1; this in turn rapidly decays to the Tfinal state with pH-dependent rates, without populating other detectable intermediates. Immunoblotting assays show that SORGi is expressed in the disease-causing trophozoite of Giardia. We propose that the superoxide-scavenging activity of SOR in Giardia may promote the survival of this air-sensitive parasite in the fairly aerobic proximal human small intestine during infection. (literal)
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