000165266 001__ 165266
000165266 005__ 20251219174252.0
000165266 0247_ $$2doi$$a10.1042/BJ20041683
000165266 0248_ $$2sideral$$a56223
000165266 037__ $$aART-2005-56223
000165266 041__ $$aeng
000165266 100__ $$aIarrea, P
000165266 245__ $$aRedox Activation of Mitochondrial Intermembrane Space Cu,Zn-Superoxide Dismutase
000165266 260__ $$c2005
000165266 5203_ $$aThe localization of Cu,Zn-superoxide dismutase in the mitochondrial intermembrane space suggests a functional relationship with superoxide anion (O2*-) released into this compartment. The present study was aimed at examining the functionality of Cu,Zn-superoxide dismutase and elucidating the molecular basis for its activation in the intermembrane space. Intact rat liver mitochondria neither scavenged nor dismutated externally generated O2*-, unless the mitochondrial outer membrane was disrupted selectively by digitonin. The activation of the intermembrane space Cu,Zn-superoxide dismutase following the disruption of mitochondrial outer membrane was largely inhibited by bacitracin, an inhibitor of protein disulphide-isomerase. Thiol alkylating agents, such as N-methylmaleimide or iodoacetamide, decreased intermembrane space Cu,Zn-superoxide dismutase activation during, but not after, disruption of the outer membrane. This inhibitory effect was overcome by exposing mitochondria to low micromolar concentrations of H2O2 before disruption of the outer membrane in the presence of the alkylating agents. Moreover, H2O2 treatment alone enabled intact mitochondria to scavenge externally generated O2*-. These findings suggest that intermembrane space Cu,Zn-superoxide dismutase is inactive in intact mitochondria and that an oxidative modification of its critical thiol groups is necessary for its activation.
000165266 540__ $$9info:eu-repo/semantics/closedAccess$$aAll rights reserved$$uhttp://www.europeana.eu/rights/rr-f/
000165266 590__ $$a4.224$$b2005
000165266 591__ $$aBIOCHEMISTRY & MOLECULAR BIOLOGY$$b62 / 256 = 0.242$$c2005$$dQ1$$eT1
000165266 655_4 $$ainfo:eu-repo/semantics/article$$vinfo:eu-repo/semantics/publishedVersion
000165266 700__ $$aMoini, H
000165266 700__ $$aRettori, D
000165266 700__ $$aHan, D
000165266 700__ $$0(orcid)0000-0002-5406-3280$$aMartinez, J$$uUniversidad de Zaragoza
000165266 700__ $$aGarcia, L
000165266 700__ $$0(orcid)0000-0002-2469-142X$$aFernandez Vizarra, E
000165266 700__ $$0(orcid)0000-0003-4904-2319$$aIturralde, M$$uUniversidad de Zaragoza
000165266 700__ $$aCadenas, E.
000165266 7102_ $$11002$$2060$$aUniversidad de Zaragoza$$bDpto. Bioq.Biolog.Mol. Celular$$cÁrea Bioquímica y Biolog.Mole.
000165266 7102_ $$12003$$2395$$aUniversidad de Zaragoza$$bDpto. Física Materia Condensa.$$cÁrea Física Materia Condensada
000165266 773__ $$g387 (2005), 203-209$$pBiochem. j.$$tBiochemical Journal$$x0264-6021
000165266 8564_ $$s201658$$uhttps://zaguan.unizar.es/record/165266/files/texto_completo.pdf$$yVersión publicada
000165266 8564_ $$s3128180$$uhttps://zaguan.unizar.es/record/165266/files/texto_completo.jpg?subformat=icon$$xicon$$yVersión publicada
000165266 909CO $$ooai:zaguan.unizar.es:165266$$particulos$$pdriver
000165266 951__ $$a2025-12-19-14:44:04
000165266 980__ $$aARTICLE