title: Superoxide reduction of a disulfide: a model of intracellular redox modulation?
abstract: Superoxide dismutase (SOD), which breaks down superoxide to oxygen and hydrogen peroxide, is generally considered an antioxidant enzyme. However, superoxide is a potent reducing agent and as such could affect cellular function by reducing disulfides in important proteins, such as, ionic channels and pumps. In support of this concept, we show that superoxide, generated by two different sources, is able to reduce disulfide bonds in an in vitro model. Depending on the source of superoxide this reduction is accelerated by an unsaturated fatty acid or ferric iron and is inhibited by SOD.
authors.affiliation: Department of Medicine, Minneapolis VA Medical Center, Mn.
authors.forename: D A
authors.initials: DA
authors.lastname: Peterson
authors.forename: S L
authors.initials: SL
authors.lastname: Archer
authors.forename: E K
authors.initials: EK
authors.lastname: Weir
mesh_terms: D016718:Arachidonic Acid / Q000737:chemistry; D004220:Disulfides / Q000737:chemistry; D004228:Dithionitrobenzoic Acid / Q000737:chemistry; D005290:Ferric Compounds / Q000737:chemistry; D005296:Ferrous Compounds / Q000737:chemistry; D008956:Models, Chemical; D010084:Oxidation-Reduction; D013481:Superoxides / Q000378:metabolism*
chemical_list: D004220:Disulfides; D005290:Ferric Compounds; D005296:Ferrous Compounds; D013481:Superoxides; D016718:Arachidonic Acid; D004228:Dithionitrobenzoic Acid