title: Molecular identification of the enzyme responsible for the mitochondrial NADH-supported ammonium-dependent hydrogen peroxide production.
abstract: A homogeneous protein with a subunit apparent molecular mass of ∼50 kDa that catalyzes the previously described mitochondrial NADH-supported ammonium-stimulated hydrogen peroxide production (Grivennikova, V.G., Gecchini, G. and Vinogradov, A.D. (2008) FEBS Lett. 583, 1287-1291) was purified from the mitochondrial matrix of bovine heart. Chromatography of partially purified protein showed that the peaks of ammonium-stimulated NADH-dependent H(2)O(2) production and that of NADH:lipoamide oxidoreductase activity coincided. The catalytic properties and mass spectrometry of the trypsin-digested protein revealed peptides that allowed identification of the protein as the Bos taurus dihydrolipoyl dehydrogenase.
authors.affiliation: Department of Biochemistry, School of Biology, Moscow State University, Moscow, Russian Federation.
authors.forename: Alexandra V
authors.initials: AV
authors.lastname: Kareyeva
authors.forename: Vera G
authors.initials: VG
authors.lastname: Grivennikova
authors.forename: Gary
authors.initials: G
authors.lastname: Cecchini
authors.forename: Andrei D
authors.initials: AD
authors.lastname: Vinogradov
mesh_terms: D000818:Animals; D002384:Catalysis; D002417:Cattle; D008058:Dihydrolipoamide Dehydrogenase / Q000302:isolation & purification* / Q000378:metabolism; D006861:Hydrogen Peroxide / Q000378:metabolism*; D013058:Mass Spectrometry; D008929:Mitochondria, Heart / Q000201:enzymology*; D009243:NAD; D000644:Quaternary Ammonium Compounds
chemical_list: D000644:Quaternary Ammonium Compounds; D009243:NAD; D006861:Hydrogen Peroxide; D008058:Dihydrolipoamide Dehydrogenase