Molecular identification of the enzyme responsible for the mitochondrial NADH-supported ammonium-dependent hydrogen peroxide production |
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| Authors: | Kareyeva Alexandra V Grivennikova Vera G Cecchini Gary Vinogradov Andrei D |
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| Affiliation: | aDepartment of Biochemistry, School of Biology, Moscow State University, Moscow 119991, Russian Federation;bMolecular Biology Division, VA Medical Center, 4150 Clement Street, San Francisco, CA 94121, USA;cDepartment of Biochemistry and Biophysics, University of California, San Francisco, CA 94158, USA;dInstitute of Mitoengineering of Moscow State University, Moscow 119991, Russian Federation |
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| 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 H2O2 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. |
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| Keywords: | Hydrogen peroxide Ammonium Reactive oxygen species Dihydrolipoyl dehydrogenase Mitochondria |
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