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Molecular identification of the enzyme responsible for the mitochondrial NADH‐supported ammonium‐dependent hydrogen peroxide production
Author(s) -
Kareyeva Alexandra V.,
Grivennikova Vera G.,
Cecchini Gary,
Vinogradov Andrei D.
Publication year - 2011
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2010.12.019
Subject(s) - biochemistry , chemistry , hydrogen peroxide , molecular mass , dihydrolipoamide dehydrogenase , mitochondrial matrix , enzyme , oxidoreductase , protein subunit , trypsin , ammonium , nadh dehydrogenase , dehydrogenase , cytosol , organic chemistry , gene
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.