Molecular identification of the enzyme responsible for the mitochondrial NADH-supported ammonium-dependent hydrogen peroxide production

FEBS Lett. 2011 Jan 21;585(2):385-9. doi: 10.1016/j.febslet.2010.12.019. Epub 2010 Dec 17.

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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Animals
  • Catalysis
  • Cattle
  • Dihydrolipoamide Dehydrogenase / isolation & purification*
  • Dihydrolipoamide Dehydrogenase / metabolism
  • Hydrogen Peroxide / metabolism*
  • Mass Spectrometry
  • Mitochondria, Heart / enzymology*
  • NAD*
  • Quaternary Ammonium Compounds*

Substances

  • Quaternary Ammonium Compounds
  • NAD
  • Hydrogen Peroxide
  • Dihydrolipoamide Dehydrogenase