Allosteric nucleotide-binding site in the mitochondrial NADH:ubiquinone oxidoreductase (respiratory complex I)

FEBS Lett. 2011 Jul 21;585(14):2212-6. doi: 10.1016/j.febslet.2011.05.039. Epub 2011 May 27.

Abstract

The rotenone-insensitive NADH:hexaammineruthenium III (HAR) oxidoreductase reactions catalyzed by bovine heart and Yarrowia lipolytica submitochondrial particles or purified bovine complex I are stimulated by ATP and other purine nucleotides. The soluble fraction of mammalian complex I (FP) and prokaryotic complex I homolog NDH-1 in Paracoccus denitrificans plasma membrane lack stimulation of their activities by ATP. The stimulation appears as a decrease in apparent K(m) values for NADH and HAR. Thus, the "accessory" subunits of eukaryotic complex I bear an allosteric ATP-binding site.

Publication types

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

MeSH terms

  • Adenosine Triphosphate / metabolism
  • Allosteric Regulation*
  • Animals
  • Binding Sites
  • Cattle
  • Electron Transport Complex I / chemistry*
  • Electron Transport Complex I / metabolism
  • Fungal Proteins / chemistry*
  • Fungal Proteins / metabolism
  • Mitochondria / enzymology*
  • NAD / metabolism
  • NADH, NADPH Oxidoreductases / chemistry*
  • NADH, NADPH Oxidoreductases / metabolism
  • Nucleotides / metabolism*
  • Paracoccus denitrificans / cytology
  • Paracoccus denitrificans / metabolism
  • Ruthenium Compounds / metabolism
  • Yarrowia / cytology
  • Yarrowia / metabolism

Substances

  • Fungal Proteins
  • Nucleotides
  • Ruthenium Compounds
  • NAD
  • hexammineruthenium
  • Adenosine Triphosphate
  • NADH, NADPH Oxidoreductases
  • Electron Transport Complex I