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- Title
Allosteric nucleotide-binding site in the mitochondrial NADH:ubiquinone oxidoreductase (respiratory complex I)
- Authors
Grivennikova, Vera G.; Gladyshev, Grigory V.; Vinogradov, Andrei D.
- Abstract
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.
- Subjects
MITOCHONDRIA; NAD (Coenzyme); UBIQUINONES; OXIDOREDUCTASES; ROTENONE; CATALYSIS; ADENOSINE triphosphate; PURINE nucleotides
- Publication
FEBS Letters, 2011, Vol 585, Issue 14, p2212
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/j.febslet.2011.05.039