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Penefsky 1960 J Biol Chem

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Penefsky HS, Pullman ME, Datta A, Racker E (1960) Partial resolution of the enzymes catalyzing oxidative phosphorylation II. Participation of a soluble adenosine triphosphatase in oxidative phosphorylation. J Biol Chem 235:3330-6.

Β» PMID: 1373409 Open Access

Penefsky HS, Pullman ME, Datta A, Racker E (1960) J Biol Chem

Abstract:

  1. Mechanically fragmented beef heart mitochondria have been resolved by differential centrifugation into a particulate and a soluble protein component, both of which were required for oxidative phosphorylation. The particulate fraction alone catalyzed the oxidation of succinate, Ξ²-hydroxybutyrate, isocitrate, and glutamate with little or no concomitant phosphorylation. Addition of the soluble factor to the particles resulted in a net uptake of inorganic phosphate with a P:O of 0.4 to 0.8. Similarly, both fractions were required for a P32-ATP exchange.
  2. The highly purified, soluble coupling factor catalyzed a dinitrophenol-stimulated hydrolysis of ATP.
  3. Comparative studies of the cold lability, heat stability, and other physical properties strongly favored the conclusion that the coupling and ATPase activity were catalyzed by the same protein.
  4. The significance of these results in relation to current concepts of the mechanism of oxidative phosphorylation has been discussed.

β€’ Keywords: oxidative phosphorylation, soluble ATP


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Enzyme: Complex II;succinate dehydrogenase  Regulation: ATP  Coupling state: OXPHOS 


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