Difference between revisions of "Penefsky 1960 J Biol Chem"
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{{Publication | {{Publication | ||
|title=Penefsky HS, Pullman ME, Datta A, Racker E (1960) Partial resolution of the enzymes catalyzing oxidative phosphorylation II. Participation of a soluble adenosine | |title=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. | ||
|info=[http://www.jbc.org/content/235/11/3330.full.pdf+html PMID: 1373409 Open Access] | |info=[http://www.jbc.org/content/235/11/3330.full.pdf+html PMID: 1373409 Open Access] | ||
|authors=Penefsky HS, Pullman ME, Datta A, Racker E | |authors=Penefsky HS, Pullman ME, Datta A, Racker E | ||
|year=1960 | |year=1960 | ||
|journal=J Biol Chem | |journal=J Biol Chem | ||
|abstract=# 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, β-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. | |||
# The highly purified, soluble coupling factor catalyzed a dinitrophenol-stimulated hydrolysis of ATP. | |||
# 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. | |||
# The significance of these results in relation to current concepts of the mechanism of oxidative phosphorylation has been discussed. | |||
|keywords=oxidative phosphorylation, soluble ATP | |||
}} | }} | ||
{{Labeling | {{Labeling | ||
|enzymes=Complex II;succinate dehydrogenase | |||
|topics=ATP | |||
|couplingstates=OXPHOS | |||
|additional=Made history | |additional=Made history | ||
}} | }} | ||
Latest revision as of 17:58, 25 November 2015
| 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. |
Penefsky HS, Pullman ME, Datta A, Racker E (1960) J Biol Chem
Abstract:
- 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, β-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.
- The highly purified, soluble coupling factor catalyzed a dinitrophenol-stimulated hydrolysis of ATP.
- 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.
- The significance of these results in relation to current concepts of the mechanism of oxidative phosphorylation has been discussed.
• Keywords: oxidative phosphorylation, soluble ATP
Labels:
Enzyme: Complex II;succinate dehydrogenase Regulation: ATP Coupling state: OXPHOS
Made history
