Difference between revisions of "Penefsky 1960 J Biol Chem"
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# 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.  | # 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. | # The significance of these results in relation to current concepts of the mechanism of oxidative phosphorylation has been discussed. | ||
 | |keywords=oxidative phosphorylation, soluble ATP | ||
|keywords=oxidative phosphorylation, soluble ATP Â | |||
}} | }} | ||
{{Labeling | {{Labeling | ||
|couplingstates=OXPHOS | |||
|enzymes=Complex II; Succinate Dehydrogenase | |enzymes=Complex II; Succinate Dehydrogenase | ||
|topics= | |topics=ATP; ADP; AMP; PCr | ||
|additional=Made history | |additional=Made history | ||
}} | }} | ||
Revision as of 16:22, 27 November 2012
| 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: 3330-3336. |
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, ÎČ-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.
âą Keywords: oxidative phosphorylation, soluble ATP
Labels:
Enzyme: Complex II; Succinate Dehydrogenase"Complex II; Succinate Dehydrogenase" is not in the list (Adenine nucleotide translocase, Complex I, Complex II;succinate dehydrogenase, Complex III, Complex IV;cytochrome c oxidase, Complex V;ATP synthase, Inner mt-membrane transporter, Marker enzyme, Supercomplex, TCA cycle and matrix dehydrogenases, ...) of allowed values for the "Enzyme" property. Regulation: ATP; ADP; AMP; PCr"ATP; ADP; AMP; PCr" is not in the list (Aerobic glycolysis, ADP, ATP, ATP production, AMP, Calcium, Coupling efficiency;uncoupling, Cyt c, Flux control, Inhibitor, ...) of allowed values for the "Respiration and regulation" property. Coupling state: OXPHOS
Made history
