Difference between revisions of "Ragan 1973 J Biol Chem"
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Latest revision as of 09:42, 27 November 2015
Ragan CI, Racker E (1973) Partial resolution of the enzymes catalyzing oxidative phosphorylation XXVII. The reconstitution of the first site of energy conservation. J Biol Chem 248:2563-9. |
Β» PMID: 4144592 Open Access; PDF
Ragan CI, Racker E (1973) J Biol Chem
Abstract:
- The ability to phosphorylate ADP during oxidation of NADH by ubiquinone-1 was restored to the NADH-ubiquinone reductase complex by combining the latter with phospholipids and a hydrophobic protein fraction derived from bovine heart mitochondria.
- Phosphorylation was abolished by rotenone, uncoupling agents, or rutamycin. The efficiency of ATP formation was as high as 0.5 mole per mole of NADH oxidized under optimal conditions.
- Reconstitution of phosphorylation had an absolute requirement for phosphatidylethanolamine and a partial requirement for phosphatidylcholine, a molar ratio of approximately 4:1 being optimal. A much more marked requirement for phosphatidylcholine was observed in the presence of low concentrations of cardiolipin (0.05 to 1.5% of the total phospholipid). In the presence of cardiolipin, an equal molar ratio of phosphatidylethanolamine to phosphatidylcholine gave the highest phosphorylation efficiency.
- The NADH-ubiquinone reductase complex is oriented in the reconstituted vesicles such that approximately 50% of the molecules can react with added NADH. Reaction of all the molecules with NADH occurs in the presence of 0.5% deoxycholate.
- Phosphorylation efficiency can be significantly improved by purification of the vesicles on sucrose density gradients.
β’ Keywords: Oxidative phosphorylation, Energy conservation, Bovine heart submitochondrial particles
Labels:
Organism: Bovines
Tissue;cell: Heart
Preparation: Isolated mitochondria
Enzyme: Complex V;ATP synthase
Regulation: ATP
Made history