Difference between revisions of "Thayer 1975 J Biol Chem"
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{{Publication | {{Publication | ||
|title=Thayer WS, Hinkle PC (1975) Synthesis of adenosine triphosphate by an artificially imposed electrochemical proton gradient in bovine heart submitochondrial particles. J Biol Chem 250: 5330- | |title=Thayer WS, Hinkle PC (1975) Synthesis of adenosine triphosphate by an artificially imposed electrochemical proton gradient in bovine heart submitochondrial particles. J Biol Chem 250:5330-5. | ||
|info=[http://www.jbc.org/content/250/14/5330.full.pdf+html PMID: 237916 Open Access] | |info=[http://www.jbc.org/content/250/14/5330.full.pdf+html PMID: 237916 Open Access] | ||
|authors=Thayer WS, Hinkle PC | |authors=Thayer WS, Hinkle PC | ||
|year=1975 | |year=1975 | ||
|journal=J Biol Chem | |journal=J Biol Chem | ||
|abstract=Submitochondrial particles subjected to an artificially imposed electrochemical proton gradient consisting of a pH gradient (acid to base transition) and membrane potential (low to high K-+ transition in the presence of valinomycin) catalyzed the net synthesis of 2.5 nmol of [-32P]ATP per mg of protein from ADP and 32-Pi. Optimal reaction conditions included incubation of submitochondrial particles in malonate at pH 5.0 with valinomycin in the absence of added K-+, followed by a rapid transition to pH 7.5 and 100 mM K-+. ATP synthesis continued for about 6 s and was sensitive to uncouplers or oligomycin but insensitive to inhibitors of electron transport. Lower amounts of ATP were formed by either the pH gradient (25%) of K-+ gradient (15%) alone. These results demonstrate that an electrochemical gradient of protons can drive the synthesis of ATP by reversal of the proton-translocating ATPase independent of electron transport. | |abstract=Submitochondrial particles subjected to an artificially imposed electrochemical proton gradient consisting of a pH gradient (acid to base transition) and membrane potential (low to high K<sup>-+</sup> transition in the presence of valinomycin) catalyzed the net synthesis of 2.5 nmol of [-32P]ATP per mg of protein from ADP and 32-Pi. Optimal reaction conditions included incubation of submitochondrial particles in malonate at pH 5.0 with valinomycin in the absence of added K<sup>-+</sup>, followed by a rapid transition to pH 7.5 and 100 mM K<sup>-+</sup>. ATP synthesis continued for about 6 s and was sensitive to uncouplers or oligomycin but insensitive to inhibitors of electron transport. Lower amounts of ATP were formed by either the pH gradient (25%) of K<sup>-+</sup> gradient (15%) alone. These results demonstrate that an electrochemical gradient of protons can drive the synthesis of ATP by reversal of the proton-translocating ATPase independent of electron transport. | ||
|keywords=ATP synthesis, | |keywords=ATP synthesis, Proton gradient, Submitochondrial particles, Beef heart | ||
}} | }} | ||
{{Labeling | {{Labeling | ||
|organism= | |area=Respiration | ||
|tissues= | |organism=Bovines | ||
|preparations= | |tissues=Heart | ||
| | |preparations=SMP | ||
| | |topics=ATP production, Coupling efficiency;uncoupling, Ion;substrate transport, pH | ||
|couplingstates=OXPHOS | |||
|additional=Made history | |additional=Made history | ||
}} | }} | ||
Latest revision as of 09:56, 27 November 2015
| Thayer WS, Hinkle PC (1975) Synthesis of adenosine triphosphate by an artificially imposed electrochemical proton gradient in bovine heart submitochondrial particles. J Biol Chem 250:5330-5. |
Thayer WS, Hinkle PC (1975) J Biol Chem
Abstract: Submitochondrial particles subjected to an artificially imposed electrochemical proton gradient consisting of a pH gradient (acid to base transition) and membrane potential (low to high K-+ transition in the presence of valinomycin) catalyzed the net synthesis of 2.5 nmol of [-32P]ATP per mg of protein from ADP and 32-Pi. Optimal reaction conditions included incubation of submitochondrial particles in malonate at pH 5.0 with valinomycin in the absence of added K-+, followed by a rapid transition to pH 7.5 and 100 mM K-+. ATP synthesis continued for about 6 s and was sensitive to uncouplers or oligomycin but insensitive to inhibitors of electron transport. Lower amounts of ATP were formed by either the pH gradient (25%) of K-+ gradient (15%) alone. These results demonstrate that an electrochemical gradient of protons can drive the synthesis of ATP by reversal of the proton-translocating ATPase independent of electron transport. • Keywords: ATP synthesis, Proton gradient, Submitochondrial particles, Beef heart
Labels: MiParea: Respiration
Organism: Bovines
Tissue;cell: Heart
Preparation: SMP
Regulation: ATP production, Coupling efficiency;uncoupling, Ion;substrate transport, pH Coupling state: OXPHOS
Made history
