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Energy coupling to ATP synthesis by the proton-translocating ATPase
The Journal of Membrane Biology, 1982This review summarizes recent work on energy coupling to ATP synthesis by the reversible, proton-translocating ATPase to mitochondria, chloroplasts, and bacteria. In the first sections, this enzyme is distinguished from other ATP-linked ion transport systems, and progress in the biochemical analysis is discussed.
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Proton-translocating ATPase of chromaffin granule membranes.
Federation proceedings, 1982Active transport of catecholamines into chromaffin granules is driven by the transmembrane pH gradient and membrane potential, created by an electrogenic proton-translocating ATPase in the granule membrane. The ATPase activity of highly purified chromaffin granule membranes is inhibited by a number of agents in common with mitochondrial ATPase, and ...
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Assembly of the yeast vacuolar proton-translocating ATPase.
Journal of bioenergetics and biomembranes, 1999The yeast vacuolar proton-translocating ATPase (V-ATPase) is the best characterized member of the V-ATPase family. Biochemical and genetic screens led to the identification of a large number of genes in yeast, designated VMA, encoding proteins required to assemble a functional V-ATPase.
L A, Graham, T H, Stevens
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The Proton-Translocating F0F1 ATP Synthase-ATPase Complex
2006The F0F1 ATP synthase is responsible for electron-transport coupled ATP synthesis in every living cell, and functions also as a reversible ATPase. It is composed of an integral membrane sector, F0, containing four subunits in a stoichiometry of a1b1b11c6−12, and an extrinsic sector, F1, containing five subunits in a stoichiometry of α3β3γ1δ1e1.
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Proton translocating ATPase: its pump, gate, and channel.
Advances in biophysics, 1978Proton translocating ATPase of oxidative phosphorylation was divided into three functional units: pump, channel, and gate. This was achieved by the use of highly stable pure ATPase obtained from a thermophilic bacterium PS3. The pump and gate were found in a catalytic moiety of the ATPase called TF1, and the channel was in the remaining hydrophobic ...
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[Proton translocation coefficient for H+-ATPase of rat liver mitochondria].
Biokhimiia (Moscow, Russia), 1982Some features of H+-ATPase function in intact mitochondria of rat liver were studied. Simultaneously the activities of ATPase and proton translocase were measured, using a previously described technique. The proton translocation coefficient of H+-ATPase has been found to be equal to 3.6.
K F, Shol'ts +2 more
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The proton-translocating ATPase of the fungal plasma membrane
Biochimica et Biophysica Acta (BBA) - Reviews on Bioenergetics, 1981A, Goffeau, C W, Slayman
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The Proton-Translocating Membrane ATPase (F1F0) in Streptococcus faecalis (faecium)
1985It is generally believed that a proton-translocating ATPase, referred to as the F1F0 ATPase, is present universally in bacterial cell membranes. It is also apparent that, at the level of quaternary structure, the bacterial enzyme is essentially identical to the F1F0 ATPase localized in membranes of mitochondria, photosynthesizing organelles, and ...
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Proton Translocating ATPases of Photosynthetic Membranes
1982RICHARD E. MCCARTY, CHANOCH CARMELI
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