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- W2017589360 abstract "Membranes of mitochondria (1–2), chloroplasts (3–4), and photosynthetic bacteria (5), manifest mechanochemical changes that are coupled to energy transfer reactions. These changes in membrane structure or membrane deformations, conveniently measured by the recording of a physical parameter such as light-scattering, can be closely correlated to conditions favorable for oxidative or photophosphorylation. Since all of the reactants required for phosphorylation coupled to electron transport in both photosynthetic and non-photosynthetic systems are required for the change in structure, and since inhibitors of these functions abolish the change, it has been suggested (1–2, 4–5) that the structural parameter is under the control of energy-containing intermediates. Recent experiments with mitochondria (6) have demonstrated that swelling induced by electron transport is oligomycin sensitive, whereas reversal of swelling by ADP (under conditions of oxidative phosphorylation) is specifically blocked by oligomycin. These observations implicate the ATPase site in the control of mechanochemical changes. Ohnishi and Ohnishi (7) have isolated a protein from mitochondria which undergoes conformational changes with ATP (light-scattering, viscosity) and manifests ATPase activity. It is an attractive hypothesis that in mitochondria, a contractile-like substance may be involved in the changes in macromolecular structure coupled to energy transduction. In view of this, it seemed worthwhile to examine the role of ATP and ATPase activity in the control of chloroplast structure in more detail. In brief, effects of ATP on structural changes in spinach chloroplasts have been demonstrated. Furthermore, a protein fraction has been isolated from chloroplast membranes which undergoes light-scattering changes with ATP and which hydrolyzes this substance." @default.
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- W2017589360 date "1963-06-01" @default.
- W2017589360 modified "2023-10-18" @default.
- W2017589360 title "Observations on the control of chloroplast structure by adenosine triphosphate" @default.
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- W2017589360 doi "https://doi.org/10.1016/0006-291x(63)90087-1" @default.
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