Title: Role of Subunits in Proton-Translocating ATPase (F0–F1)
Abstract: All forms of living cells conserve energy in chemical compounds, especially in adenosine triphosphate (ATP). The proton-translocating ATPase in membranes of chloroplasts, mitochondria, and bacteria synthesizes this high energy compound utilizing energy from the electron transfer chain. The overall reactions of ATP synthesis in these organellae have been explained by the chemiosmotic hypothesis. This hypothesis proposes that ATP is synthesized by the ATPase complex, utilizing an electrochemical gradient of protons. This electrochemical gradient of protons or proton-motive force is formed by the unidirectional movement of protons across membranes during the flow of electrons through the respiratory or photosynthetic electron transfer chain. The ATPase complex phosphorylates adenosine diphosphate (ADP) to form ATP driven by a reverse flow of protons. The complex can work reversibly and form an electrochemical gradient of protons coupled with the hydrolysis of ATP. Although the basic features of the mechanism of phosphorylation have been established, it is still unknown at the molecular level how synthesis or hydrolysis of ATP by the enzyme complex, is coupled to vectorial translocation of protons
Publication Year: 1980
Publication Date: 1980-01-01
Language: en
Type: book-chapter
Indexed In: ['crossref']
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Cited By Count: 73
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