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ATP synthase is an enzyme that catalyzes the formation of the energy storage molecule adenosine triphosphate (ATP) using adenosine diphosphate (ADP) and inorganic phosphate (P i). ATP synthase is a molecular machine. The overall reaction catalyzed by ATP synthase is: ADP + P i + 2H + out ⇌ ATP + H 2 O + 2H + in
ATPases (or ATP synthases) are membrane-bound enzyme complexes/ion transporters that combine ATP synthesis and/or hydrolysis with the transport of protons across a membrane. ATPases can harness the energy from a proton gradient, using the flux of ions across the membrane via the ATPase proton channel to drive the synthesis of ATP. Some ATPases ...
The "machinery" is similar to that in mitochondria except that light energy is used to pump protons across a membrane to produce a proton-motive force. ATP synthase then ensues exactly as in oxidative phosphorylation. [28] Some of the ATP produced in the chloroplasts is consumed in the Calvin cycle, which produces triose sugars.
Both the structure of ATP synthase and its underlying gene are remarkably similar in all known forms of life. ATP synthase is powered by a transmembrane electrochemical potential gradient, usually in the form of a proton gradient. In all living organisms, a series of redox reactions is used to produce a transmembrane electrochemical potential ...
This gradient is used by the F O F 1 ATP synthase complex to make ATP via oxidative phosphorylation. ATP synthase is sometimes described as Complex V of the electron transport chain. [10] The F O component of ATP synthase acts as an ion channel that provides for a proton flux back into the mitochondrial matrix. It is composed of a, b and c ...
This potential is then used to drive ATP synthase and produce ATP from ADP and a phosphate group. Biology textbooks often state that 38 ATP molecules can be made per oxidized glucose molecule during cellular respiration (2 from glycolysis, 2 from the Krebs cycle, and about 34 from the electron transport system). [5]
Mechanism of ATP synthase. ATP is shown in red, ADP and phosphate in pink and the rotating γ subunit in black. This ATP synthesis reaction is called the binding change mechanism and involves the active site of a β subunit cycling between three states. [77] In the "open" state, ADP and phosphate enter the active site (shown in brown in the ...
F-ATP synthases are identical in appearance and function except for the mitochondrial F 0 F 1-ATP synthase, which contains 7-9 additional subunits. [12] The electrochemical potential is what causes the c-ring to rotate in a clockwise direction for ATP synthesis. This causes the central stalk and the catalytic domain to change shape.