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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
The ATP synthase complex exists within the mitochondrial membrane (F O portion) and protrudes into the matrix (F 1 portion). The energy derived as a result of the chemical gradient is then used to synthesize ATP by coupling the reaction of inorganic phosphate to ADP in the active site of the ATP synthase enzyme; the equation for this can be ...
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.
The ABC transporters, ATP synthase (ATP)-binding cassette transporters are a transport system superfamily that is one of the largest and possibly one of the oldest gene families. It is represented in all extant phyla , from prokaryotes to humans .
F-type proton ATPase [12] [13] (or F-ATPase) typically operates as an ATP synthase that dissipates a proton gradient rather than generating one; i.e. protons flow in the reverse direction compared to V-type ATPases. In eubacteria, F-type ATPases are found in plasma membranes.
ATP synthase is powered by a proton-motive force created by using the energy generated from the electron transport chain. A hydrogen ion (H + ) has a positive charge and if separated by a cellular membrane, it creates a difference in charge between the inside and outside of the membrane.
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F-ATPase, also known as F-Type ATPase, is an ATPase/synthase found in bacterial plasma membranes, in mitochondrial inner membranes (in oxidative phosphorylation, where it is known as Complex V), and in chloroplast thylakoid membranes.