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ADP and Pi (inorganic phosphate) bind spontaneously to the three β subunits of the F 1 domain, so that every time it goes through a 120° rotation ATP is released (rotational catalysis). The F o domains sits within the membrane, spanning the phospholipid bilayer, while the F 1 domain extends into the cytosol of the cell to facilitate the use ...
Some ATPases work in reverse, using the energy from the hydrolysis of ATP to create a proton gradient. There are different types of ATPases, which can differ in function (ATP synthesis and/or hydrolysis), structure (F-, V- and A-ATPases contain rotary motors) and in the type of ions they transport. [3] [4] The types with this domain include:
The structure of the intact ATP synthase is currently known at low-resolution from electron cryo-microscopy (cryo-EM) studies of the complex. The cryo-EM model of ATP synthase suggests that the peripheral stalk is a flexible structure that wraps around the complex as it joins F 1 to F O.
ATP synthase is composed of two linked multi-subunit complexes: the soluble catalytic core, F1, and the membrane-spanning component, Fo, comprising the proton channel. The catalytic portion of mitochondrial ATP synthase consists of 5 different subunits (alpha, beta, gamma, delta, and epsilon) assembled with a stoichiometry of 3 alpha, 3 beta ...
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.
Adenosine triphosphate Adenosine diphosphate Adenosine monophosphate. ATPases (EC 3.6.1.3, Adenosine 5'-TriPhosphatase, adenylpyrophosphatase, ATP monophosphatase, triphosphatase, SV40 T-antigen, ATP hydrolase, complex V (mitochondrial electron transport), (Ca 2+ + Mg 2+)-ATPase, HCO 3 −-ATPase, adenosine triphosphatase) are a class of enzymes that catalyze the decomposition of ATP into ADP ...
ATP synthase is the enzyme that makes ATP by chemiosmosis. It allows protons to pass through the membrane and uses the free energy difference to convert phosphorylate adenosine diphosphate (ADP) into ATP. The ATP synthase contains two parts: CF0 (present in thylakoid membrane) and CF1 (protrudes on the outer surface of thylakoid membrane).
The formation of ATP is energetically unfavorable and would not normally proceed. In order to drive this reaction forward, ATP synthase couples ATP synthesis to an electrochemical gradient that drives rotational motor mechanism allowing for ATP production. Because of its rotating subunit, ATP synthase is a molecular machine.