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Interactive animation of the structure of ATP. Adenosine triphosphate (ATP) is a nucleoside triphosphate [2] that provides energy to drive and support many processes in living cells, such as muscle contraction, nerve impulse propagation, and chemical synthesis.
The following other wikis use this file: Usage on ba.wikipedia.org Аденозинтрифосфор кислотаһы — АТФ; Usage on be.wikipedia.org
The chemical structure of adenosine triphosphate. Date: 16 August 2007: Source: Self-made in bkchem; edited in perl. Author: Mysid: Other versions: Derivative works of this file: ATP structure revised.png: SVG development
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.
A mitochondrion (pl. mitochondria) is an organelle found in the cells of most eukaryotes, such as animals, plants and fungi.Mitochondria have a double membrane structure and use aerobic respiration to generate adenosine triphosphate (ATP), which is used throughout the cell as a source of chemical energy. [2]
The protons return to the mitochondrial matrix through the protein ATP synthase. The energy is used in order to rotate ATP synthase which facilitates the passage of a proton, producing ATP. A pH difference between the matrix and intermembrane space creates an electrochemical gradient by which ATP synthase can pass a proton into the matrix ...
Structure of ATP Structure of ADP Four possible resonance structures for inorganic phosphate. ATP hydrolysis is the catabolic reaction process by which chemical energy that has been stored in the high-energy phosphoanhydride bonds in adenosine triphosphate (ATP) is released after splitting these bonds, for example in muscles, by producing work in the form of mechanical energy.
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 diagram).