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Most useful ATP analogs cannot be hydrolyzed as ATP would be; instead, they trap the enzyme in a structure closely related to the ATP-bound state. Adenosine 5′-(γ-thiotriphosphate) is an extremely common ATP analog in which one of the gamma-phosphate oxygens is replaced by a sulfur atom; this anion is hydrolyzed at a dramatically slower rate ...
ATPase, any enzyme that makes use of adenosine triphosphate; Advanced Technology Program, US government program; Alberta Taciuk process, for extracting oil from shale, etc. Anti-tachycardia pacing, process similar to a pacemaker; Assistive Technology Practitioner - Rehabilitation Engineering and Assistive Technology Society of North America (RESNA)
The driving force is due to the ATP (−4) having a more negative charge than the ADP (−3), and thus it dissipates some of the electrical component of the proton electrochemical gradient. The outcome of these transport processes using the proton electrochemical gradient is that more than 3 H + are needed to make 1 ATP.
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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.
The F 1 portion of ATP synthase is hydrophilic and responsible for hydrolyzing ATP. The F 1 unit protrudes into the mitochondrial matrix space. Subunits α and β make a hexamer with 6 binding sites. Three of them are catalytically inactive and they bind ADP. Three other subunits catalyze the ATP synthesis.
The result is that the cell or mitochondrion expends energy to generate a proton-motive force, but the proton-motive force is dissipated before the ATP synthase can recapture this energy and use it to make ATP. Because the intracellular supply of protons is replenished, uncouplers actually stimulate cellular metabolism and oxygen consumption ...
ATP contains one more phosphate group than ADP, while AMP contains one fewer phosphate group. Energy transfer used by all living things is a result of dephosphorylation of ATP by enzymes known as ATPases. The cleavage of a phosphate group from ATP results in the coupling of energy to metabolic reactions and a by-product of ADP. [1]