enow.com Web Search

Search results

  1. Results from the WOW.Com Content Network
  2. Adenosine triphosphate - Wikipedia

    en.wikipedia.org/wiki/Adenosine_triphosphate

    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 ...

  3. ATPase - Wikipedia

    en.wikipedia.org/wiki/ATPase

    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.

  4. ATP synthase - Wikipedia

    en.wikipedia.org/wiki/ATP_synthase

    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.

  5. Mitochondrion - Wikipedia

    en.wikipedia.org/wiki/Mitochondrion

    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]

  6. ATP synthase alpha/beta subunits - Wikipedia

    en.wikipedia.org/wiki/ATP_synthase_alpha/beta...

    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:

  7. ATP-binding motif - Wikipedia

    en.wikipedia.org/wiki/ATP-binding_motif

    An ATP-binding motif is a 250-residue sequence within an ATP-binding protein’s primary structure. The binding motif is associated with a protein’s structure and/or function. [ 1 ] ATP is a molecule of energy, and can be a coenzyme, involved in a number of biological reactions.

  8. ATP hydrolysis - Wikipedia

    en.wikipedia.org/wiki/ATP_hydrolysis

    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.

  9. ATP5F1A - Wikipedia

    en.wikipedia.org/wiki/ATP5F1A

    ATP synthase is composed of two linked multi-subunit complexes: the soluble catalytic core, F 1, and the membrane-spanning component, F o, 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 ...