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  2. Adenosine triphosphate - Wikipedia

    en.wikipedia.org/wiki/Adenosine_triphosphate

    Higher concentrations of Mg 2+ decrease free energy released in the reaction due to binding of Mg 2+ ions to negatively charged oxygen atoms of ATP at pH 7. [17] This image shows a 360-degree rotation of a single, gas-phase magnesium-ATP chelate with a charge of −2. The anion was optimized at the UB3LYP/6-311++G(d,p) theoretical level and the ...

  3. Translocase - Wikipedia

    en.wikipedia.org/wiki/Translocase

    Several of these involve the hydrolysis of ATP and had been previously classified as ATPases (EC 3.6.3.-), although the hydrolytic reaction is not their primary function. In August 2018, the International Union of Biochemistry and Molecular Biology classified these enzymes under a new enzyme class (EC) of translocases (EC 7). [2]

  4. Phosphorylation - Wikipedia

    en.wikipedia.org/wiki/Phosphorylation

    Phosphorylation is essential to the processes of both anaerobic and aerobic respiration, which involve the production of adenosine triphosphate (ATP), the "high-energy" exchange medium in the cell. During aerobic respiration, ATP is synthesized in the mitochondrion by addition of a third phosphate group to adenosine diphosphate (ADP) in a ...

  5. Cellular respiration - Wikipedia

    en.wikipedia.org/wiki/Cellular_respiration

    The ATP generated in this process is made by substrate-level phosphorylation, which does not require oxygen. Fermentation is less efficient at using the energy from glucose: only 2 ATP are produced per glucose, compared to the 38 ATP per glucose nominally produced by aerobic respiration. Glycolytic ATP, however, is produced more quickly.

  6. 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.

  7. Nucleoside-phosphate kinase - Wikipedia

    en.wikipedia.org/wiki/Nucleoside-phosphate_kinase

    A number of crystal structures have been solved for this class of enzymes, revealing that they share a common ATP binding domain. This section of the enzyme is commonly referred to as the P-loop, [5] in reference to its interaction with the phosphoryl groups on ATP. This binding domain also consists of a β sheet flanked by α helices.

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  9. Adenosine diphosphate - Wikipedia

    en.wikipedia.org/wiki/Adenosine_diphosphate

    Breaking one of ATP's phosphorus bonds generates approximately 30.5 kilojoules per mole of ATP (7.3 kcal). [3] ADP can be converted, or powered back to ATP through the process of releasing the chemical energy available in food; in humans, this is constantly performed via aerobic respiration in the mitochondria. [2]