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  2. Photophosphorylation - Wikipedia

    en.wikipedia.org/wiki/Photophosphorylation

    Both the structure of ATP synthase and its underlying gene are remarkably similar in all known forms of life. ATP synthase is powered by a transmembrane electrochemical potential gradient, usually in the form of a proton gradient. In all living organisms, a series of redox reactions is used to produce a transmembrane electrochemical potential ...

  3. ATP synthase - Wikipedia

    en.wikipedia.org/wiki/ATP_synthase

    ATP synthase is an enzyme that catalyzes the formation of the energy storage molecule adenosine triphosphate (ATP) using adenosine diphosphate (ADP) and inorganic phosphate (P i). ATP synthase is a molecular machine. The overall reaction catalyzed by ATP synthase is: ADP + P i + 2H + out ⇌ ATP + H 2 O + 2H + in

  4. Light-dependent reactions - Wikipedia

    en.wikipedia.org/wiki/Light-dependent_reactions

    Cytochrome b 6 f and ATP synthase work together to produce ATP (photophosphorylation) in two distinct ways. In non-cyclic photophosphorylation, cytochrome b 6 f uses electrons from PSII and energy from PSI [citation needed] to pump protons from the stroma to the lumen. The resulting proton gradient across the thylakoid membrane creates a proton ...

  5. Cellular respiration - Wikipedia

    en.wikipedia.org/wiki/Cellular_respiration

    This potential is then used to drive ATP synthase and produce ATP from ADP and a phosphate group. Biology textbooks often state that 38 ATP molecules can be made per oxidized glucose molecule during cellular respiration (2 from glycolysis, 2 from the Krebs cycle, and about 34 from the electron transport system). [5]

  6. Oxidative phosphorylation - Wikipedia

    en.wikipedia.org/wiki/Oxidative_phosphorylation

    Mechanism of ATP synthase. 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 ...

  7. 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 ...

  8. Mitochondrion - Wikipedia

    en.wikipedia.org/wiki/Mitochondrion

    The protons can return to the matrix through the ATP synthase complex, and their potential energy is used to synthesize ATP from ADP and inorganic phosphate (P i). [21] This process is called chemiosmosis , and was first described by Peter Mitchell , [ 46 ] [ 47 ] who was awarded the 1978 Nobel Prize in Chemistry for his work.

  9. Adenosine diphosphate - Wikipedia

    en.wikipedia.org/wiki/Adenosine_diphosphate

    The ATP synthase complex exists within the mitochondrial membrane (F O portion) and protrudes into the matrix (F 1 portion). The energy derived as a result of the chemical gradient is then used to synthesize ATP by coupling the reaction of inorganic phosphate to ADP in the active site of the ATP synthase enzyme; the equation for this can be ...