Oxidative phosphorylation

Edge evidence

• Oxidative phosphorylation uses pathway electron transport chain

  Oxidative phosphorylation couples phosphorylation to respiratory electron transfer.

  • DOI:10.1038/191144a0 electron and hydrogen transfer Mitchell paper supports coupling electron/hydrogen transfer to phosphorylation.
• electron transport chain localized to cellular membrane biolink:located_in

  Electron transfer and proton translocation are membrane-coupled.

  • DOI:10.1038/191144a0 Chemi-Osmotic Type of Mechanism Chemiosmotic mechanism requires a membrane-separated ion gradient.
• electron transport chain generates proton motive force biolink:produces

  Respiratory electron transfer establishes a proton motive force.

  • DOI:10.1038/s41598-019-38564-0 proton motive force (pmf) established and maintained by respiratory chain enzymes Supports respiratory chain generation of pmf.
• proton motive force regulates F1Fo ATP synthase RO:0002211

  Proton motive force energizes F1Fo ATP synthase.

  • DOI:10.1038/s41598-019-38564-0 energized by the proton motive force Supports pmf-driven ATP synthase.
• F1Fo ATP synthase produces ATP METPO:2000202

  ATP synthase synthesizes ATP from ADP and phosphate.

  • DOI:10.1007/BF01923429 synthesis of ATP is also driven by a proton motive force ATP synthase review supports pmf-driven ATP synthesis.
• NADH is oxidized by Complex I / NADH:quinone oxidoreductase (NDH-1)

  Complex I oxidizes NADH at the respiratory chain entry point.

  • DOI:10.3390/ijms252413421 complex I catalyzes the oxidation of NADH by ubiquinone (general prokaryotic claim).
• Complex I / NADH:quinone oxidoreductase (NDH-1) reduces quinone pool METPO:2000017

  Complex I transfers electrons from NADH to the quinone pool.

  • DOI:10.3390/ijms252413421 oxidation of NADH by ubiquinone; reduces the membrane quinone pool.
• Complex I / NADH:quinone oxidoreductase (NDH-1) translocates proton

  Complex I couples redox chemistry to transmembrane proton translocation.

  • DOI:10.3390/ijms252413421 coupled with the vectorial transmembrane transfer of four H+ ions.
• succinate is oxidized by succinate dehydrogenase / Complex II

  Succinate dehydrogenase oxidizes succinate, reducing quinone.

  • DOI:10.1007/s10863-024-10041-y succinate dehydrogenase catalyzes the two-electron reduction of quinone by succinate.
• proton translocation generates proton motive force biolink:produces

  Vectorial proton translocation establishes the proton motive force.

  • DOI:10.3390/ijms252413421 energy conservation in the form of an electrochemical gradient (proton motive force, pmf).
• terminal oxidase reduces oxygen METPO:2000017

  Terminal oxidases catalyze four-electron reduction of O2 to water.

  • DOI:10.3390/ijms25021277 Terminal oxidases catalyze four-electron reduction of O2 to 2H2O (general bacterial claim).
• heme-copper oxidase translocates proton

  Heme-copper oxidases act as proton pumps contributing to PMF.

  • DOI:10.3390/ijms25021277 Heme-copper oxidases are true proton pumps (general claim).