首页|Novel molecular insights into ATP synthesis in oxidative phosphorylation based on the principle of least action

Novel molecular insights into ATP synthesis in oxidative phosphorylation based on the principle of least action

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  • NSTL
  • Elsevier
In previous papers in Chemical Physics Letters, the author has analyzed the coupled nonequilibrium processes of ATP synthesis in oxidative phosphorylation (OXPHOS) with succinate as substrate. It was shown experimentally that the system evolves with time to a minimum unit action of 1.4 x 10(-3) J s natom O-1 mg protein(-1). Here the experimental value of the average unit action is suitably normalized. It is shown that the average unit action per elementary ion (proton or anion/countercation) translocation event through the F-O portion of the FOF1-ATP synthase yields a value of 6.70 x 10(-34) J s. This is equal to the value of the Planck's constant, h to within 1%. The results provide a novel molecular interpretation of energy transduction by ATP synthase in OXPHOS under optimal conditions, linking it to a fundamental physical constant.

Adenosine triphosphateOxidative phosphorylation (OXPHOS)FOF1-ATP synthaseMolecular motorsComplex systemsMitchell's single-ion chemiosmotic theoryNath's two-ion theory of energy coupling and ATP synthesisNath's torsional mechanism of energy transduction and ATP synthesisIon translocation in membrane transportersIon-coupled transportMitochondrial countingSpectrophotometric measurement of pigment concentrationMinimum average unit actionPrinciple of least actionPlanck's constantMolecular implicationsVariational principleTORSIONAL MECHANISMRESPIRATORY-CHAINENERGY LANDSCAPESION-TRANSPORTSYNTHASEEFFICIENCY

Nath, Sunil

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Indian Inst Technol Delhi

2022

10.1016/j.cplett.2022.139561

Chemical Physics Letters

Chemical Physics Letters

EISCI
ISSN：0009-2614
年,卷(期)：2022.796
  • 80