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Torque generation and elastic power transmission in the rotary FOF1-ATPase

Author

Listed:
  • Wolfgang Junge

    (University of Osnabrück)

  • Hendrik Sielaff

    (University of Osnabrück
    Present address: Institute of Biophysics, University of Ulm, 89081 Ulm, Germany.)

  • Siegfried Engelbrecht

    (University of Osnabrück
    Present address: Department of Biochemistry, University of Osnabrück, 49076 Osnabrück, Germany.)

Abstract

Adenosine triphosphate (ATP), the universal fuel of the cell, is synthesized from adenosine diphosphate (ADP) and inorganic phosphate (Pi) by 'ATP synthase' (FOF1-ATPase). During respiration or photosynthesis, an electrochemical potential difference of protons is set up across the respective membranes. This powers the enzyme's electrical rotary nanomotor (FO), which drives the chemical nanomotor (F1) by elastic mechanical-power transmission, producing ATP with high kinetic efficiency. Attempts to understand in detail the mechanisms of torque generation in this simple and robust system have been both aided and complicated by a wealth of sometimes conflicting data.

Suggested Citation

  • Wolfgang Junge & Hendrik Sielaff & Siegfried Engelbrecht, 2009. "Torque generation and elastic power transmission in the rotary FOF1-ATPase," Nature, Nature, vol. 459(7245), pages 364-370, May.
    • Handle: RePEc:nat:nature:v:459:y:2009:i:7245:d:10.1038_nature08145
    DOI: 10.1038/nature08145
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    Cited by:

    1. Jiyao Song & Liesa Steidle & Isabelle Steymans & Jasjot Singh & Anne Sanner & Lena Böttinger & Dominic Winter & Thomas Becker, 2023. "The mitochondrial Hsp70 controls the assembly of the F1FO-ATP synthase," Nature Communications, Nature, vol. 14(1), pages 1-15, December.

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