Nature 459, 364-370 (21 May 2009) | doi:10.1038/nature08145; Published online 20 May 2009
Review Article
Torque generation and elastic power transmission in the rotary FOF1-ATPase
Wolfgang Junge1, Hendrik Sielaff1,2 & Siegfried Engelbrecht1,3
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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.
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