Thermodynamic marking of FOF1 ATP synthase

Biochim Biophys Acta Bioenerg. 2021 Apr 1;1862(4):148369. doi: 10.1016/j.bbabio.2021.148369. Epub 2021 Jan 14.

Abstract

FOF1 ATP synthase is a ~100% efficient molecular machine for energy conversion in biology, and holds great lessons for man-made energy technology and nanotechnology. In light of formidable biocomplexity of the FOF1 machinery, its modeling from pure physical principles remains difficult and rare. Here we construct a thermodynamic model of FOF1 from experimentally accessible quantities plus a single entropy production that generally has vanishingly small values (<1kB). Based on the physical inputs, this model captures FOF1 performance observed over an exhaustively wide range of proton-motive force and nucleotide concentrations. The model predicts a distinct 1/8kBT slope for ATP synthesis rate versus proton-motive force, which is verified by experimental data and represents a profound thermodynamic marking of this amazingly efficient machine operating near a universal limit of the 2nd law of thermodynamics. The model further predicts two symmetries of heat productions, which are testable by available experimental techniques and offer quantitative constraints on FOF1's possible mechanisms behind its ~100% efficiency.

Keywords: ATP; Directionality; Entropy; F(O)F(1); Molecular motors; Proton-motive force.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphate / chemistry*
  • Models, Chemical*
  • Proton-Translocating ATPases / chemistry*
  • Thermodynamics

Substances

  • Adenosine Triphosphate
  • Proton-Translocating ATPases