Energy Equivalence of Information in the Mitochondrion and the Thermodynamic Efficiency of ATP Synthase

Biochemistry. 2015 Sep 1;54(34):5376-8. doi: 10.1021/acs.biochem.5b00834. Epub 2015 Aug 17.

Abstract

Half a century ago, Johnson and Knudsen resolved the puzzle of the apparent low efficiency of the kidney (∼ 0.5%) compared to most other bodily organs (∼ 40%) by taking into account the entropic cost of ion sorting, the principal function of this organ. Similarly, it is shown that the efficiency of energy transduction of the chemiosmotic proton-motive force by ATP synthase is closer to 90% instead of the oft-quoted textbook value of only 60% when information theoretic considerations are applied to the mitochondrion. This high efficiency is consistent with the mechanical energy transduction of ATP synthase known to be close to the 100% thermodynamic limit. It would have been wasteful for evolution to maximize the mechanical energy transduction to 100% while wasting 40% of the chemiosmotic free energy in the conversion of the proton-motive force into mechanical work before being captured as chemical energy in adenosine 5'-triphosphate.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Review

MeSH terms

  • Adenosine Triphosphate / biosynthesis
  • Animals
  • Energy Metabolism
  • Humans
  • Kidney / metabolism
  • Mitochondria / metabolism
  • Mitochondrial Proton-Translocating ATPases / chemistry*
  • Mitochondrial Proton-Translocating ATPases / metabolism*
  • Models, Biological
  • Proton-Motive Force
  • Thermodynamics

Substances

  • Adenosine Triphosphate
  • Mitochondrial Proton-Translocating ATPases