Mar 5, 1976

A non-equilibrium thermodynamics analysis of active transport within the framework of the chemiosotic theory

Biochimica Et Biophysica Acta
A E Lagarde


The proton circuit devised by Mitchell in the chemiosmotic theory was subjected to analysis using the formalism of irreversible thermodynamics. The phenomenological coefficients and the degree of coupling relating co-permeant flows were derived from anion/H+, substrate/H+, cation/H+ and anion/anion biporter models. Linearity and equality of the cross-coefficients in Onsager relations were always satisfied. Macroscopic flows leading to charges splitting, such as oxido-reduction, hydro-dehydratation and transhydrogenase, are driven by a composite thermodynamic force which includes the proton-motive component. Multiple coupling occurs in the circuit when it is assumed that the net inward flux of protons becomes zero, i.e. when the circulation of protons reaches a stationary state. Under these conditions, oxidative phosphorylation, ATPase- or respiration-linked transhydrogenase and uptake of anion or cation against their electrochemical gradient may be predicted, in agreement with known experimental evidence.

  • References2
  • Citations4


  • References2
  • Citations4

Mentioned in this Paper

Adenosine Triphosphatases
Cell Respiration
Oxidative Phosphorylation
Respiratory Gaseous Exchange in Organisms
NADP Transhydrogenase
Membranes, Artificial

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