THe proton-per-electron stoicheiometry of 'site 1' of oxidative phosphorylation at high protonmotive force is close to 1.5.
The maximum redox potential difference between the NAD+/NADH couple and the succinate/fumarate couple generated during ATP-energized reduction of NAD+ by succinate in submitochondrial particles was measured, together with the electrochemical potential difference for protons (delta mu approximately H+). The presence of cyanide, the time-independence of the redox potential difference and the irrelevance of the initial redox state of the NAD+/NADH couple ensured that the experimental situation corresponded to a 'static-head condition' with delta mu approximately H+ as the input force and the redox potential difference as the output force, the flow of electrons having reached dynamic equilibrium. Consequently, the observed value of 1.6 for the ratio delta Ge/delta mu approximately H+ is interpreted as indicating that the leads to H+/e- stoicheiometry at 'site 1' is 1.5 and that therefore the mechanism of the proton pump at 'site 1' is not of the group-translocation type (no direct leads to e - leads to H+ coupling).
D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D002417:Cattle; D004579:Electron Transport; D066298:In Vitro Techniques; D008564:Membrane Potentials; D008928:Mitochondria / Q000378:metabolism*; D008954:Models, Biological; D009243:NAD / Q000378:metabolism; D010085:Oxidative Phosphorylation; D011522:Protons; D013367:Submitochondrial Particles / Q000378:metabolism*; D013386:Succinates / Q000378:metabolism; D019802:Succinic Acid; D013816:Thermodynamics
D011522:Protons; D013386:Succinates; D009243:NAD; D000255:Adenosine Triphosphate; D019802:Succinic Acid