ATP synthase-mediated proton fluxes and phosphorylation in rat liver mitochondria: dependence on delta mu H.
The dependence of the proton flux through the ATP synthases of rat liver mitochondria on a driving force composed mainly of a potassium diffusion potential was determined and compared with the relationship between rate of phosphorylation and delta mu H given by titrations with the respiratory inhibitor malonate. The two functions are in good agreement in the lower part of the delta mu H range covered. However, the maximal proton fluxes through the ATP synthases are much lower than needed to account for the rate of State 3 phosphorylation sustained by the same mitochondria oxidizing succinate. Possible reasons for this behavior are discussed.
Zoratti
M
M
Petronilli
V
V
Azzone
G F
GF
D000818:Animals; D004058:Diffusion; D008314:Malonates / Q000378:metabolism; D008433:Mathematics; D008930:Mitochondria, Liver / Q000187:drug effects / Q000378:metabolism*; D008956:Models, Chemical; D009994:Osmolar Concentration; D010085:Oxidative Phosphorylation; D010766:Phosphorylation; D011188:Potassium / Q000378:metabolism; D006180:Proton-Translocating ATPases / Q000378:metabolism*; D011522:Protons; D051381:Rats; D013386:Succinates / Q000378:metabolism; D019802:Succinic Acid; D014634:Valinomycin / Q000494:pharmacology
D008314:Malonates; D011522:Protons; D013386:Succinates; D014634:Valinomycin; C030290:malonic acid; D019802:Succinic Acid; D006180:Proton-Translocating ATPases; D011188:Potassium