The ATP-induced K(+)-transport pathway of yeast mitochondria may function as an uncoupling pathway.
The effect of the presence of K+ during oxidative phosphorylation measured on isolated yeast mitochondria was dependent on phosphate concentration. At 0.5 mM phosphate, K+ did promote an uncoupling of oxidative phosphorylation, which was prevented by decavanadate, a potent inhibitor of the ATP-induced K(+)-transport pathway. AT 5 mM phosphate, no uncoupling effect of K+ could be evidenced. These data suggest that the ATP-induced K(+)-transport pathway may, under certain conditions, function as an uncoupling pathway of oxidative phosphorylation.
Manon
S
S
Institut de Biochimie et de Génétique Cellulaire, Centre National de la Recherche Scientifique, Université de Bordeaux II, France. stephen.manon@ibgc.u-bordeaux2.fr
Guérin
M
M
D000255:Adenosine Triphosphate / Q000096:biosynthesis*; D017136:Ion Transport / Q000187:drug effects; D007700:Kinetics; D008634:Mersalyl / Q000494:pharmacology; D008928:Mitochondria / Q000187:drug effects / Q000378:metabolism*; D010085:Oxidative Phosphorylation; D010101:Oxygen Consumption / Q000187:drug effects; D010710:Phosphates / Q000378:metabolism; D011188:Potassium / Q000378:metabolism* / Q000494:pharmacology; D012441:Saccharomyces cerevisiae / Q000187:drug effects / Q000378:metabolism*; D014475:Uncoupling Agents / Q000494:pharmacology; D014638:Vanadates / Q000494:pharmacology
D010710:Phosphates; D014475:Uncoupling Agents; D014638:Vanadates; D008634:Mersalyl; D000255:Adenosine Triphosphate; D011188:Potassium