Kinetic models of coupling between H+ and Na(+)-translocation and ATP synthesis/hydrolysis by F0F1-ATPases: can a cell utilize both delta mu H+ and delta mu Na+ for ATP synthesis under in vivo conditions using the same enzyme?
Kinetic models of the F0F1-ATPase able to transport H+ or/and Na+ ions are proposed. It is assumed that (i) H+ and Na+ compete for the same binding sites, (ii) ion translocation through F0 is coupled to the rate-limiting step of the F1-catalyzed reaction. The main characteristics of the dependences of ATP synthesis and hydrolysis rates on delta psi, delta pH, and delta pNa are predicted for various versions of the coupling model. The mechanism of the switchover from delta mu H(+)-dependent synthesis to the delta mu Na(+)-dependent one is demonstrated. It is shown that even with a drastic drop in delta mu H+, ATP hydrolysis by the proton mode of catalysis can be effectively inhibited by delta psi and delta pNa. The results obtained strongly support the possibility that the same F0F1-ATPase in bacterial cells can utilize both delta muH+ and delta muNa+ for ATP synthesis under in vivo conditions.
Kholodenko
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A. N. Belozersky Institute of Physicochemical Biology, Moscow State University, Russia.
D000255:Adenosine Triphosphate / Q000378:metabolism*; D001426:Bacterial Proteins / Q000378:metabolism; D002384:Catalysis; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D007700:Kinetics; D008954:Models, Biological; D010085:Oxidative Phosphorylation; D017494:Proton Pumps; D006180:Proton-Translocating ATPases / Q000378:metabolism*; D011522:Protons; D000254:Sodium-Potassium-Exchanging ATPase
D001426:Bacterial Proteins; D017494:Proton Pumps; D011522:Protons; D000255:Adenosine Triphosphate; D006180:Proton-Translocating ATPases; D000254:Sodium-Potassium-Exchanging ATPase