[Model of proton-potassium transport systems].
Previous experimental results are discussed. It was shown that two H+--K+-exchange systems operate in the E. coli membranes and that they can be stopped by N,N'-dicyclohexylcarbodiimide. Either of the two systems is assumed to include the ATPase complex F1 x F0 that has relation to the exchange of 2H+ from the cell for K+ of the medium, another system includes as a portion the ionic channel F0. The aim of the paper is to present the current evidence about intramembrane interplay between the fluxes of H+ and K+ during the operation of F1 x F0 and about the lack of the relationship between these fluxes via electrochemical potential differences.
D000251:Adenosine Triphosphatases / Q000378:metabolism; D001693:Biological Transport, Active / Q000187:drug effects; D002462:Cell Membrane / Q000187:drug effects / Q000378:metabolism; D004024:Dicyclohexylcarbodiimide / Q000494:pharmacology; D004926:Escherichia coli / Q000187:drug effects / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008954:Models, Biological; D010086:Oxidative Phosphorylation Coupling Factors / Q000378:metabolism; D011188:Potassium / Q000378:metabolism*; D006180:Proton-Translocating ATPases
D010086:Oxidative Phosphorylation Coupling Factors; D004024:Dicyclohexylcarbodiimide; D000251:Adenosine Triphosphatases; D006180:Proton-Translocating ATPases; D011188:Potassium
Model' protono-kalievykh transportnykh sistem.