Model of anion and monovalent cation transport as neutral ion pairs through lipophilic water channels of the Na,K ATPase complex.
A model of anion and monovalent cation transport through a lipophilic water channel of the Na,K ATPase complex is presented. Literature data for the Na,K ATPase cation binding sites are combined with data for the anion binding sites of Band 3 to obtain adjacent cation and anion combining sites at the inner and outer channel mouths. Cations and anions form neutral ion pairs or undissociated acids at these sites and then partition much more favorably into lipophilic channel water, passing through the channel in diffusive fashion. Cation movements in an "uphill" direction occur without an enzyme translocating moiety and its specific energetic requirement. The pertinent factors are the exclusion of unpaired cations by the tight channel and the site selectivity or pickup ratios for Na/K at each side which dominate over bulk and transmembrane concentration ratios. ATP hydrolysis provides phosphate for ion pairing.
Doonan
B
B
D000838:Anions / Q000378:metabolism*; D001665:Binding Sites; D001692:Biological Transport; D002414:Cations, Monovalent / Q000378:metabolism*; D007473:Ion Channels / Q000378:metabolism*; D008954:Models, Biological; D000254:Sodium-Potassium-Exchanging ATPase / Q000378:metabolism*
D000838:Anions; D002414:Cations, Monovalent; D007473:Ion Channels; D000254:Sodium-Potassium-Exchanging ATPase