title: Proton diet for the sodium pump.
abstract: In the absence of Na(+) and K(+) ions the Na,K-ATPase shows a pH-dependent ATP hydrolysis that can be inhibited by ouabain. At pH 7.2 this activity is 5% of the maximal under physiological conditions. It could be inferred that this activity is associated with H(+) transport in both directions across the membrane and facilitates an H-only mode of the sodium pump under such unphysiological conditions. By the analysis of experiments with reconstituted proteoliposomes an overall electroneutral transport mode has been proven. The stoichiometry was determined to be 2 H(+)/2 H(+)/1 ATP and is comparable to what is known from the closely related H,K-ATPase. By time-resolved ATP-concentration jump experiments it was found that at no time was the third, Na(+)-specific binding site of the pump occupied by protons. A modified Post-Albers pump cycle is proposed, with H(+) ions as congeners for Na(+) and K(+), by which all experiments performed can be explained.
authors.affiliation: Department of Biology, University of Konstanz, 78464 Konstanz, Germany. h-j.apell@uni-konstanz.de
authors.forename: Hans-Jürgen
authors.initials: HJ
authors.lastname: Apell
authors.forename: Gabriela
authors.initials: G
authors.lastname: Benz
authors.forename: Daniel
authors.initials: D
authors.lastname: Sauerbrunn
mesh_terms: D000255:Adenosine Triphosphate / Q000737:chemistry / Q000378:metabolism; D001693:Biological Transport, Active; D006863:Hydrogen-Ion Concentration; D011188:Potassium / Q000737:chemistry / Q000378:metabolism; D011510:Proteolipids / Q000737:chemistry / Q000378:metabolism; D011522:Protons; D012964:Sodium / Q000737:chemistry / Q000378:metabolism; D000254:Sodium-Potassium-Exchanging ATPase / Q000737:chemistry* / Q000378:metabolism
chemical_list: D011510:Proteolipids; D011522:Protons; C020485:proteoliposomes; D000255:Adenosine Triphosphate; D012964:Sodium; D000254:Sodium-Potassium-Exchanging ATPase; D011188:Potassium