Proton diet for the sodium pump

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Biochemistry. 2011, 50(3), pp. 409-418. ISSN 0006-2960. eISSN 1520-4995. Available under: doi: 10.1021/bi101576s
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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 withH þ 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 þ -specific binding site of the pump occupied by protons.Amodified Post-Albers pump cycle is proposed, with H+ ions as congeners for Na+ and K+, by which all experiments performed can be explained.

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ISO 690APELL, Hans-Jürgen, Gabriela BENZ, Daniel SAUERBRUNN, 2011. Proton diet for the sodium pump. In: Biochemistry. 2011, 50(3), pp. 409-418. ISSN 0006-2960. eISSN 1520-4995. Available under: doi: 10.1021/bi101576s
BibTex
@article{Apell2011-01-25Proto-14095,
  year={2011},
  doi={10.1021/bi101576s},
  title={Proton diet for the sodium pump},
  number={3},
  volume={50},
  issn={0006-2960},
  journal={Biochemistry},
  pages={409--418},
  author={Apell, Hans-Jürgen and Benz, Gabriela and Sauerbrunn, Daniel}
}
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    <dcterms:abstract xml:lang="eng">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 withH þ 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 þ -specific binding site of the pump occupied by protons.Amodified Post-Albers pump cycle is proposed, with H+ ions as congeners for Na+ and K+, by which all experiments performed can be explained.</dcterms:abstract>
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