Probing the Extracellular Access Channel of the Na,K-ATPase

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GRADINARU, Robert V., Hans-Jürgen APELL, 2015. Probing the Extracellular Access Channel of the Na,K-ATPase. In: Biochemistry. 54(15), pp. 2508-2519. ISSN 0006-2960. eISSN 1520-4995. Available under: doi: 10.1021/acs.biochem.5b00182

@article{Gradinaru2015Probi-31503, title={Probing the Extracellular Access Channel of the Na,K-ATPase}, year={2015}, doi={10.1021/acs.biochem.5b00182}, number={15}, volume={54}, issn={0006-2960}, journal={Biochemistry}, pages={2508--2519}, author={Gradinaru, Robert V. and Apell, Hans-Jürgen} }

Probing the Extracellular Access Channel of the Na,K-ATPase Apell, Hans-Jürgen 2015 Apell, Hans-Jürgen Gradinaru, Robert V. When the Na,K-ATPase pumps at each turnover two K<sup>+</sup> ions into the cytoplasm, this translocation consists of several reaction steps. First, the ions diffuse consecutively from the extracellular phase through an access pathway to the binding sites where they are coordinated. In the next step, the enzyme is dephosphorylated and the ions are occluded inside the membrane domain. The subsequent transition to the E<sub>1</sub> conformation produces a deocclusion of the binding sites to the cytoplasmic side of the membrane and allows in the last steps ion dissociation and diffusion to the aqueous phase. The interaction and competition of K<sup>+</sup> with various quaternary organic ammonium ions have been used to gain insight into the molecular mechanism of the ion binding process from the extracellular side in the P-E<sub>2</sub> conformation of the enzyme. Using the electrochromic styryl dye RH421, evidence has been obtained that the access pathway consists of a wide and water-filled funnel-like part that is accessible also for bulky cations such as the benzyltriethylammonium ion, and a narrow part that permits passage only of small cations such as K<sup>+</sup> and NH4<sup>+</sup> in a distinct electrogenic way. Benzyltriethylammonium ions inhibit K<sup>+</sup> binding in a competitive manner that can be explained by a stopper-like function at the interface between the wide and narrow parts of the access pathway. In contrast to other quaternary organic ammonium ions, benzyltriethylammonium ions show a specific binding to the ion pump in a position inside the access pathway where it blocks effectively the access to the binding sites. eng Gradinaru, Robert V. 2015-07-27T14:38:51Z 2015-07-27T14:38:51Z

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