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Ion Selectivity of the cytoplasmic binding sites of the Na,K-ATPase : I. sodium binding is associated with a conformational rearrangement

Ion Selectivity of the cytoplasmic binding sites of the Na,K-ATPase : I. sodium binding is associated with a conformational rearrangement

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SCHNEEBERGER, Anne, Hans-Jürgen APELL, 1999. Ion Selectivity of the cytoplasmic binding sites of the Na,K-ATPase : I. sodium binding is associated with a conformational rearrangement. In: Journal of Membrane Biology. 168(3), pp. 221-228. ISSN 0022-2631. eISSN 1432-1424

@article{Schneeberger1999Selec-7625, title={Ion Selectivity of the cytoplasmic binding sites of the Na,K-ATPase : I. sodium binding is associated with a conformational rearrangement}, year={1999}, doi={10.1007/s002329900511}, number={3}, volume={168}, issn={0022-2631}, journal={Journal of Membrane Biology}, pages={221--228}, author={Schneeberger, Anne and Apell, Hans-Jürgen} }

<rdf:RDF xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns:bibo="http://purl.org/ontology/bibo/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:dcterms="http://purl.org/dc/terms/" xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > <rdf:Description rdf:about="https://kops.uni-konstanz.de/rdf/resource/123456789/7625"> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:35:52Z</dc:date> <dcterms:bibliographicCitation>First publ. in: Journal of Membrane Biology 168 (1999), pp. 221-228</dcterms:bibliographicCitation> <dcterms:rights rdf:resource="https://creativecommons.org/licenses/by-nc-nd/2.0/legalcode"/> <dcterms:title>Ion Selectivity of the cytoplasmic binding sites of the Na,K-ATPase : I. sodium binding is associated with a conformational rearrangement</dcterms:title> <dcterms:issued>1999</dcterms:issued> <dcterms:abstract xml:lang="eng">To investigate Na+ binding to the ion-binding sites presented on the cytoplasmic side of the Na,KATPase, equilibrium Na+-titration experiments were performed using two fluorescent dyes, RH421¹ and FITC, to detect protein-specific actions. Fluorescence changes upon addition of Na+ in the presence of various Mg2+ concentrations were similar and could be fitted with a Hill function. The half-saturating concentrations and Hill coefficients determined were almost identical. As RH421 responds to binding of a Na+ ion to the third neutral site whereas FITC monitors conformational changes in the ATP-binding site or its environment, this result implies that electrogenic binding of the third Na+ ion is the trigger for a structural rearrangement of the ATP-binding moiety. This enables enzyme phosphorylation, which is accompanied by a fast occlusion of the Na+ ions and followed by the conformational transition E1/E2 of the protein. The coordinated action both at the ion and the nucleotide binding sites allows for the first time a detailed formulation of the mechanism of enzyme phosphorylation that occurs only when three Na+ ions are bound.</dcterms:abstract> <dc:creator>Schneeberger, Anne</dc:creator> <dc:creator>Apell, Hans-Jürgen</dc:creator> <dc:format>application/pdf</dc:format> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/7625"/> <dc:contributor>Apell, Hans-Jürgen</dc:contributor> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:35:52Z</dcterms:available> <dc:contributor>Schneeberger, Anne</dc:contributor> <dc:rights>deposit-license</dc:rights> <dc:language>eng</dc:language> </rdf:Description> </rdf:RDF>

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