Toward an Understanding of Ion Transport through the Na,K-ATPase

Apell, Hans-Jürgen

Toward an Understanding of Ion Transport through the Na,K-ATPase

Dateien

Toward_an_Understanding_of_Ion_Transport.pdfGröße: 189 KBDownloads: 398

Datum

2003

Open Access-Veröffentlichung

Open Access Green

Sammlungen

Biologie

Publikationstyp

Zeitschriftenartikel

Publikationsstatus

Published

Erschienen in

Annals of the New York Academy of Science. 2003, 986(1), pp. 133-140. ISSN 0077-8923. eISSN 1749-6632. Available under: doi: 10.1111/j.1749-6632.2003.tb07150.x

Zusammenfassung

In the Na,K-ATPase the charge-translocating reaction steps were found to be binding of the third Na+ ion to the cytoplasmic side and the release of all three Na+ ions to the extracellular side as well as binding of the two K+ ions on the extracellular side. The conformation transition E1 -> E2 was only of minor electrogenicity; all other reaction steps produced no significant charge movements. In the SR Ca-ATPase and the gastric H,K-ATPase, all ionbinding and -release steps were identified to move charge through the membrane. The high-resolution structure of the SR Ca-ATPase in state E1 revealed the position of the ion-binding sites in the transmembrane part of the protein. If the same arrangement is assumed for the Na pump, the missing expected charge movements in state E1 may to be assumed to be apparent effects. With the proposal that binding of 2 Na+ or 2 K+ is compensated correspondingly by H+ ions, agreement between structural and functional aspects is obtained. Investigations of the pH-dependence of ion-binding steps indicate competition between the ions and electrogenic H+ binding in support of this concept.

Fachgebiet (DDC)

570 Biowissenschaften, Biologie

Schlagwörter

binding sites, ion transport, pH effects, electrogenicity, styryl dyes, fluorescence, competitive inhibition of ion binding

Zitieren

ISO 690

APELL, Hans-Jürgen, 2003. Toward an Understanding of Ion Transport through the Na,K-ATPase. In: Annals of the New York Academy of Science. 2003, 986(1), pp. 133-140. ISSN 0077-8923. eISSN 1749-6632. Available under: doi: 10.1111/j.1749-6632.2003.tb07150.x

BibTex

@article{Apell2003Towar-7918,
  year={2003},
  doi={10.1111/j.1749-6632.2003.tb07150.x},
  title={Toward an Understanding of Ion Transport through the Na,K-ATPase},
  number={1},
  volume={986},
  issn={0077-8923},
  journal={Annals of the New York Academy of Science},
  pages={133--140},
  author={Apell, Hans-Jürgen}
}

RDF

<rdf:RDF
    xmlns:dcterms="http://purl.org/dc/terms/"
    xmlns:dc="http://purl.org/dc/elements/1.1/"
    xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#"
    xmlns:bibo="http://purl.org/ontology/bibo/"
    xmlns:dspace="http://digital-repositories.org/ontologies/dspace/0.1.0#"
    xmlns:foaf="http://xmlns.com/foaf/0.1/"
    xmlns:void="http://rdfs.org/ns/void#"
    xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > 
  <rdf:Description rdf:about="https://kops.uni-konstanz.de/server/rdf/resource/123456789/7918">
    <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/>
    <dcterms:rights rdf:resource="http://creativecommons.org/licenses/by-nc-nd/2.0/"/>
    <dspace:hasBitstream rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/7918/1/Toward_an_Understanding_of_Ion_Transport.pdf"/>
    <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dc:rights>Attribution-NonCommercial-NoDerivs 2.0 Generic</dc:rights>
    <dc:language>eng</dc:language>
    <dc:contributor>Apell, Hans-Jürgen</dc:contributor>
    <dc:creator>Apell, Hans-Jürgen</dc:creator>
    <dcterms:hasPart rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/7918/1/Toward_an_Understanding_of_Ion_Transport.pdf"/>
    <dcterms:abstract xml:lang="eng">In the Na,K-ATPase the charge-translocating reaction steps were found to be binding of the third Na+ ion to the cytoplasmic side and the release of all three Na+ ions to the extracellular side as well as binding of the two K+ ions on the extracellular side. The conformation transition E1 -&gt; E2 was only of minor electrogenicity; all other reaction steps produced no significant charge movements. In the SR Ca-ATPase and the gastric H,K-ATPase, all ionbinding and -release steps were identified to move charge through the membrane. The high-resolution structure of the SR Ca-ATPase in state E1 revealed the position of the ion-binding sites in the transmembrane part of the protein. If the same arrangement is assumed for the Na pump, the missing expected charge movements in state E1 may to be assumed to be apparent effects. With the proposal that binding of 2 Na+ or 2 K+ is compensated correspondingly by H+ ions, agreement between structural and functional aspects is obtained. Investigations of the pH-dependence of ion-binding steps indicate competition between the ions and electrogenic H+ binding in support of this concept.</dcterms:abstract>
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:38:30Z</dc:date>
    <dcterms:bibliographicCitation>First publ. in: Annals of the New York Academy of Science 986 (2003), pp. 133-140</dcterms:bibliographicCitation>
    <dc:format>application/pdf</dc:format>
    <dcterms:issued>2003</dcterms:issued>
    <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:38:30Z</dcterms:available>
    <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/7918"/>
    <dcterms:title>Toward an Understanding of Ion Transport through the Na,K-ATPase</dcterms:title>
    <foaf:homepage rdf:resource="http://localhost:8080/"/>
  </rdf:Description>
</rdf:RDF>

Universitätsbibliographie

Ja