Publikation:

Protonation of Ca2+ -ATPase Residues upon Ca2+ Release : [Abstracts of papers at the Fifty-Ninth Annual Meeting of the Society of General Physiologists]

Lade...
Vorschaubild

Dateien

Zu diesem Dokument gibt es keine Dateien.

Datum

2005

Autor:innen

Andersson, Julia
Barth, Andreas

Herausgeber:innen

Kontakt

ISSN der Zeitschrift

Electronic ISSN

ISBN

Bibliografische Daten

Verlag

Schriftenreihe

Auflagebezeichnung

DOI (zitierfähiger Link)
ArXiv-ID

Internationale Patentnummer

Angaben zur Forschungsförderung

Projekt

Open Access-Veröffentlichung
Core Facility der Universität Konstanz

Gesperrt bis

Titel in einer weiteren Sprache

Publikationstyp
Beitrag zu einem Konferenzband
Publikationsstatus
Published

Erschienen in

Journal of General Physiology. 2005. no.35

Zusammenfassung

We have studied protonation of the sarcoplasmic reticulum Ca2 -ATPase during Ca2 release and E2P formation (Ca2E1→E2P) using rapid scan Fourier transform infrared spectroscopy. The reaction has been investigated from pH 6.0 to 9.0. Infrared spectra show four signals in the spectral region of protonated carboxyl groups at pH 6.0–7.5 and only two at pH 8.0–9.0. The results show that at least two of the protonated carboxyl groups of E2P have a pK of 7.7. We have concluded that these carboxyl groups participate in H countertransport. To identify these carboxyl groups and to assign the IR bands, multiconformation continuum electrostatic calculations (MCCE) have been performed to calculate the residues’ ionization, at various pH, for the calcium-free and the calcium-occluded structure, respectively. The combination of infrared measurements and MCCE calculations clearly indicates that Asp800 is involved in the proton countertransport whereas Glu309 is not. The second carboxyl group involved in the countertransport might be Glu908. Our results also indicate a pH-dependent conformational change in a -sheet or turn structure of E2P. Additionally, we have tentatively assigned a band to the C O bond of the phosphorylated Asp 351. Based on infrared data, we concluded that the bond strength is essentially unchanged but is slightly reduced in E2P compared with Ca2E1P. This reduction is larger when Mg2 is bound to the aspartyl phosphate.

Zusammenfassung in einer weiteren Sprache

Fachgebiet (DDC)
570 Biowissenschaften, Biologie

Schlagwörter

Konferenz

Rezension
undefined / . - undefined, undefined

Forschungsvorhaben

Organisationseinheiten

Zeitschriftenheft

Zugehörige Datensätze in KOPS

Zitieren

ISO 690ANDERSSON, Julia, Karin HAUSER, Andreas BARTH, 2005. Protonation of Ca2+ -ATPase Residues upon Ca2+ Release : [Abstracts of papers at the Fifty-Ninth Annual Meeting of the Society of General Physiologists]. In: Journal of General Physiology. 2005. no.35
BibTex
@inproceedings{Andersson2005Proto-16479,
  year={2005},
  title={Protonation of Ca2+ -ATPase Residues upon Ca2+ Release : [Abstracts of papers at the Fifty-Ninth Annual Meeting of the Society of General Physiologists]},
  series={no.35},
  booktitle={Journal of General Physiology},
  author={Andersson, Julia and Hauser, Karin and Barth, Andreas}
}
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/123456789/16479">
    <dc:creator>Andersson, Julia</dc:creator>
    <dc:contributor>Hauser, Karin</dc:contributor>
    <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/29"/>
    <dcterms:bibliographicCitation>Publ. in: Journal of General Physiology ; 126 (2005), 1. - 1a-82a (no. 35)</dcterms:bibliographicCitation>
    <dc:contributor>Andersson, Julia</dc:contributor>
    <dc:rights>terms-of-use</dc:rights>
    <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/16479"/>
    <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/>
    <dcterms:title>Protonation of Ca2+ -ATPase Residues upon Ca2+ Release : [Abstracts of papers at the Fifty-Ninth Annual Meeting of the Society of General Physiologists]</dcterms:title>
    <dcterms:rights rdf:resource="https://rightsstatements.org/page/InC/1.0/"/>
    <dc:contributor>Barth, Andreas</dc:contributor>
    <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/29"/>
    <dcterms:abstract xml:lang="eng">We have studied protonation of the sarcoplasmic reticulum Ca2 -ATPase during Ca2  release and E2P formation (Ca2E1→E2P) using rapid scan Fourier transform infrared spectroscopy. The reaction has been investigated from pH 6.0 to 9.0. Infrared spectra show four signals in the spectral region of protonated carboxyl groups at pH 6.0–7.5 and only two at pH 8.0–9.0. The results show that at least two of the protonated carboxyl groups of E2P have a pK of  7.7. We have concluded that these carboxyl groups participate in H countertransport. To identify these carboxyl groups and to assign the IR bands, multiconformation continuum electrostatic calculations (MCCE) have been performed to calculate the residues’ ionization, at various pH, for the calcium-free and the calcium-occluded structure, respectively. The combination of infrared measurements and MCCE calculations clearly indicates that Asp800 is involved in the proton countertransport whereas Glu309 is not. The second carboxyl group involved in the countertransport might be Glu908. Our results also indicate a pH-dependent conformational change in a  -sheet or turn structure of E2P. Additionally, we have tentatively assigned a band to the C O bond of the phosphorylated Asp 351. Based on infrared data, we concluded that the bond strength is essentially unchanged but is slightly reduced in E2P compared with Ca2E1P. This reduction is larger when Mg2  is bound to the aspartyl phosphate.</dcterms:abstract>
    <dc:language>eng</dc:language>
    <foaf:homepage rdf:resource="http://localhost:8080/"/>
    <dc:creator>Hauser, Karin</dc:creator>
    <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2012-01-03T17:43:44Z</dcterms:available>
    <dc:creator>Barth, Andreas</dc:creator>
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2012-01-03T17:43:44Z</dc:date>
    <dcterms:issued>2005</dcterms:issued>
  </rdf:Description>
</rdf:RDF>

Interner Vermerk

xmlui.Submission.submit.DescribeStep.inputForms.label.kops_note_fromSubmitter

Kontakt
URL der Originalveröffentl.

Prüfdatum der URL

Prüfungsdatum der Dissertation

Finanzierungsart

Kommentar zur Publikation

Allianzlizenz
Corresponding Authors der Uni Konstanz vorhanden
Internationale Co-Autor:innen
Universitätsbibliographie
Nein
Begutachtet
Diese Publikation teilen