Publikation:

Localization of Ubiquinone-8 in the Na+-pumping NADH:Quinone Oxidoreductase from Vibrio cholerae

Lade...
Vorschaubild

Dateien

Casutt_212755.pdf
Casutt_212755.pdfGröße: 979.77 KBDownloads: 387

Datum

2011

Autor:innen

Casutt, Marco S.
Wendelspiess, Severin
Vossler, Sara
Gerken, Uwe
Murai, Masatoshi
Miyoshi, Hideto
Steuber, Julia

Herausgeber:innen

Kontakt

ISSN der Zeitschrift

Electronic ISSN

ISBN

Bibliografische Daten

Verlag

Schriftenreihe

Auflagebezeichnung

ArXiv-ID

Internationale Patentnummer

Angaben zur Forschungsförderung

Projekt

Open Access-Veröffentlichung
Open Access Green
Core Facility der Universität Konstanz

Gesperrt bis

Titel in einer weiteren Sprache

Publikationstyp
Zeitschriftenartikel
Publikationsstatus
Published

Erschienen in

Journal of Biological Chemistry. 2011, 286(46), pp. 40075-40082. ISSN 0021-9258. eISSN 1083-351X. Available under: doi: 10.1074/jbc.M111.224980

Zusammenfassung

Na + is the second major coupling ion at membranes after protons, and many pathogenic bacteria use the sodium-motive force to their advantage. A prominent example is Vibrio cholerae, which relies on the Na+ -pumping NADH:quinone oxidoreductase (Na + -NQR) as the first complex in its respiratory chain. The Na + -NQR is a multisubunit, membrane-embedded NADH dehydrogenase that oxidizes NADH and reduces quinone to quinol. Existing models describing redox-driven Na + translocation by the Na + -NQR are based on the assumption that the pump contains four flavins and one FeS cluster. Here we show that the large, peripheral NqrA subunit of the Na + -NQR binds one molecule of ubiquinone-So Investigations of the dynamic interaction of NqrA with quinones by surface plasmon resonance and saturation transfer difference NMR reveal a high affinity, which is determined by the methoxy groups at the C-2 and C-3 positions of the quinone headgroup. Using photoactivatable quinone derivatives, it is demonstrated that ubiquinone-S bound to NqrA occupies a functional site. A novel scheme of electron transfer in Na + -NQR is proposed that is initiated by NADH oxidation on sub unit NqrF and leads to quinol formation on subunit NqrA.

Zusammenfassung in einer weiteren Sprache

Fachgebiet (DDC)
540 Chemie

Schlagwörter

Konferenz

Rezension
undefined / . - undefined, undefined

Forschungsvorhaben

Organisationseinheiten

Zeitschriftenheft

Zugehörige Datensätze in KOPS

Zitieren

ISO 690CASUTT, Marco S., Ruslan NEDIELKOV, Severin WENDELSPIESS, Sara VOSSLER, Uwe GERKEN, Masatoshi MURAI, Hideto MIYOSHI, Heiko M. MÖLLER, Julia STEUBER, 2011. Localization of Ubiquinone-8 in the Na+-pumping NADH:Quinone Oxidoreductase from Vibrio cholerae. In: Journal of Biological Chemistry. 2011, 286(46), pp. 40075-40082. ISSN 0021-9258. eISSN 1083-351X. Available under: doi: 10.1074/jbc.M111.224980
BibTex
@article{Casutt2011-11-18Local-21275,
  year={2011},
  doi={10.1074/jbc.M111.224980},
  title={Localization of Ubiquinone-8 in the Na<sup>+</sup>-pumping NADH:Quinone Oxidoreductase from Vibrio cholerae},
  number={46},
  volume={286},
  issn={0021-9258},
  journal={Journal of Biological Chemistry},
  pages={40075--40082},
  author={Casutt, Marco S. and Nedielkov, Ruslan and Wendelspiess, Severin and Vossler, Sara and Gerken, Uwe and Murai, Masatoshi and Miyoshi, Hideto and Möller, Heiko M. and Steuber, Julia}
}
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/123456789/21275">
    <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/29"/>
    <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/21275"/>
    <dspace:hasBitstream rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/21275/1/Casutt_212755.pdf"/>
    <dc:contributor>Nedielkov, Ruslan</dc:contributor>
    <dcterms:rights rdf:resource="https://rightsstatements.org/page/InC/1.0/"/>
    <foaf:homepage rdf:resource="http://localhost:8080/"/>
    <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/29"/>
    <dc:contributor>Miyoshi, Hideto</dc:contributor>
    <dc:creator>Steuber, Julia</dc:creator>
    <dc:creator>Gerken, Uwe</dc:creator>
    <dc:creator>Wendelspiess, Severin</dc:creator>
    <dcterms:hasPart rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/21275/1/Casutt_212755.pdf"/>
    <dc:contributor>Murai, Masatoshi</dc:contributor>
    <dc:contributor>Vossler, Sara</dc:contributor>
    <dc:contributor>Möller, Heiko M.</dc:contributor>
    <dc:contributor>Gerken, Uwe</dc:contributor>
    <dc:rights>terms-of-use</dc:rights>
    <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/>
    <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2013-01-30T08:13:18Z</dcterms:available>
    <dc:contributor>Wendelspiess, Severin</dc:contributor>
    <dc:creator>Möller, Heiko M.</dc:creator>
    <dc:creator>Nedielkov, Ruslan</dc:creator>
    <dcterms:abstract xml:lang="eng">Na + is the second major coupling ion at membranes after protons, and many pathogenic bacteria use the sodium-motive force to their advantage. A prominent example is Vibrio cholerae, which relies on the Na+ -pumping NADH:quinone oxidoreductase (Na + -NQR) as the first complex in its respiratory chain. The Na + -NQR is a multisubunit, membrane-embedded NADH dehydrogenase that oxidizes NADH and reduces quinone to quinol. Existing models describing redox-driven Na + translocation by the Na + -NQR are based on the assumption that the pump contains four flavins and one FeS cluster. Here we show that the large, peripheral NqrA subunit of the Na + -NQR binds one molecule of ubiquinone-So Investigations of the dynamic interaction of NqrA with quinones by surface plasmon resonance and saturation transfer difference NMR reveal a high affinity, which is determined by the methoxy groups at the C-2 and C-3 positions of the quinone headgroup. Using photoactivatable quinone derivatives, it is demonstrated that ubiquinone-S bound to NqrA occupies a functional site. A novel scheme of electron transfer in Na + -NQR is proposed that is initiated by NADH oxidation on sub unit NqrF and leads to quinol formation on subunit NqrA.</dcterms:abstract>
    <dcterms:issued>2011-11-18</dcterms:issued>
    <dc:creator>Casutt, Marco S.</dc:creator>
    <dc:creator>Murai, Masatoshi</dc:creator>
    <dcterms:title>Localization of Ubiquinone-8 in the Na&lt;sup&gt;+&lt;/sup&gt;-pumping NADH:Quinone Oxidoreductase from Vibrio cholerae</dcterms:title>
    <dc:contributor>Casutt, Marco S.</dc:contributor>
    <dc:contributor>Steuber, Julia</dc:contributor>
    <dcterms:bibliographicCitation>Journal of Biological Chemistry ; 286 (2011), 46. - S. 40075-40082</dcterms:bibliographicCitation>
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2013-01-30T08:13:18Z</dc:date>
    <dc:creator>Miyoshi, Hideto</dc:creator>
    <dc:language>eng</dc:language>
    <dc:creator>Vossler, Sara</dc:creator>
  </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
Ja
Begutachtet
Diese Publikation teilen