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  2. School of Engineering
  3. Publikationen
  4. Publikationen School of Engineering
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dc.contributor.authorKastner, C.-
dc.contributor.authorPrummer, M.-
dc.contributor.authorSick, Beate-
dc.contributor.authorRenn, A.-
dc.contributor.authorWild, U.P.-
dc.contributor.authorDimroth, P.-
dc.date.accessioned2018-12-20T09:12:54Z-
dc.date.available2018-12-20T09:12:54Z-
dc.date.issued2003-
dc.identifier.issn1542-0086de_CH
dc.identifier.issn0006-3495de_CH
dc.identifier.urihttps://digitalcollection.zhaw.ch/handle/11475/14038-
dc.descriptionContent available via Elsevier Open Archivede_CH
dc.description.abstractA prominent region of the Naþ-dependent citrate carrier (CitS) from Klebsiella pneumoniae is the highly conserved loop X-XI, which contains a putative citrate binding site. To monitor potential conformational changes within this region by single-molecule fluorescence spectroscopy, the target cysteines C398 and C414 of the single-Cys mutants (CitSsC398, CitS-sC414) were selectively labelled with the thiol-reactive fluorophores AlexaFluor 546/568 C5 maleimide (AF546, AF568). While both single-cysteine mutants were catalytically active citrate carriers, labelling with the fluorophore was only tolerated at C398. Upon citrate addition to the functional protein fluorophore conjugate CitS-sC398-AF546, complete fluorescence quenching of the majority of molecules was observed, indicating a citrate-induced conformational change of the fluorophore-containing domain of CitS. This quenching was specific for the physiological substrate citrate and therefore most likely reflecting a conformational change in the citrate transport mechanism. Single-molecule studies with dual-labelled CitSsC398-AF546/568 and dual-color detection provided strong evidence for a homodimeric association of CitS.de_CH
dc.language.isoende_CH
dc.publisherCell Pressde_CH
dc.relation.ispartofBiophysical Journalde_CH
dc.rightsLicence according to publishing contractde_CH
dc.subjectOpticsde_CH
dc.subjectMembrane proteinde_CH
dc.subjectSingle moleculede_CH
dc.subjectBiologyde_CH
dc.subject.ddc572: Biochemiede_CH
dc.titleThe citrate carrier CitS probed by single-molecule fluorescence spectroscopyde_CH
dc.typeBeitrag in wissenschaftlicher Zeitschriftde_CH
dcterms.typeTextde_CH
zhaw.departementSchool of Engineeringde_CH
zhaw.organisationalunitInstitut für Datenanalyse und Prozessdesign (IDP)de_CH
dc.identifier.doi10.1016/S0006-3495(03)74974-1de_CH
zhaw.funding.euNode_CH
zhaw.issue3de_CH
zhaw.originated.zhawNode_CH
zhaw.pages.end1659de_CH
zhaw.pages.start1651de_CH
zhaw.publication.statuspublishedVersionde_CH
zhaw.volume84de_CH
zhaw.publication.reviewPeer review (Publikation)de_CH
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Kastner, C., Prummer, M., Sick, B., Renn, A., Wild, U. P., & Dimroth, P. (2003). The citrate carrier CitS probed by single-molecule fluorescence spectroscopy. Biophysical Journal, 84(3), 1651–1659. https://doi.org/10.1016/S0006-3495(03)74974-1
Kastner, C. et al. (2003) ‘The citrate carrier CitS probed by single-molecule fluorescence spectroscopy’, Biophysical Journal, 84(3), pp. 1651–1659. Available at: https://doi.org/10.1016/S0006-3495(03)74974-1.
C. Kastner, M. Prummer, B. Sick, A. Renn, U. P. Wild, and P. Dimroth, “The citrate carrier CitS probed by single-molecule fluorescence spectroscopy,” Biophysical Journal, vol. 84, no. 3, pp. 1651–1659, 2003, doi: 10.1016/S0006-3495(03)74974-1.
KASTNER, C., M. PRUMMER, Beate SICK, A. RENN, U.P. WILD und P. DIMROTH, 2003. The citrate carrier CitS probed by single-molecule fluorescence spectroscopy. Biophysical Journal. 2003. Bd. 84, Nr. 3, S. 1651–1659. DOI 10.1016/S0006-3495(03)74974-1
Kastner, C., M. Prummer, Beate Sick, A. Renn, U.P. Wild, and P. Dimroth. 2003. “The Citrate Carrier CitS Probed by Single-Molecule Fluorescence Spectroscopy.” Biophysical Journal 84 (3): 1651–59. https://doi.org/10.1016/S0006-3495(03)74974-1.
Kastner, C., et al. “The Citrate Carrier CitS Probed by Single-Molecule Fluorescence Spectroscopy.” Biophysical Journal, vol. 84, no. 3, 2003, pp. 1651–59, https://doi.org/10.1016/S0006-3495(03)74974-1.


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