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Dipolar Relaxation Dynamics at the Active Site of an ATPase Regulated by Membrane Lateral Pressure

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    SYSNO ASEP0471291
    Document TypeJ - Journal Article
    R&D Document TypeJournal Article
    Subsidiary JČlánek ve WOS
    TitleDipolar Relaxation Dynamics at the Active Site of an ATPase Regulated by Membrane Lateral Pressure
    Author(s) Fischermeier, E. (DE)
    Pospíšil, Petr (UFCH-W)
    Sayed, A. (DE)
    Hof, Martin (UFCH-W) RID, ORCID
    Solioz, M. (CH)
    Fahmy, K. (DE)
    Number of authors6
    Source TitleAngewandte Chemie - International Edition. - : Wiley - ISSN 1433-7851
    Roč. 56, č. 5 (2017), s. 1269-1272
    Number of pages4 s.
    Languageeng - English
    CountryDE - Germany
    Keywordsfluorescence ; ion pump ; membrane proteins ; nanodiscs ; time-resolved emission
    Subject RIVCF - Physical ; Theoretical Chemistry
    OECD categoryPhysical chemistry
    R&D ProjectsGBP208/12/G016 GA ČR - Czech Science Foundation (CSF)
    Institutional supportUFCH-W - RVO:61388955
    UT WOS000394997700014
    EID SCOPUS85007324122
    DOI10.1002/anie.201611582
    AnnotationThe active transport of ions across biological membranes requires their hydration shell to interact with the interior of membrane proteins. However, the influence of the external lipid phase on internal dielectric dynamics is hard to access by experiment. Using the octahelical transmembrane architecture of the copper-transporting P1B-type ATPase from Legionella pneumophila as a model structure, we have established the site-specific labeling of internal cysteines with a polarity-sensitive fluorophore. This enabled dipolar relaxation studies in a solubilized form of the protein and in its lipid-embedded state in nanodiscs. Time-dependent fluorescence shifts revealed the site-specific hydration and dipole mobility around the conserved ion-binding motif. The spatial distribution of both features is shaped significantly and independently of each other by membrane lateral pressure.
    WorkplaceJ. Heyrovsky Institute of Physical Chemistry
    ContactMichaela Knapová, michaela.knapova@jh-inst.cas.cz, Tel.: 266 053 196
    Year of Publishing2018
Number of the records: 1  

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