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Dipolar Relaxation Dynamics at the Active Site of an ATPase Regulated by Membrane Lateral Pressure
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SYSNO ASEP 0471291 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Dipolar 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 authors 6 Source Title Angewandte Chemie - International Edition. - : Wiley - ISSN 1433-7851
Roč. 56, č. 5 (2017), s. 1269-1272Number of pages 4 s. Language eng - English Country DE - Germany Keywords fluorescence ; ion pump ; membrane proteins ; nanodiscs ; time-resolved emission Subject RIV CF - Physical ; Theoretical Chemistry OECD category Physical chemistry R&D Projects GBP208/12/G016 GA ČR - Czech Science Foundation (CSF) Institutional support UFCH-W - RVO:61388955 UT WOS 000394997700014 EID SCOPUS 85007324122 DOI https://doi.org/10.1002/anie.201611582 Annotation The 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. Workplace J. Heyrovsky Institute of Physical Chemistry Contact Michaela Knapová, michaela.knapova@jh-inst.cas.cz, Tel.: 266 053 196 Year of Publishing 2018
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