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

Fischermeier, Elisabeth; Pospíšil, Petr; Sayed, Ahmed; Hof, Martin; Solioz, Marc; Fahmy, Karim (2017). Dipolar Relaxation Dynamics at the Active Site of an ATPase Regulated by Membrane Lateral Pressure. Angewandte Chemie (International ed.), 56(5), pp. 1269-1272. Wiley-VCH 10.1002/anie.201611582

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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.

Item Type:

Journal Article (Original Article)

Division/Institute:

04 Faculty of Medicine > Pre-clinic Human Medicine > BioMedical Research (DBMR) > DBMR Forschung Mu35 > Forschungsgruppe Hepatologie
04 Faculty of Medicine > Pre-clinic Human Medicine > BioMedical Research (DBMR) > DBMR Forschung Mu35 > Forschungsgruppe Hepatologie

04 Faculty of Medicine > Pre-clinic Human Medicine > BioMedical Research (DBMR)

UniBE Contributor:

Solioz, Marc

Subjects:

600 Technology > 610 Medicine & health

ISSN:

1433-7851

Publisher:

Wiley-VCH

Language:

English

Submitter:

Lilian Karin Smith-Wirth

Date Deposited:

14 Jul 2017 12:36

Last Modified:

14 Jul 2017 12:36

Publisher DOI:

10.1002/anie.201611582

PubMed ID:

28026092

Uncontrolled Keywords:

fluorescence; ion pump; membrane proteins; nanodiscs; time-resolved emission

BORIS DOI:

10.7892/boris.93607

URI:

https://boris.unibe.ch/id/eprint/93607

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