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  Probing Membrane Protein Conformations with an Extrinsic Fluorophore

Lewitzki, E., Schick, E., Brand, K., Hutterer, R., Schneider, F., & Grell, E. (1995). Probing Membrane Protein Conformations with an Extrinsic Fluorophore. In J. C. Merlin, S. Turrell, & J. P. Huvenne (Eds.), Spectroscopy of Biological Molecules (pp. 409-410). Dordrecht: Springer Science+Business Media.

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Item Permalink: https://hdl.handle.net/21.11116/0000-0008-282D-A Version Permalink: https://hdl.handle.net/21.11116/0000-0008-282E-9
Genre: Conference Paper

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 Creators:
Lewitzki, Erwin1, Author           
Schick, Eginhard1, Author           
Brand, K.2, Author
Hutterer, R.2, Author
Schneider, F.W.2, Author
Grell, Ernst1, Author           
Affiliations:
1Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society, ou_2068289              
2University of Würzburg, Institute of Physical Chemistry, Würzburg, Germany, ou_persistent22              

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 Abstract: Upon hydrolysis of ATP the integral membrane protein Na,K-ATPase actively transports the cations Na+ and K+ across its membrane. According to earlier kinetic studies, this pumping activity against the existing concentration gradient has been characterized in terms of two major conformational states of the enzyme that have been denoted E1 (Na+-bound state) and E2 (K+-bound state) [1,2]. Since it is difficult to separate the ATP binding process, which is assumed to lead to the formation of E1 in the presence of Na+, from the subsequent hydrolytic reaction steps considerable interest has been devoted to the investigation of molecules mimiking the binding of the substrate. A molecule exhibiting such features as well as fluorescence properties that are sensitive to changes in its local environment is eosin Y (Fig. 1), introduced by M. Esmann and J.C. Skou [3]. Up to now binding of the negatively charged eosin Y has been interpreted in terms of an interaction with the enzyme induced primarily by Na+. This interaction can be characterized by a time-resolvable fluorescence intensity increase employing the stopped flow technique [4,5]. This intensity increase in the millisecond time range has been attributed to a conformational change leading to the state E1.

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Language(s): eng - English
 Dates: 1995
 Publication Status: Issued
 Pages: 2
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1007/978-94-011-0371-8_188
 Degree: -

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Title: 6th European Conference on the Spectroscopy of Biological Molecules
Place of Event: Villeneuve d’Ascq, France
Start-/End Date: 1995-09-03 - 1995-09-08

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Title: Spectroscopy of Biological Molecules
Source Genre: Proceedings
 Creator(s):
Merlin, Jean Claude1, Editor
Turrell, Sylvia1, Editor
Huvenne, Jean Pierre1, Editor
Affiliations:
1 Laboratoire de Spectrochimie, Infrarouge et Raman, CNRS, UST Lille, Villeneuve d’Ascq, France, ou_persistent22            
Publ. Info: Dordrecht : Springer Science+Business Media
Pages: 626 Volume / Issue: - Sequence Number: - Start / End Page: 409 - 410 Identifier: DOI: 10.1007/978-94-011-0371-8
ISBN: 978-0-7923-3628-0
ISBN: 978-94-011-0371-8