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  Proton transport through a peptide-tethered bilayer lipid membrane by the H+-ATP synthase from chloroplasts measured by impedance spectroscopy

Naumann, R., Baumgart, T., Graber, P., Jonczyk, A., Offenhäusser, A., & Knoll, W. (2002). Proton transport through a peptide-tethered bilayer lipid membrane by the H+-ATP synthase from chloroplasts measured by impedance spectroscopy. Biosensors & Bioelectronics, 17(1-2), 25-34.

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 Creators:
Naumann, Renate1, Author           
Baumgart, T.1, Author           
Graber, P., Author
Jonczyk, A., Author
Offenhäusser, Andreas1, Author           
Knoll, Wolfgang1, Author           
Affiliations:
1MPI for Polymer Research, Max Planck Society, ou_1309545              

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Free keywords: H+-ATP synthase; proton transport; thiolipopeptide; surface plasmon resonance spectroscopy impedance spectroscopy; fluorescence microscopy; tethered lipid membrane
 Abstract: A lipid membrane was tethered to a gold film by a peptide spacer molecule terminated by a sulfhydryl group. Membranes were formed by fusion of liposomes prepared from egg phosphatidylcholine on self assembled monolayers of the thiolipopeptide Myr-Lys(Myr)-Ser-Ser-Pro-Ala-Ser-Ser-Ala-Ala- Ser-Ala-Cys-amide mixed with mercaptoethanol as a diluent molecule or lateral spacer. These mixed films, although not representing a perfect lipid bilayer, have been shown to retain the activity of incorporated H+-ATP synthases from chloroplasts in contrast to films prepared from the pure thiolipopeptide. The activity of the protein was demonstrated by impedance spectroscopy. The resistance decreased due to proton transport across the lipid film, which occurs as a consequence of adenosine triphosphate (ATP) hydrolysis. Several effects previously determined from kinetic measurements of the enzyme reconstituted in liposomes such as saturation with respect to the substrate (ATP), inhibition by venturicidin, activation by a positive potential pulse and increase of the proton current as a function of increasingly negative potentials have been confirmed also for this tethered membrane system. Changes in the impedance spectra due to the addition of ATP were fully reversible. (C) 2002 Elsevier Science B.V. All rights reserved.

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Language(s): eng - English
 Dates: 2002-01
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: No review
 Identifiers: eDoc: 28298
ISI: 000173263200004
Other: P-02-13
 Degree: -

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Title: Biosensors & Bioelectronics
  Alternative Title : Biosens. Bioelectron.
Source Genre: Journal
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Pages: - Volume / Issue: 17 (1-2) Sequence Number: - Start / End Page: 25 - 34 Identifier: ISSN: 0956-5663