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  Electrogenic K+ Transport by the Kdp-ATPase of Escherichia coli

Fendler, K., Dröse, S., Altendorf, K., & Bamberg, E. (1996). Electrogenic K+ Transport by the Kdp-ATPase of Escherichia coli. Biochemistry, 35(24), 8009-8017. doi:10.1021/bi960175e.

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Genre: Journal Article

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 Creators:
Fendler, Klaus1, Author              
Dröse, Stefan2, Author
Altendorf, Karlheinz2, Author
Bamberg, Ernst1, Author              
Affiliations:
1Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society, ou_2068289              
2Universität Osnabrück, Fachbereich Biologie/Chemie, 49069 Osnabrück, Germany, ou_persistent22              

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Free keywords: Vesicles; Peptides and proteins; Ions; Membranes; Electrical conductivity
 Abstract: Charge translocation by the Kdp-ATPase of Escherichia coli was measured by adsorption of proteoliposomes to a planar lipid membrane. The proteoliposomes were prepared by reconstitution of purified Kdp-ATPase into liposomes prepared from E. coli lipids. The protein was activated by a ATP concentration jump produced by photolysis of a protected derivative of ATP, caged ATP. Charge translocation was measured with a time resolution of 15−40 ms. Stationary currents demonstrated the continuous pumping activity of the enzyme. Control measurements with the potential-sensitive dye DiSC3(5) showed a negative potential inside the proteoliposomes after activation with ATP. The measured electrical signals as well as the dye measurements correspond to the transport of positive charge to the intracellular face of the protein. The electrical signal was increased when K+ was inside the proteoliposomes (K0.5 ≈ 50 μM) and was inhibited by vanadate. These experiments demonstrate the electrogeneity of the Kdp-ATPase in a purified reconstituted system.

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Language(s): eng - English
 Dates: 1996-04-041996-01-241996-06-181996
 Publication Status: Published in print
 Pages: 9
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1021/bi960175e
 Degree: -

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Title: Biochemistry
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Columbus, Ohio : American Chemical Society
Pages: - Volume / Issue: 35 (24) Sequence Number: - Start / End Page: 8009 - 8017 Identifier: ISSN: 0006-2960
CoNE: https://pure.mpg.de/cone/journals/resource/954925384103