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  The Kdp-ATPase of Escherichia coli mediates an ATP-dependent, K+-independent electrogenic partial reaction

Fendler, K., Dröse, S., Epstein, W., Bamberg, E., & Altendorf, K. (1999). The Kdp-ATPase of Escherichia coli mediates an ATP-dependent, K+-independent electrogenic partial reaction. Biochemistry, 38(6), 1850-1856. doi:10.1021/bi982238u.

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 Creators:
Fendler, Klaus1, Author           
Dröse, Stefan2, Author
Epstein, Wolfgang3, Author
Bamberg, Ernst1, Author           
Altendorf, Karlheinz 2, Author
Affiliations:
1Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society, ou_2068289              
2Fachbereich Biologie/Chemie, Universität Osnabrück, 49069 Osnabrück, Germany, ou_persistent22              
3Department of Molecular Genetics and Cell Biology, University of Chicago, Illinois 60637, USA, ou_persistent22              

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Free keywords: Biological transport; Ions; Membranes; Charge transport; Electrical conductivity
 Abstract: Charge transport by the K+ transporting Kdp-ATPase from Escherichiacoli was investigated using planar lipid membranes to which liposomes reconstituted with the enzyme were adsorbed. To study reactions in the absence of K+, given some contamination of solutions with K+, we used a mutant of Kdp whose affinity for K+ was 6 mM instead of the wild-type whose affinity is 2 μM. Upon rapid release of ATP from caged ATP, a transient current occurred in the absence of K+. In the presence of K+, a stationary current was seen. On the basis of their structural similarity, we propose a kinetic model for the Kdp-ATPase analogous to that of the Na+K+-ATPase. In this model, the first, K+-independent step is electrogenic and corresponds to the outward transport of a negative charge. The second, K+-translocating step is probably also electrogenic and corresponds to transport of positive charge to the intracellular side of the protein.

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Language(s): eng - English
 Dates: 1989-11-201989-09-171999-01-231999-02-01
 Publication Status: Issued
 Pages: 7
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1021/bi982238u
PMID: 10026265
 Degree: -

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Title: Biochemistry
Source Genre: Journal
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Publ. Info: Columbus, Ohio : American Chemical Society
Pages: - Volume / Issue: 38 (6) Sequence Number: - Start / End Page: 1850 - 1856 Identifier: ISSN: 0006-2960
CoNE: https://pure.mpg.de/cone/journals/resource/954925384103