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  P3[2-(4-hydroxyphenyl)-2-oxo]ehtyl ATP for the Rapid Activation of the Na+, K+-ATPase

Geibel, S., Barth, A., Amslinger, S., Jung, A. H., Burzik, C., Clarke, R. J., et al. (2000). P3[2-(4-hydroxyphenyl)-2-oxo]ehtyl ATP for the Rapid Activation of the Na+, K+-ATPase. Biophysical Journal, 79(3), 1346-1357. doi:10.1016/S0006-3495(00)76387-9.

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 Creators:
Geibel, Sven1, Author           
Barth, Andreas2, Author
Amslinger, Sabine3, Author
Jung, Andreas H.3, Author
Burzik, Christiane1, Author           
Clarke, Ronald J.1, Author           
Givens, Richard S.3, Author
Fendler, Klaus1, Author           
Affiliations:
1Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society, ou_2068289              
2Institut für Biophysik, Johann Wolfgang Goethe-Universität, D-60590 Frankfurt/Main, Germany, ou_persistent22              
3Department of Chemistry, University of Kansas, Lawrence, Kansas 66045 USA, ou_persistent22              

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 Abstract: P3-[2-(4-hydroxyphenyl)-2-oxo]ethyl ATP (pHP-caged ATP) has been investigated for its application as a phototrigger for the rapid activation of electrogenic ion pumps. The yield of ATP after irradiation with a XeCl excimer laser (λ = 308 nm) was determined at pH 6.0–7.5. For comparison, the photolytic yields of P3-[1-(2-nitrophenyl)]ethyl ATP (NPE-caged ATP) and P3-[1,2-diphenyl-2-oxo]ethyl ATP (desyl-caged ATP) were also measured. It was shown that at λ = 308 nm pHP-caged ATP is superior to the other caged ATP derivatives investigated in terms of yield of ATP after irradiation. Using time-resolved single-wavelength IR spectroscopy, we determined a lower limit of 106 s−1 for the rate constant of release of ATP from pHP-caged ATP at pH 7.0. Like NPE-caged ATP, pHP-caged ATP and desyl-caged ATP bind to the Na+,K+-ATPase and act as competitive inhibitors of ATPase function. Using pHP-caged ATP, we investigated the charge translocation kinetics of the Na+,K+-ATPase at pH 6.2–7.4. The kinetic parameters obtained from the electrical measurements are compared to those obtained with a technique that does not require caged ATP, namely parallel stopped-flow experiments using the voltage-sensitive dye RH421. It is shown that the two techniques yield identical results, provided the inhibitory properties of the caged compound are taken into account. Our results demonstrate that under physiological (pH 7.0) and slightly basic (pH 7.5) or acidic (pH 6.0) conditions, pHP-caged ATP is a rapid, effective, and biocompatible phototrigger for ATP-driven biological systems.

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Language(s): eng - English
 Dates: 2000-06-082000-01-242000-06-082009-01-062000-09-01
 Publication Status: Issued
 Pages: 12
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/S0006-3495(00)76387-9
PMID: 10968997
PMC: PMC1301029
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Title: Biophysical Journal
  Other : Biophys. J.
Source Genre: Journal
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Publ. Info: Cambridge, Mass. : Cell Press
Pages: - Volume / Issue: 79 (3) Sequence Number: - Start / End Page: 1346 - 1357 Identifier: ISSN: 0006-3495
CoNE: https://pure.mpg.de/cone/journals/resource/954925385117