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Investigation of charge translocation by ion pumps and carriers using caged substrates

MPS-Authors
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Fendler,  Klaus
Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;

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Hartung,  Klaus
Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;

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Nagel,  Georg
Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;

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Bamberg,  Ernst
Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Fendler, K., Hartung, K., Nagel, G., & Bamberg, E. (1998). Investigation of charge translocation by ion pumps and carriers using caged substrates. In G. Marriott (Ed.), Methods in Enzymology (pp. 289-306). Academic Press. doi:10.1016/S0076-6879(98)91020-5.


Cite as: https://hdl.handle.net/21.11116/0000-0007-A5B3-4
Abstract
Publisher Summary:
This chapter presents studies on the application of caged compounds to planar lipid membranes as well as on giant patches of heart cell membranes. The chapter gives a few examples of transport ATPases and carriers that have been investigated using caged substrates. The advantage of this approach is the high time resolution that allows the investigation of pre steady-state kinetics. A number of other ion-translocating ATPases are investigated in the chapter using caged ATP: the Ca-ATPase from sarcoplasmatic reticulum, the H,K-ATPase from stomach, the F0F1-ATPase from chloroplasts, and the Kdp-ATPase from the plasma membrane of Escherichia coli. In the case of caged ATP the time resolution is limited by the time constant of ATP release from the caged compound used in those studies. By working at a somewhat acidic pH (6.2), ATP is released rapidly enough to study most of the enzymatic reactions of interest.