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* Department of Biochemistry, Weill Graduate School of Medical Sciences, Cornell University, New York, New York 10021; and
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06520
Correspondence: Address reprint requests to Lise Heginbotham, Dept. of Molecular Biophysics and Biochemistry, PO Box 208114, Yale University, New Haven, CT 06520. Tel.: 203-432-9803; Fax: 203-432-5175; E-mail: lise.heginbotham{at}yale.edu.
Intracellular tetraethylammonium (TEA) inhibition was studied at the single-channel level in the KcsA potassium channel reconstituted in planar lipid bilayers. TEA acts as a fast blocker (resulting in decreased current amplitude) with an affinity in the 75 mM range even at high bandwidth. Studies over a wide voltage range reveal that TEA block has a complex voltage-dependence that also depends on the ionic conditions. These observations are examined in the context of permeation models to extend our understanding of the coupling between permeant ions and TEA blockade.
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