Kcv, isolated from a Chlorella virus, is the smallest known K+ channel. When Kcv is expressed in Xenopus oocytes and exposed to 50 mM [K+](o), its open-state current-voltage relationship (I-V) has the shape of a "tilted S'' between -200 and + 120 mV. Details of this shape depend on the conditioning voltage (Vc) immediately before an I-V recording. Unexpectedly, the I-V relationships, recorded in different [K+] o, do intersect. These characteristics are numerically described here by. ts of a kinetic model to the experimental data. In this model, the Vc sensitivity of I-V is mainly assigned to an affinity increase of external K+ association at more positive voltages. The general, tilted-S shape as well as the unexpected intersections of the I-V relationships are kinetically described by a decrease of the cord conductance by the electrochemical driving force for K+ in either direction, like in fast V-dependent blocking by competing ions.

Electrokinetics of miniature K+ channel: Open-state V sensitivity and inhibition by K+ driving force / S. Gazzarrini, A. Abenavoli, D. Gradmann, G. Thiel, A. Moroni. - In: THE JOURNAL OF MEMBRANE BIOLOGY. - ISSN 0022-2631. - 214:1-2(2006), pp. 9-17. [10.1007/s00232-006-0024-3]

Electrokinetics of miniature K+ channel: Open-state V sensitivity and inhibition by K+ driving force

S. Gazzarrini
Primo
;
A. Abenavoli
Secondo
;
A. Moroni
Ultimo
2006

Abstract

Kcv, isolated from a Chlorella virus, is the smallest known K+ channel. When Kcv is expressed in Xenopus oocytes and exposed to 50 mM [K+](o), its open-state current-voltage relationship (I-V) has the shape of a "tilted S'' between -200 and + 120 mV. Details of this shape depend on the conditioning voltage (Vc) immediately before an I-V recording. Unexpectedly, the I-V relationships, recorded in different [K+] o, do intersect. These characteristics are numerically described here by. ts of a kinetic model to the experimental data. In this model, the Vc sensitivity of I-V is mainly assigned to an affinity increase of external K+ association at more positive voltages. The general, tilted-S shape as well as the unexpected intersections of the I-V relationships are kinetically described by a decrease of the cord conductance by the electrochemical driving force for K+ in either direction, like in fast V-dependent blocking by competing ions.
Electrophysiology; Enzyme kinetics; K+ channel; Open state; Selectivity filter; Xenopus expression
Settore BIO/04 - Fisiologia Vegetale
2006
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2434/38442
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