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Figure 8. (A) A simple kinetic scheme for Kir6.2ΔC26 channel gating in ATP-free solution, where O is the open state, C1 represents the short closed state observed within a burst of openings, and C2 represents the long closed state that governs the interburst duration. The dotted line represents the rate constant affected by the C166S mutation. (B) Voltage dependence of the rate constants k1, k−1, k2, and k−2 in the absence of ATP, calculated for Kir6.2ΔC26-C166S currents (n = 3). The rate constants were calculated from measured values of τo, τC1, Po, and percent C2. The lines are fitted to the equation k = a + ko exp (zδVF/RT), where ko is the rate constant at a membrane potential of 0 mV, V is the membrane potential, zδ is a term describing the electrical distance through the membrane, and a is a voltage-independent component. (C) Values of the parameters used to fit the voltage dependence of the rate constants shown in B. Image published in: Trapp S et al. (1998) Image reproduced on Xenbase with permission of the publisher and the copyright holder. This image is reproduced with permission of the journal and the copyright holder. This is an open-access article distributed under the terms of the Creative Commons Attribution-NonCommercial-ShareAlike license Larger Image Printer Friendly View

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