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From the Department of Biophysical Sciences, State University of New York at Buffalo, Buffalo, New York 14214
The kinetic properties of main and subconductance states of a mutant mouse N-methyl-D-aspartate
(NMDA) receptor channel were examined. Recombinant receptors made of 
-
2 (NR1-NR2B) subunits having asparagine-to-glutamine mutations in the M2 segment (N598Q /2N589Q) were expressed in Xenopus oocytes. Single channel currents recorded from outside-out patches were analyzed using hidden Markov model techniques. In
Ca2+-free solutions, an open receptor channel occupies a main conductance (93 pS) and a subconductance (62 pS) with about equal probability. There are both brief and long-lived subconductance states, but only a single
main level state. At 
80 mV, the lifetime of the main and the longer-lived sub level are both ~3.3 ms. The gating of the pore and the transition between conductance levels are essentially independent processes. Surprisingly, hyperpolarization speeds both the sub-to-main and main-to-sub transition rate constants (~120 mV/e-fold change),
but does not alter the equilibrium occupancies. Extracellular Ca2+ does not influence the transition rate constants. We conclude that the subconductance levels arise from fluctuations in the energetics of ion permeation
through a single pore, and that the voltage dependence of these fluctuations reflects the modulation by the membrane potential of the barrier between the main and subconductance conformations of the pore.
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