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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 zeta-epsilon 2 (NR1-NR2B) subunits having asparagine-to-glutamine mutations in the M2 segment (zeta N598Q/epsilon 2N589Q) were expressed in Xenopus oocytes. Single channel currents recorded from outside-out patches were analyzed using hidden Markov model techniques. In Ca(2+)-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 approximately 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 (approximately 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.

Subconductance States of a Mutant NMDA Receptor Channel Kinetics, Calcium, and Voltage Dependence