In rate-theory analysis of ion transport in channels, the energy of binding sites and the height of activation barriers are usually considered to be time-independent and not influenced by the movement of the ion. The assumption of a fixed barrier structure seems questionable, however, in view of the fact that proteins may exist in a large number of conformational states and may rapidly move from one state to the other. In this study, some of the effects of multiple conformational states of a channel on ion transport are analyzed. In the first part of the paper, the ion permeability of a channel with n binding sites is treated on the assumption that interconversion of channel states is much faster than ion transfer between binding sites. Under this condition, the form of the flux equation remains the same as for a channel with fixed barriers, provided that the rate constants for ion jumps are replaced by weighted averages over the rate constants for the individual conformational states. In the second part, a channel with two (main) barriers and a single (main) binding site is considered, with the rates of conformational transitions being arbitrary. This case, in particular, includes the situation where a jump of the ion is followed by a slow transition to a more polarized state of the binding site. Under this condition, the conductance of the channel exhibits a nonlinear dependence on ion concentration which is different from a simple saturation behavior. Under non-stationary conditions damped oscillations may occur.