Effect of the proton electrochemical gradient on maleimide inactivation of active transport in Escherichia coli membrane vesicles.

Many active transport systems present in Escherichia coli membrane vesicles are inhibited by maleimides and other sulfhydryl reagents. These reagents do not interfere with the oxidation of reduced phenazine methosulfate or with the electrochemical proton gradient (delta muH+). The rate of inactivation is increased in the presence of reduced phenazine methosulfate, and it is shown that the electrochemical proton gradient is responsible for the effect. Furthermore, similar effects observed with the proline and melibiose transport systems. Thus, it appears that either the reactivity or accessibility of a sulfhydryl group(s) in each of these carriers is altered by the presence of a transmembrane delta muH+. The findings are consistent with the notion that delta muH+, in addition to acting as the immediate driving force the active transport, may bring about structural or conformational changes in certain membrane proteins that catalyze active transport.