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The Na + , Li + /H +  antiporter of  Escherichia coli  (Ec-NhaA) maintains pH, Na +  homeostasis in enterobacteria. We used isothermal titration calorimetry to perform a detailed thermodynamic analysis of Li +  binding to Ec-NhaA and several of its mutants. We found that, in line with the canonical alternative access mechanistic model of secondary transporters, Li + /H +  binding to the antiporter is antagonistically coupled. Binding of Li +  displaces 2 H +  from the binding site. The process is enthalpically driven, the enthalpic gain just compensating for an entropic loss and the buffer-associated enthalpic changes dominate the overall free-energy change. Li +  binding, H +  release and antiporter activity were all affected to the same extent by mutations in the Li +  binding site (D163E, D163N, D164N, D164E), while D133C changed the H + /Li +  stoichiometry to 4. Most striking, however, was the mutation, A167P, which converted the Ec-NhaA antagonistic binding into synergistic binding which is only known to occur in Cl − /H +  antiporter.

The Ec-NhaA antiporter switches from antagonistic to synergistic antiport upon a single point mutation