ATP synthesis by the F1Fo ATP synthase of Escherichia coli is obligatorily dependent on the electric potential.

Abstract

The H+-translocating F1Fo ATP synthase of Escherichia coli was purified and reconstituted into proteoliposomes. This system catalyzed ATP synthesis when energized by an acid/base transition (pHin = 5.0; pHout = 8.3) with succinate, malonate or maleinate but not with MES as the acidic buffer. Under these experimental conditions an electric potential of 125… (More)

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