Báo cáo khoa học: A point mutation in the ATP synthase of Rhodobacter capsulatus results in differential contributions of DpH and Du in driving the ATP synthesis reaction
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The interface between thec-subunit oligomer and the asubunit in the F0sector of the ATP synthase is believed to formthe core of the rotatingmotor powered by the protonic ¯ow. Besides the essential cAsp61 and aArg210 residues (Escherichia colinumbering), a few other residues at this interface, although nonessential, show a high degree of conservation, among these aGlu219.
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