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Significance of charged residues in the catalytic sites of Escherichia coli ATP synthase

F1Fo ATP synthase, the smallest biological nanomotor, is the fundamental means of cellular energy production in almost all living systems. Oxidative or photophosphorylation in membranes of bacteria, mitochondria, and chloroplasts generates ATP from ADP and Pi (inorganic phosphate). The molecular mechanism of ATP synthase and generation of ATP depends on the designated catalytic site residues. We have been interested in identifying the specific Pi binding residues in the cyclical process of binding change mechanism. So far we have investigated eleven residues, βArg‐246, βAsn‐243, αArg‐376, βLys‐155, βArg‐182, αPhe‐291, αSer‐347, αThr‐349, αIle‐346, αIle‐348, and αGly‐351 based their proximity to the phosphate analogs AlF3 or SO42− in x‐ray structures of catalytic sites. We suspect that many other catalytic site residues including highly conserved αVISIT‐DG sequence residue αAsp‐350 plays important functional role in the catalytic sites.