(1) Department of Biochemistry and Biophysics, University of Rochester Medical Center, Rochester, New York
Abstract:
Four positively-charged residues, namely βLys-155, βArg-182, βArg-246, and αArg-376 have been identified as Pi binding residues
in Escherichia coli ATP synthase. They form a triangular Pi binding site in catalytic site βE where substrate Pi initially binds for ATP synthesis
in oxidative phosphorylation. Positive electrostatic charge in the vicinity of βArg-246 is shown to be one important component
of Pi binding.