Conformational Changes of Nucleotide Binding Sites Following Sequential Addition of ADP to Nucleotide-depleted F 1 -ATPase of Escherichia coli Investigated with 31 P NMR Spectroscopy

, Asymmetry,Nucleotide binding site Oxidative phosphorylation in Escherichia coli is catalyzedby an electron transport system that generates a protonelectrochemical gradient across the cytoplasmic membraneand an ATP synthase enzyme that catalyzes the conversionof ADP and Pi to ATP at the expense of a gradient ofsufficient magnitude. The ATP synthase of this organism isessentially identical in other bacteria, the mitochondria ofeukaryotes and the thylakoids of green plants.