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It was regarded that the resonances of inherent nucleotides in -ATPase (EF1), as large as 380KDa, could not be observed by NMR spectroscopy. However, our NMR spectroscopy could differentiate between different nucleotide binding sites on EF1 from Escherichia coli. When EF1 was prepared in the absence of , EF1 contained only ADP. Multiple resonances from -phosphates of ADP bound to the EF1 were observed from the enzyme prepared without , suggesting asymmetry or flexibility amongst nucleotide binding sites. resonances from enzyme bound ATP could be observed only from EF1, when the enzyme was prepared in the presence of . This dependent ATP binding was very tight that, once bound, nucleotide could not be removed even after removal of . NMR proved to be a valuable tool for investigating phosphorous related enzymes.

Observation of Asymmetry amongst Nucleotide Binding Sites of F1-ATPase of Escherichia coli by31P NMR Spectroscopy

Observation of Asymmetry amongst Nucleotide Binding Sites of F₁-ATPase of Escherichia coli by³¹P NMR Spectroscopy