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Bulletin of the Korean Chemical Society (BKCS)

ISSN 0253-2964(Print)
ISSN 1229-5949(Online)
Volume 32, Number 2
BKCSDE 32(2)
February 20, 2011 

Observation of Asymmetry amongst Nucleotide Binding Sites of F1-ATPase of Escherichia coli by 31P NMR Spectroscopy
Namkung Jun, Joon Hyung Sohn, Byung Il Yeh, Jong Whan Choi, Hyun Won Kim*
31P NMR spectroscopy, F1-ATPase of Escherichia coli, Asymmetry, Nucleotide binding site
It was regarded that the 31P resonances of inherent nucleotides in F1-ATPase (EF1), as large as 380KDa, could not be observed by 31P NMR spectroscopy. However, our 31P NMR spectroscopy could differentiate between different nucleotide binding sites on EF1 from Escherichia coli. When EF1 was prepared in the absence of Mg2+, EF1 contained only ADP. Multiple 31P resonances from β-phosphates of ADP bound to the EF1 were observed from the enzyme prepared without Mg2+, suggesting asymmetry or flexibility amongst nucleotide binding sites. 31P resonances from enzyme bound ATP could be observed only from EF1, when the enzyme was prepared in the presence of Mg2+. This Mg2+ dependent ATP binding was very tight that, once bound, nucleotide could not be removed even after removal of Mg2+. 31P NMR proved to be a valuable tool for investigating phosphorous related enzymes.
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