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

Sohn, Joon-Hyung; Namkung, Jun; Yeh, Byung‐Il; Choi, Jong-Whan; Kim, Hyun-Won

doi:10.5012/bkcs.2011.32.3.1051

Bulletin of the Korean Chemical Society

2011

DOI: 10.5012/bkcs.2011.32.3.1051

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Conformational Changes of Nucleotide Binding Sites Following Sequential Addition of ADP to Nucleotide-depleted F₁-ATPase of Escherichia coli Investigated with³¹P NMR Spectroscopy

Joon-Hyung Sohn¹,

Jun Namkung²,

Byung‐Il Yeh³

et al.

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2012

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Catalytic Sites of F₁-ATPase from Escherichia coli was Investigated with GTP and GDP Titration Using³¹P NMR Spectroscopy

Kim¹,

Yeh²,

Choi³

et al. 2012

Bulletin of the Korean Chemical Society

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Oxidative phosphorylation in Escherichia coli is catalyzed by an electron transport system, which generates a proton electrochemical gradient across the cytoplasmic membrane and an ATP synthase enzyme, catalyzing the conversion of ADP and Pi to ATP at the expense of a gradient of sufficient magnitude. The ATP synthase of this organism is similar to other bacteria, the mitochondria of eukaryotes, and the thylakoids of green plants. [1][2][3][4][5][6][7] Two functionally distinct parts of the protein are: (i) the F 0 sector, comprised of three polypeptide chains known as a, b and c in forming a transmembrane proton channel, and (ii) F 1 sector, containing five polypeptide chains with relative stoichiometry α 3 β 3 γδε, in E. coli.Many investigations on F 1 -ATPases from diverse origins, bacteria, thylakoids and mitochondria, established that the composition of F 1 -ATPases comprised of three catalytic sites and a further set of non-catalytic sites.7,8 The non-catalytic sites had the characteristics of slow exchange of the bound ligand for ligands in the medium (t 1/2~h ours) with considerable specificity for adenine nucleotides. 2,5,6 In contrast, the catalytic sites were not adenine-specific and revealed rapid exchanges of bound ligand with ligands in the medium (t 1/2 ~ minutes). 5,9,10

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Catalytic Sites of F₁-ATPase from Escherichia coli was Investigated with GTP and GDP Titration Using³¹P NMR Spectroscopy

Kim¹,

Yeh²,

Choi³

et al. 2012

Bulletin of the Korean Chemical Society

Self Cite

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Conformational Changes of Nucleotide Binding Sites Following Sequential Addition of ADP to Nucleotide-depleted F₁-ATPase of Escherichia coli Investigated with³¹P NMR Spectroscopy

Cited by 1 publication

References 14 publications

Catalytic Sites of F₁-ATPase from Escherichia coli was Investigated with GTP and GDP Titration Using³¹P NMR Spectroscopy

Catalytic Sites of F₁-ATPase from Escherichia coli was Investigated with GTP and GDP Titration Using³¹P NMR Spectroscopy

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Conformational Changes of Nucleotide Binding Sites Following Sequential Addition of ADP to Nucleotide-depleted F1-ATPase of Escherichia coli Investigated with31P NMR Spectroscopy

Cited by 1 publication

References 14 publications

Catalytic Sites of F1-ATPase from Escherichia coli was Investigated with GTP and GDP Titration Using31P NMR Spectroscopy

Catalytic Sites of F1-ATPase from Escherichia coli was Investigated with GTP and GDP Titration Using31P NMR Spectroscopy

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Conformational Changes of Nucleotide Binding Sites Following Sequential Addition of ADP to Nucleotide-depleted F₁-ATPase of Escherichia coli Investigated with³¹P NMR Spectroscopy

Catalytic Sites of F₁-ATPase from Escherichia coli was Investigated with GTP and GDP Titration Using³¹P NMR Spectroscopy

Catalytic Sites of F₁-ATPase from Escherichia coli was Investigated with GTP and GDP Titration Using³¹P NMR Spectroscopy