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Volumn 43, Issue 4, 2004, Pages 1054-1064

Binding of the b-Subunit in the ATP Synthase from Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINETRIPHOSPHATE; AMINO ACIDS; DATA REDUCTION; DIMERIZATION; DISSOCIATION; ENERGY TRANSFER; ESCHERICHIA COLI; FLUORESCENCE; FREE ENERGY; SYNTHESIS (CHEMICAL);

EID: 0942301383     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0357098     Document Type: Article
Times cited : (41)

References (47)
  • 1
    • 0032311441 scopus 로고    scopus 로고
    • ATP synthase - Past and future
    • Boyer, P. D. (1998) ATP synthase - past and future, Biochim. Biophys. Acta 1365, 3-9.
    • (1998) Biochim. Biophys. Acta , vol.1365 , pp. 3-9
    • Boyer, P.D.1
  • 5
    • 0027492268 scopus 로고
    • The binding change mechanism for ATP synthase - Some probabilities and possibilities
    • Boyer, P. D. (1993) The binding change mechanism for ATP synthase - some probabilities and possibilities, Biochim. Biophys. Acta 1140, 215-250.
    • (1993) Biochim. Biophys. Acta , vol.1140 , pp. 215-250
    • Boyer, P.D.1
  • 8
    • 0030863908 scopus 로고    scopus 로고
    • ATP synthase: An electrochemical transducer with rotatory mechanics
    • Engelbrecht, S., and Junge, W. (1997) ATP synthase: an electrochemical transducer with rotatory mechanics, FEBS Lett. 414, 485-491.
    • (1997) FEBS Lett. , vol.414 , pp. 485-491
    • Engelbrecht, S.1    Junge, W.2
  • 11
    • 0037063327 scopus 로고    scopus 로고
    • 1-ATP synthase observed by intramolecular single-molecule fluorescence resonance energy transfer
    • 1-ATP synthase observed by intramolecular single-molecule fluorescence resonance energy transfer, FEBS Lett. 527, 147-152.
    • (2002) FEBS Lett. , vol.527 , pp. 147-152
    • Börsch, M.1    Diez, M.2    Zimmermann, B.3    Reuter, R.4    Gräber, P.5
  • 16
    • 0033538506 scopus 로고    scopus 로고
    • Novel features in the structure of bovine ATP synthase
    • Karrasch, S., and Walker, J. E. (1999) Novel features in the structure of bovine ATP synthase, J. Mol. Biol. 290, 379-384.
    • (1999) J. Mol. Biol. , vol.290 , pp. 379-384
    • Karrasch, S.1    Walker, J.E.2
  • 17
  • 18
    • 0033609081 scopus 로고    scopus 로고
    • Energy transduction in the sodium F-ATPase of Propionigenium modestum
    • Dimroth, P., Wang, H., Grabe, M., and Oster, G. (1999) Energy transduction in the sodium F-ATPase of Propionigenium modestum, Proc. Natl. Acad. Sci. U.S.A. 96, 4924-4929.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 4924-4929
    • Dimroth, P.1    Wang, H.2    Grabe, M.3    Oster, G.4
  • 19
    • 0038584352 scopus 로고    scopus 로고
    • 3 as determined by fluorescence correlation spectroscopy
    • 3 as determined by fluorescence correlation spectroscopy, Biochemistry 38, 13759-13765.
    • (1999) Biochemistry , vol.38 , pp. 13759-13765
    • Häsler, K.1    Pänke, O.2    Junge, W.3
  • 21
    • 0032502352 scopus 로고    scopus 로고
    • 2δ complex from Escherichia coli ATP synthase
    • 2δ complex from Escherichia coli ATP synthase, J. Biol. Chem. 273, 8646-8651.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8646-8651
    • Dunn, S.D.1    Chandler, J.2
  • 22
    • 0032491567 scopus 로고    scopus 로고
    • 1 via an α-subunit in the Escherichia coli ATP synthase
    • 1 via an α-subunit in the Escherichia coli ATP synthase, J. Biol. Chem. 273, 29406-29410.
    • (1998) J. Biol. Chem. , vol.273 , pp. 29406-29410
    • Rodgers, A.J.1    Capaldi, R.A.2
  • 23
    • 0034625459 scopus 로고    scopus 로고
    • Site-directed cross-linking of b to the α, β, and a subunits of the Escherichia coli ATP synthase
    • McLachlin, D. T., Coveny, A. M., Clark, S. M., and Dunn, S. D. (2000) Site-directed cross-linking of b to the α, β, and a subunits of the Escherichia coli ATP synthase, J. Biol. Chem. 275, 17571-17577.
    • (2000) J. Biol. Chem. , vol.275 , pp. 17571-17577
    • McLachlin, D.T.1    Coveny, A.M.2    Clark, S.M.3    Dunn, S.D.4
  • 26
    • 0026788447 scopus 로고
    • 1) via cysteines introduced by site-directed mutagenesis
    • 1) via cysteines introduced by site-directed mutagenesis, J. Biol. Chem. 267, 21355-21359.
    • (1992) J. Biol. Chem. , vol.267 , pp. 21355-21359
    • Aggeler, R.1    Capaldi, R.A.2
  • 27
    • 0024372288 scopus 로고
    • 1 adenosinetriphosphatase decorated with monoclonal antibodies to individual subunits of the complex
    • 1 adenosinetriphosphatase decorated with monoclonal antibodies to individual subunits of the complex, Biochemistry 28, 4717-4724.
    • (1989) Biochemistry , vol.28 , pp. 4717-4724
    • Gogol, E.P.1    Aggeler, R.2    Sagermann, M.3    Capaldi, R.A.4
  • 28
    • 0028308212 scopus 로고
    • ATP hydrolysis-driven structural changes in the γ-subunit of Escherichia coli ATPase monitored by fluorescence from probes bound at introduced cysteine residues
    • Turina, P., and Capaldi, R. A. (1994) ATP hydrolysis-driven structural changes in the γ-subunit of Escherichia coli ATPase monitored by fluorescence from probes bound at introduced cysteine residues, J. Biol. Chem. 269, 13465-13471.
    • (1994) J. Biol. Chem. , vol.269 , pp. 13465-13471
    • Turina, P.1    Capaldi, R.A.2
  • 29
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill, S. C., and von Hippel, P. H. (1989) Calculation of protein extinction coefficients from amino acid sequence data, Anal. Biochem. 182, 319-326.
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 31
  • 32
    • 0021195067 scopus 로고
    • Amino acid, peptide, and protein volume in solution
    • Zamyatin, A. A. (1984) Amino acid, peptide, and protein volume in solution, Annu. Rev. Biophys. Bioeng. 13, 145-165.
    • (1984) Annu. Rev. Biophys. Bioeng. , vol.13 , pp. 145-165
    • Zamyatin, A.A.1
  • 33
    • 0039025943 scopus 로고
    • Fluorescence correlation spectroscopy of triplet states in solution: A theoretical and experimental study
    • Widengren, J., Mets, Ü., and Rigler, R. (1995) Fluorescence correlation spectroscopy of triplet states in solution: a theoretical and experimental study, J. Phys. Chem. 99, 13368-13379.
    • (1995) J. Phys. Chem. , vol.99 , pp. 13368-13379
    • Widengren, J.1    Mets, Ü.2    Rigler, R.3
  • 36
    • 0037188394 scopus 로고    scopus 로고
    • The "second stalk" of Escherichia coli ATP synthase: Structure of the isolated dimerization domain
    • Del Rizzo, P. A., Bi, Y., Dunn, S. D., and Shilton, B. H. (2002) The "second stalk" of Escherichia coli ATP synthase: structure of the isolated dimerization domain, Biochemistry 41, 6875-6884.
    • (2002) Biochemistry , vol.41 , pp. 6875-6884
    • Del Rizzo, P.A.1    Bi, Y.2    Dunn, S.D.3    Shilton, B.H.4
  • 38
    • 0025871645 scopus 로고
    • Structure-function relationships of domains of the δ subunit in E. coli adenosine triphosphatase
    • Mendel-Hartvig, J., and Capaldi, R. A. (1991) Structure-function relationships of domains of the δ subunit in E. coli adenosine triphosphatase, Biochim. Biophys. Acta 1060, 115-124.
    • (1991) Biochim. Biophys. Acta , vol.1060 , pp. 115-124
    • Mendel-Hartvig, J.1    Capaldi, R.A.2
  • 40
    • 0032511038 scopus 로고    scopus 로고
    • The b and δ subunits of the Escherichia coli ATP synthase interact via residues in their C-terminal regions
    • McLachlin, D. T., Bestard, J. A., and Dunn, S. D. (1998) The b and δ subunits of the Escherichia coli ATP synthase interact via residues in their C-terminal regions, J. Biol. Chem. 273, 15162-15168.
    • (1998) J. Biol. Chem. , vol.273 , pp. 15162-15168
    • McLachlin, D.T.1    Bestard, J.A.2    Dunn, S.D.3
  • 42
    • 0029893335 scopus 로고    scopus 로고
    • Intersubunit rotation in active F-ATPase
    • Sabbert, D., Engelbrecht, S., and Junge, W. (1996) Intersubunit rotation in active F-ATPase, Nature 381, 623-625.
    • (1996) Nature , vol.381 , pp. 623-625
    • Sabbert, D.1    Engelbrecht, S.2    Junge, W.3
  • 44
    • 17144435428 scopus 로고    scopus 로고
    • 1-ATP synthase: Storage of elastic energy during energy transduction
    • 1-ATP synthase: storage of elastic energy during energy transduction, Biochim. Biophys. Acta 1412, 118-128.
    • (1999) Biochim. Biophys. Acta , vol.1412 , pp. 118-128
    • Pänke, O.1    Rumberg, B.2
  • 45
    • 0034738090 scopus 로고    scopus 로고
    • Reverse engineering a protein: The mechanochemistry of ATP synthase
    • Oster, G., and Wang, H. (2000) Reverse engineering a protein: the mechanochemistry of ATP synthase, Biochim. Biophys. Acta 1458, 482-510.
    • (2000) Biochim. Biophys. Acta , vol.1458 , pp. 482-510
    • Oster, G.1    Wang, H.2
  • 46
    • 0034738153 scopus 로고    scopus 로고
    • The rotary binding change mechanism of ATP synthases
    • Cross, R. L. (2000) The rotary binding change mechanism of ATP synthases, Biochim. Biophys. Acta 1458, 270-275.
    • (2000) Biochim. Biophys. Acta , vol.1458 , pp. 270-275
    • Cross, R.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.