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Volumn 88, Issue 3, 2005, Pages 2047-2056

One rotary mechanism for F1-ATPaSe over ATP concentrations from millimolar down to nanomolar

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; NUCLEOTIDE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; MOLECULAR MOTOR; NANOMATERIAL; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE;

EID: 21244466033     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.104.054668     Document Type: Article
Times cited : (78)

References (37)
  • 4
    • 0031008228 scopus 로고    scopus 로고
    • The ATP synthase-a splendid molecular machine
    • Boyer, P. D. 1997. The ATP synthase-a splendid molecular machine. Annu. Rev. Biochem. 66:717-749.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 717-749
    • Boyer, P.D.1
  • 5
    • 0037070150 scopus 로고    scopus 로고
    • Catalytic site occupancy during ATP synthase catalysis
    • Boyer, P. D. 2002. Catalytic site occupancy during ATP synthase catalysis. FEBS Lett. 512:29-32.
    • (2002) FEBS Lett. , vol.512 , pp. 29-32
    • Boyer, P.D.1
  • 6
    • 0002888351 scopus 로고
    • The present status of the binding-change mechanism and its relation to ATP formation by chloroplasts
    • B. R. Selman, and S. Selman-Reimer, editors. Elsevier, Amsterdam
    • Boyer, P. D., and W. E. Kohlbrenner. 1981. The present status of the binding-change mechanism and its relation to ATP formation by chloroplasts. In Energy Coupling in Photosynthesis. B. R. Selman, and S. Selman-Reimer, editors. Elsevier, Amsterdam. 231-240.
    • (1981) Energy Coupling in Photosynthesis , pp. 231-240
    • Boyer, P.D.1    Kohlbrenner, W.E.2
  • 7
    • 77956986494 scopus 로고
    • Purification and properties of firefly luciferase
    • DeLuca, M., and W. D. McElroy. 1978. Purification and properties of firefly luciferase. Methods Enzymol. 57:3-15.
    • (1978) Methods Enzymol. , vol.57 , pp. 3-15
    • DeLuca, M.1    McElroy, W.D.2
  • 10
    • 0028145209 scopus 로고
    • The force exerted by a single kinesin molecule against a viscous load
    • Hunt, A. J., F. Gittes, and J. Howard. 1994. The force exerted by a single kinesin molecule against a viscous load. Biophys. J. 67:766-781.
    • (1994) Biophys. J. , vol.67 , pp. 766-781
    • Hunt, A.J.1    Gittes, F.2    Howard, J.3
  • 13
    • 0029658807 scopus 로고    scopus 로고
    • 1-ATPase from the thermophilic Bacillus PS3 with the βT165S substitution does not entrap inhibitory MgADP in a catalytic site during turnover
    • 1-ATPase from the thermophilic Bacillus PS3 with the βT165S substitution does not entrap inhibitory MgADP in a catalytic site during turnover. J. Biol. Chem. 271:28818-28824.
    • (1996) J. Biol. Chem. , vol.271 , pp. 28818-28824
    • Jault, J.-M.1    Dou, C.2    Grodsky, N.B.3    Matsui, T.4    Yoshida, M.5    Allison, W.S.6
  • 14
    • 0014027518 scopus 로고
    • Partial resolution of the enzymes catalyzing oxidative phosphorylation. IX. Reconstruction of oligomycin-sensitive adenosine triphosphatase
    • Kagawa, Y., and E. Racker. 1966. Partial resolution of the enzymes catalyzing oxidative phosphorylation. IX. Reconstruction of oligomycin-sensitive adenosine triphosphatase. J. Biol. Chem. 241:2467-2474.
    • (1966) J. Biol. Chem. , vol.241 , pp. 2467-2474
    • Kagawa, Y.1    Racker, E.2
  • 20
    • 0035838982 scopus 로고    scopus 로고
    • 1-ATPase with nucleotide bound to all three catalytic sites: Implications for the mechanism of rotary catalysis
    • 1-ATPase with nucleotide bound to all three catalytic sites: implications for the mechanism of rotary catalysis. Cell. 106:331-341.
    • (2001) Cell , vol.106 , pp. 331-341
    • Menz, R.I.1    Walker, J.E.2    Leslie, A.G.W.3
  • 26
    • 0022824129 scopus 로고
    • The loose coupling mechanism in molecular machines of living cells
    • Oosawa, F., and S. Hayashi. 1986. The loose coupling mechanism in molecular machines of living cells. Adv. Biophys. 22:151-183.
    • (1986) Adv. Biophys. , vol.22 , pp. 151-183
    • Oosawa, F.1    Hayashi, S.2
  • 27
    • 0034866072 scopus 로고    scopus 로고
    • Viscoelastic dynamics of actin filaments coupled to rotary F-ATPase: Angular torque profile of the enzyme
    • Pänke, O., D. A. Cherepanov, K. Gumbiowski, S. Engelbrecht, and W. Junge. 2001. Viscoelastic dynamics of actin filaments coupled to rotary F-ATPase: angular torque profile of the enzyme. Biophys. J. 81:1220-1233.
    • (2001) Biophys. J. , vol.81 , pp. 1220-1233
    • Pänke, O.1    Cherepanov, D.A.2    Gumbiowski, K.3    Engelbrecht, S.4    Junge, W.5
  • 28
    • 0034615699 scopus 로고    scopus 로고
    • 1-ATPase from the thermophilic Bacillus PS3 increases the affinity of catalytic sites for nucleotides
    • 1-ATPase from the thermophilic Bacillus PS3 increases the affinity of catalytic sites for nucleotides. J. Biol. Chem. 275: 10057-10063.
    • (2000) J. Biol. Chem. , vol.275 , pp. 10057-10063
    • Ren, H.1    Allison, W.S.2
  • 32
    • 0027317040 scopus 로고
    • 1-ATPase provides a direct probe of nucleotide binding: Maximal ATP hydrolysis occurs with three sites occupied
    • 1-ATPase provides a direct probe of nucleotide binding: Maximal ATP hydrolysis occurs with three sites occupied. J. Biol. Chem. 268: 20126-20133.
    • (1993) J. Biol. Chem. , vol.268 , pp. 20126-20133
    • Weber, J.1    Wilke-Mounts, S.2    Lee, R.S.-F.3    Grell, E.4    Senior, A.E.5
  • 35
    • 0032568695 scopus 로고    scopus 로고
    • 1-ATPase is a highly efficient molecular motor that rotates with discrete 120° steps
    • 1-ATPase is a highly efficient molecular motor that rotates with discrete 120° steps. Cell. 93:1117-1124.
    • (1998) Cell , vol.93 , pp. 1117-1124
    • Yasuda, R.1    Noji, H.2    Kinosita Jr., K.3    Yoshida, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.