메뉴 건너뛰기




Volumn 7, Issue 4, 1999, Pages

ATP synthase: Two motors, two fuels

Author keywords

[No Author keywords available]

Indexed keywords

PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE;

EID: 0033561124     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(99)80046-X     Document Type: Review
Times cited : (60)

References (25)
  • 1
    • 0023099216 scopus 로고
    • Why nature chose phosphates
    • Westheimer, F.H. (1987). Why nature chose phosphates. Science 235, 1173-1178.
    • (1987) Science , vol.235 , pp. 1173-1178
    • Westheimer, F.H.1
  • 3
    • 0030863908 scopus 로고    scopus 로고
    • ATP synthase: A tentative structural model
    • Engelbrecht, S. & Junge, W. (1997). ATP synthase: A tentative structural model. FEBS Lett. 414, 485-491.
    • (1997) FEBS Lett. , vol.414 , pp. 485-491
    • Engelbrecht, S.1    Junge, W.2
  • 4
    • 0030845490 scopus 로고    scopus 로고
    • Model of the c-subunit oligomer in the membrane domain of F-ATPases
    • Groth, G. & Walker, J. (1997). Model of the c-subunit oligomer in the membrane domain of F-ATPases. FEBS Lett. 410, 117-123.
    • (1997) FEBS Lett. , vol.410 , pp. 117-123
    • Groth, G.1    Walker, J.2
  • 6
    • 0024371966 scopus 로고
    • A perspective of the binding change mechanism for ATP synthesis
    • Boyer, P.D. (1989). A perspective of the binding change mechanism for ATP synthesis. FASEB J. 3, 2164-2178.
    • (1989) FASEB J. , vol.3 , pp. 2164-2178
    • Boyer, P.D.1
  • 7
    • 0027492268 scopus 로고
    • The binding change mechanism for ATP synthase - Some probabilities and possibilities
    • Boyer, P. (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.1
  • 8
    • 0032568845 scopus 로고    scopus 로고
    • 0 ATP synthase as determined by labeling of unique cysteine residues
    • 0 ATP synthase as determined by labeling of unique cysteine residues. J. Biol. Chem. 273, 16235-16240.
    • (1998) J. Biol. Chem. , vol.273 , pp. 16235-16240
    • Long, J.C.1    Wang, S.2    Vik, S.B.3
  • 9
    • 0027970177 scopus 로고
    • 0 ATP synthases suggested by double mutants of the a subunit
    • 0 ATP synthases suggested by double mutants of the a subunit. J. Biol. Chem. 269, 30364-30369.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30364-30369
    • Vik, S.B.1    Antonio, B.J.2
  • 10
    • 0032493845 scopus 로고    scopus 로고
    • Molecular architecture of the c-subunit oligomer in the membrane domain of F-ATPases probed by tryptophan substitution mutagenesis
    • Groth, G., Tilg, Y. & Schirwitz, K. (1998). Molecular architecture of the c-subunit oligomer in the membrane domain of F-ATPases probed by tryptophan substitution mutagenesis. J. Mol. Biol. 281, 49-59.
    • (1998) J. Mol. Biol. , vol.281 , pp. 49-59
    • Groth, G.1    Tilg, Y.2    Schirwitz, K.3
  • 16
    • 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, K.3    Yoshida, M.4
  • 17
    • 0032547899 scopus 로고    scopus 로고
    • 1 motor of ATP synthase
    • 1 motor of ATP synthase. Nature 396, 279-282.
    • (1998) Nature , vol.396 , pp. 279-282
    • Wang, H.1    Oster, G.2
  • 18
    • 0031027579 scopus 로고    scopus 로고
    • 1 ATP synthase are dependent on the energy of interaction between γ and β subunits
    • 1 ATP synthase are dependent on the energy of interaction between γ and β subunits. J. Biol. Chem. 272, 2300-2306.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2300-2306
    • Al-Shawi, M.1    Ketchum, C.2    Nakamoto, R.3
  • 19
    • 0030680983 scopus 로고    scopus 로고
    • 1-ATP synthase: The uncoupling mutation, γM23K, Disrupts the use of binding energy to drive catalysis
    • 1-ATP synthase: The uncoupling mutation, γM23K, Disrupts the use of binding energy to drive catalysis. Biochemistry. 36, 12954-12960.
    • (1997) Biochemistry , vol.36 , pp. 12954-12960
    • Al-Shawi, M.1    Nakamoto, R.2
  • 21
    • 0001362052 scopus 로고    scopus 로고
    • 1-ATPase: A molecular motor that hydrolyzes ATP with sequential opening and closing of catalytic sites coupled to rotation of its γ subunit
    • 1-ATPase: A molecular motor that hydrolyzes ATP with sequential opening and closing of catalytic sites coupled to rotation of its γ subunit. Acc. Chem. Res. 31, 819-826.
    • (1998) Acc. Chem. Res. , vol.31 , pp. 819-826
    • Allison, W.1
  • 22
    • 0033609081 scopus 로고    scopus 로고
    • Energy transduction in the sodium F-ATPase of Propionigenium modestum
    • in press
    • Dimroth, P., Wang, H., Grabe, M. & Oster, G. (1999). Energy transduction in the sodium F-ATPase of Propionigenium modestum. Proc. Natl Acad. Sci. USA, in press.
    • (1999) Proc. Natl Acad. Sci. USA
    • Dimroth, P.1    Wang, H.2    Grabe, M.3    Oster, G.4
  • 23
    • 0032576724 scopus 로고    scopus 로고
    • Energy transduction in ATP synthase
    • Elston, T., Wang, H. & Oster, G. (1998). Energy transduction in ATP synthase. Nature 391, 510-514.
    • (1998) Nature , vol.391 , pp. 510-514
    • Elston, T.1    Wang, H.2    Oster, G.3
  • 24
    • 0032311441 scopus 로고    scopus 로고
    • ATP synthase - Past and future
    • Boyer, P. (1998). ATP synthase - Past and future. Biochim. Biophys. Acta 1365, 3-9.
    • (1998) Biochim. Biophys. Acta , vol.1365 , pp. 3-9
    • Boyer, P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.