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Volumn 93, Issue 7, 1998, Pages 1117-1124

F1-ATPase is a highly efficient molecular motor that rotates with discrete 120°steps

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; ACTIN; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE;

EID: 0032568695     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)81456-7     Document Type: Article
Times cited : (745)

References (37)
  • 3
    • 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
  • 4
    • 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, eds. (Amsterdam: Elsevier)
    • Boyer, P.D., and Kohlbrenner, W.E. (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, eds. (Amsterdam: Elsevier), pp. 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 McElroy, W.D. (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
  • 9
    • 0028945654 scopus 로고
    • Imaging of single fluorescent molecules and individual ATP turnovers by single myosin molecules in aqueous solution
    • Funatsu, T., Harada, Y., Tokunaga, M., Saito, K., and Yanagida, T. (1995). Imaging of single fluorescent molecules and individual ATP turnovers by single myosin molecules in aqueous solution. Nature 374, 555-559.
    • (1995) Nature , vol.374 , pp. 555-559
    • Funatsu, T.1    Harada, Y.2    Tokunaga, M.3    Saito, K.4    Yanagida, T.5
  • 11
    • 0020491269 scopus 로고
    • Mechanism of ATP hydrolysis by beef heart mitochondrial ATPase
    • Grubmeyer, C., Cross, R.L., and Penefsky, H.S. (1982). Mechanism of ATP hydrolysis by beef heart mitochondrial ATPase. J. Biol. Chem. 257, 12092-12100.
    • (1982) J. Biol. Chem. , vol.257 , pp. 12092-12100
    • Grubmeyer, C.1    Cross, R.L.2    Penefsky, H.S.3
  • 12
    • 0030935659 scopus 로고    scopus 로고
    • Kinetics of force generation by single kinesin molecules activated by laser photolysis of caged ATP
    • Higuchi, H., Muto, E., Inoue, Y., and Yanagida, T. (1997). Kinetics of force generation by single kinesin molecules activated by laser photolysis of caged ATP. Proc. Natl. Acad. Sci. USA 94, 4395-4400.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 4395-4400
    • Higuchi, H.1    Muto, E.2    Inoue, Y.3    Yanagida, T.4
  • 13
    • 0030844286 scopus 로고    scopus 로고
    • Coupling of kinesin steps to ATP hydrolysis
    • Hua, W., Young, E.C., Fleming, M.L., and Gelles, J. (1997). Coupling of kinesin steps to ATP hydrolysis. Nature 388, 390-393.
    • (1997) Nature , vol.388 , pp. 390-393
    • Hua, W.1    Young, E.C.2    Fleming, M.L.3    Gelles, J.4
  • 14
    • 0028145209 scopus 로고
    • The force exerted by a single kinesin molecule against a viscous load
    • Hunt, A.J., Gittes, F., and Howard, J. (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
  • 15
    • 33847013578 scopus 로고
    • Muscle structure and theories of contraction
    • Huxley, A.F. (1957). Muscle structure and theories of contraction. Prog. Biophys. Mol. Biol. 7, 255-318.
    • (1957) Prog. Biophys. Mol. Biol. , vol.7 , pp. 255-318
    • Huxley, A.F.1
  • 16
    • 0029417124 scopus 로고
    • 1-ATPase from the thermophilic Bacillus PS3 containing the α-D261N substitution fails to dissociate inhibitory Mg ADP from a catalytic site when ATP binds to noncatalytic sites
    • 1-ATPaSe from the thermophilic Bacillus PS3 containing the α-D261N substitution fails to dissociate inhibitory Mg ADP from a catalytic site when ATP binds to noncatalytic sites. Biochemistry 34, 16412-16418.
    • (1995) Biochemistry , vol.34 , pp. 16412-16418
    • Jault, J.-M.1    Matsui, T.2    Jault, F.M.3    Kaibara, C.4    Muneyuki, E.5    Yoshida, M.6    Kagawa, Y.7    Allison, W.S.8
  • 17
    • 0030715561 scopus 로고    scopus 로고
    • ATP synthase: An electrochemical transducer with rotatory mechanics
    • Junge, W., Lill, H., and Engelbrecht, S. (1997). ATP synthase: an electrochemical transducer with rotatory mechanics. Trends Biochem. Sci. 22, 420-423.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 420-423
    • Junge, W.1    Lill, H.2    Engelbrecht, S.3
  • 22
    • 0023644878 scopus 로고
    • The proton flux through the bacterial flagellar motor
    • Meister, M., Lowe, G., and Berg, H.C. (1987). The proton flux through the bacterial flagellar motor. Cell 49, 643-650.
    • (1987) Cell , vol.49 , pp. 643-650
    • Meister, M.1    Lowe, G.2    Berg, H.C.3
  • 24
    • 36949083936 scopus 로고
    • Coupling of phosphorylation to electron and hydrogen transfer by a chemi-osmotic type of mechanism
    • Mitchell, P. (1961). Coupling of phosphorylation to electron and hydrogen transfer by a chemi-osmotic type of mechanism. Nature 191, 144-148.
    • (1961) Nature , vol.191 , pp. 144-148
    • Mitchell, P.1
  • 27
    • 0030796982 scopus 로고    scopus 로고
    • 3γ complex switches the kinetics of ATP hydrolysis from negative to positive cooperativity
    • 3γ complex switches the kinetics of ATP hydrolysis from negative to positive cooperativity. FEBS Lett. 413, 55-59.
    • (1997) FEBS Lett. , vol.413 , pp. 55-59
    • Muneyuki, E.1    Odaka, M.2    Yoshida, M.3
  • 29
    • 0022824129 scopus 로고
    • The loose coupling mechanism in molecular machines of living cells
    • Oosawa, F., and Hayashi, S. (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
  • 30
    • 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
  • 31
    • 0029129917 scopus 로고
    • Real time imaging of single fluorophores on moving actin with an epifluorescence microscope
    • Sase, I., Miyata, H., Corrie, J.E.T., Craik, J.S., and Kinosita, K., Jr. (1995). Real time imaging of single fluorophores on moving actin with an epifluorescence microscope. Biophys. J. 69, 323-328.
    • (1995) Biophys. J. , vol.69 , pp. 323-328
    • Sase, I.1    Miyata, H.2    Corrie, J.E.T.3    Craik, J.S.4    Kinosita K., Jr.5
  • 32
    • 0030902490 scopus 로고    scopus 로고
    • Axial rotation of sliding actin filaments revealed by single-fluorophore imaging
    • Sase, I., Miyata, H., Ishiwata, S., and Kinosita K., Jr. (1997). Axial rotation of sliding actin filaments revealed by single-fluorophore imaging. Proc. Natl. Acad. Sci. USA 94, 5646-5650.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 5646-5650
    • Sase, I.1    Miyata, H.2    Ishiwata, S.3    Kinosita K., Jr.4
  • 33
    • 0028911694 scopus 로고
    • Energetics of ATP dissociation from the mitochondrial ATPase during oxidative phosphorylation
    • Souid, A.-K., and Penefsky, H.S. (1995). Energetics of ATP dissociation from the mitochondrial ATPase during oxidative phosphorylation. J. Biol. Chem. 270, 9074-9082.
    • (1995) J. Biol. Chem. , vol.270 , pp. 9074-9082
    • Souid, A.-K.1    Penefsky, H.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.