메뉴 건너뛰기




Volumn 34, Issue 3, 2001, Pages 305-320

Characterization of reconstituted Fo from wild-type Escherichia coli and identification of two other fluxes co-purifying with Fo

Author keywords

Bilayer; F1F0 ATPase; H+ channel; Lipids; Proton channel; Reconstitution

Indexed keywords

ADENOSINE TRIPHOSPHATASE; HYDROGEN; LIPID; PROTON; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE;

EID: 0035750381     PISSN: 10859195     EISSN: None     Source Type: Journal    
DOI: 10.1385/CBB:34:3:305     Document Type: Article
Times cited : (8)

References (34)
  • 4
    • 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. TIBS 22, 420-423.
    • (1997) TIBS , vol.22 , pp. 420-423
    • Junge, W.1    Lill, H.2    Engelbrecht, S.3
  • 7
    • 0028972731 scopus 로고
    • 0 complex of Escherichia coli ATP synthase from isolated subunits. Varying the number of essential carboxylates by co-incorporation of wild-type and mutant subunit: C after purification in organic solvent
    • 0 complex of Escherichia coli ATP synthase from isolated subunits. Varying the number of essential carboxylates by co-incorporation of wild-type and mutant subunit: c after purification in organic solvent. Eur. J. Biochem. 233, 478-483.
    • (1995) Eur. J. Biochem. , vol.233 , pp. 478-483
    • Dmitriev, O.Y.1    Altendorf, K.2    Fillingame, R.H.3
  • 8
    • 0019332667 scopus 로고
    • Energy-transducing H+-ATPase of Escherichia coli. Reconstitution of proton translocation activity of the intrinsic membrane sector
    • Negrin, R. S., Foster, D. L. and Fillingame, R. H. (1980) Energy-transducing H+-ATPase of Escherichia coli. Reconstitution of proton translocation activity of the intrinsic membrane sector. J. Biol. Chem. 255, 5643-5648.
    • (1980) J. Biol. Chem. , vol.255 , pp. 5643-5648
    • Negrin, R.S.1    Foster, D.L.2    Fillingame, R.H.3
  • 12
    • 0014184404 scopus 로고
    • The properties of dicyclohexylcarbodiimide as an inhibitor of oxidative phosphorylation
    • Beechey, R. B., Roberton, A. M., Holloway, C. T., et al. (1967) The properties of dicyclohexylcarbodiimide as an inhibitor of oxidative phosphorylation. Biochemistry 6, 3867-3879.
    • (1967) Biochemistry , vol.6 , pp. 3867-3879
    • Beechey, R.B.1    Roberton, A.M.2    Holloway, C.T.3
  • 13
    • 0034713072 scopus 로고    scopus 로고
    • Proton-powered turbine of a plant motor
    • Seelert, H., Poetsch, A., Dencher, N., et al. (2000) Proton-powered turbine of a plant motor. Nature 405, 418-419.
    • (2000) Nature , vol.405 , pp. 418-419
    • Seelert, H.1    Poetsch, A.2    Dencher, N.3
  • 14
    • 0033607504 scopus 로고    scopus 로고
    • Molecular architecture of the rotary motor in ATP synthase
    • Stock, D., Leslie, A.G.W. and Walker, J. E. (2000) Molecular architecture of the rotary motor in ATP synthase. Science 286, 1700-1705.
    • (2000) Science , vol.286 , pp. 1700-1705
    • Stock, D.1    Leslie, A.G.W.2    Walker, J.E.3
  • 17
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Miller, J. H. (1972) Experiments in Molecular Genetics. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1972) Experiments in Molecular Genetics
    • Miller, J.H.1
  • 18
    • 71849104860 scopus 로고
    • Protein measurement with the folin phenol reagent
    • Lowry, O. H., Rosebrough, N. J., Farr, A. L., et al. (1951) Protein measurement with the Folin phenol reagent. J. Biol. Chem., 193, 265-275.
    • (1951) J. Biol. Chem. , vol.193 , pp. 265-275
    • Lowry, O.H.1    Rosebrough, N.J.2    Farr, A.L.3
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 20
    • 0023739629 scopus 로고
    • Use of lac fusions to measure in vivo regulation of expression of Escherichia coli proton-translocating ATPase (une) genes
    • Angov, E. and Brusilow, W.S.A. (1988) Use of lac fusions to measure in vivo regulation of expression of Escherichia coli proton-translocating ATPase (une) genes. J. Bacteriol. 170, 459-462.
    • (1988) J. Bacteriol. , vol.170 , pp. 459-462
    • Angov, E.1    Brusilow, W.S.A.2
  • 21
    • 0026078046 scopus 로고
    • Small volume extrusion apparatus for preparation of large unilamellar vesicles
    • MacDonald, R. C., MacDonald, R. I., Menco, B. P. M. et al. (1991) Small volume extrusion apparatus for preparation of large unilamellar vesicles. Biochim. et Biophys. Acta 1061, 297-303.
    • (1991) Biochim. et Biophys. Acta , vol.1061 , pp. 297-303
    • MacDonald, R.C.1    MacDonald, R.I.2    Menco, B.P.M.3
  • 22
    • 0031729067 scopus 로고    scopus 로고
    • Nystatin/ergosterol method for reconstituting ion channels into planar lipid bilayers
    • Woodbury, D. J., (1999) Nystatin/ergosterol method for reconstituting ion channels into planar lipid bilayers. Methods Enzymol. 294, 319-339.
    • (1999) Methods Enzymol. , vol.294 , pp. 319-339
    • Woodbury, D.J.1
  • 23
    • 0030028238 scopus 로고    scopus 로고
    • Ion channels from synaptic vesicle membrane fragments reconstituted into lipid bilayers
    • Kelly, M. L. and Woodbury, D. J. (1996) Ion channels from synaptic vesicle membrane fragments reconstituted into lipid bilayers. Biophys. J. 70, 2593-2599.
    • (1996) Biophys. J. , vol.70 , pp. 2593-2599
    • Kelly, M.L.1    Woodbury, D.J.2
  • 24
    • 0024991373 scopus 로고
    • Nystatin-induced liposome fusion
    • Woodbury, D. J. and Miller, C. (1990) Nystatin-induced liposome fusion. Biophys. J. 58, 833-839.
    • (1990) Biophys. J. , vol.58 , pp. 833-839
    • Woodbury, D.J.1    Miller, C.2
  • 26
    • 0020104545 scopus 로고
    • Interactions between neutral phospholipid bilayer membranes
    • Lis, L., McAllister, M., Fuller, N., et al. (1982) Interactions between neutral phospholipid bilayer membranes. Biophys. J. 37, 657-665.
    • (1982) Biophys. J. , vol.37 , pp. 657-665
    • Lis, L.1    McAllister, M.2    Fuller, N.3
  • 27
    • 0023504972 scopus 로고
    • 0 complexes and biochemical and functional characterization of their subunits
    • 0 complexes and biochemical and functional characterization of their subunits. Microbiol. Rev. 51, 477-497.
    • (1987) Microbiol. Rev. , vol.51 , pp. 477-497
    • Schneider, E.1    Altendorf, K.2
  • 28
    • 0034640202 scopus 로고    scopus 로고
    • Common themes and problems of bioenergetics and voltage-gated proton channels
    • DeCoursey, T. E. and Cherny, V. V. (2000) Common themes and problems of bioenergetics and voltage-gated proton channels. Biochim. Biophys. Acta 1458, 104-119.
    • (2000) Biochim. Biophys. Acta , vol.1458 , pp. 104-119
    • DeCoursey, T.E.1    Cherny, V.V.2
  • 33
    • 0040486399 scopus 로고    scopus 로고
    • Channel-like behavior of the transmembrane fragments of a P-type ATPase
    • Radresa, O., Goormaghtigh, E., Homble, F., et al. (2000) Channel-like behavior of the transmembrane fragments of a P-type ATPase. Biophys. J. 78(1, part 2): 428.
    • (2000) Biophys. J. , vol.78 , Issue.1 PART 2 , pp. 428
    • Radresa, O.1    Goormaghtigh, E.2    Homble, F.3
  • 34
    • 0030947939 scopus 로고    scopus 로고
    • Cholesterol and ergosterol superlattices in three-component liquid crystalline lipid bilayers as revealed by dehydroergosterol fluorescence
    • Liu, F., Sugar, I. P. and Chong, P. L. (1997) Cholesterol and ergosterol superlattices in three-component liquid crystalline lipid bilayers as revealed by dehydroergosterol fluorescence. Biophys. J. 72, 2243-2254.
    • (1997) Biophys. J. , vol.72 , pp. 2243-2254
    • Liu, F.1    Sugar, I.P.2    Chong, P.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.