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Volumn 269, Issue 22, 2002, Pages 5581-5589

Membrane embedded location of Na+ or H+ binding sites on the rotor ring of F1F0 ATP synthases

Author keywords

ATP synthase; C subunit; Coupling ion binding site; Membrane localization; Parallax analysis

Indexed keywords

1 CYCLOHEXYL 3 (1 PYRENYL)CARBODIIMIDE; ENZYME; HYDROGEN; IMIDE; OLIGOMER; PHOSPHOLIPID; PROTEIN SUBUNIT; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; SODIUM; UNCLASSIFIED DRUG;

EID: 0036436901     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2002.03264.x     Document Type: Article
Times cited : (20)

References (53)
  • 5
    • 0033607504 scopus 로고    scopus 로고
    • Molecular architecture of the rotary motor in ATP synthase
    • Stock, D., Leslie, A.G. & Walker, J.E. (1999) Molecular architecture of the rotary motor in ATP synthase. Science 286, 1700-1705.
    • (1999) Science , vol.286 , pp. 1700-1705
    • Stock, D.1    Leslie, A.G.2    Walker, J.E.3
  • 6
    • 0035846822 scopus 로고    scopus 로고
    • 1-ATPase at 3.2 Å resolution
    • 1-ATPase at 3.2 Å resolution. J. Biol. Chem. 276, 1345-1352.
    • (2001) J. Biol. Chem. , vol.276 , pp. 1345-1352
    • Groth, G.1    Pohl, E.2
  • 9
    • 0037908118 scopus 로고    scopus 로고
    • F-ATPase: Specific observation of the rotating c subunit oligomer of EF (0) EF (1)
    • Pänke, O., Gumbiowski, K., Junge, W. & Engelbrecht, S. (2000) F-ATPase: Specific observation of the rotating c subunit oligomer of EF (0) EF (1). FEBS Lett. 472, 34-38.
    • (2000) FEBS Lett. , vol.472 , pp. 34-38
    • Pänke, O.1    Gumbiowski, K.2    Junge, W.3    Engelbrecht, S.4
  • 11
    • 0034738102 scopus 로고    scopus 로고
    • The ATP synthase of Escherichia coli: Structure and function of F (0) subunits
    • Deckers-Hebestreit, G., Greie, J., Stalz, W. & Altendorf, K. (2000) The ATP synthase of Escherichia coli: Structure and function of F (0) subunits. Biochim. Biophys. Acta 1458, 364-373.
    • (2000) Biochim. Biophys. Acta , vol.1458 , pp. 364-373
    • Deckers-Hebestreit, G.1    Greie, J.2    Stalz, W.3    Altendorf, K.4
  • 15
    • 0032499690 scopus 로고    scopus 로고
    • 0 ATP synthase of Escherichia coli defined by disulfide cross-linking
    • 0 ATP synthase of Escherichia coli defined by disulfide cross-linking. Proc. Natl. Acad. Sci. USA 95, 6607-6612.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6607-6612
    • Jiang, W.1    Fillingame, R.H.2
  • 20
    • 0030809240 scopus 로고    scopus 로고
    • + in the c subunit of the ATP synthase from Propionigenium modestum
    • + in the c subunit of the ATP synthase from Propionigenium modestum. Biochemistry 36, 9185-9194.
    • (1997) Biochemistry , vol.36 , pp. 9185-9194
    • Kaim, G.1    Wehrle, F.2    Gerike, U.3    Dimroth, P.4
  • 22
    • 0023652259 scopus 로고
    • Parallax method for direct measurement of membrane penetration depth utilizing fluorescence quenching by spin-labeled phospholipids
    • Chattopadhyay, A. & London, E. (1987) Parallax method for direct measurement of membrane penetration depth utilizing fluorescence quenching by spin-labeled phospholipids. Biochemistry 26, 39-45.
    • (1987) Biochemistry , vol.26 , pp. 39-45
    • Chattopadhyay, A.1    London, E.2
  • 23
    • 0022372145 scopus 로고
    • Fluorescent analogues of N,N′-dicyclohexylcarbodiimide as structural probes of the bovine mitochondrial proton channel
    • Pringle, M.J. & Taber, M. (1985) Fluorescent analogues of N,N′-dicyclohexylcarbodiimide as structural probes of the bovine mitochondrial proton channel. Biochemistry 24, 7366-7371.
    • (1985) Biochemistry , vol.24 , pp. 7366-7371
    • Pringle, M.J.1    Taber, M.2
  • 24
    • 0034720773 scopus 로고    scopus 로고
    • Identification of lipid-accessible sites on the nephrops 16-kDa proteolipid incorporated into a hybrid vacuolar H(+)-ATPase: Site-directed labeling with N-(1-Pyrenyl) cyclohexylcarbodiimide and fluorescence quenching analysis
    • Harrison, M., Powell, B., Finbow, M.E. & Findlay, J.B. (2000) Identification of lipid-accessible sites on the nephrops 16-kDa proteolipid incorporated into a hybrid vacuolar H(+)-ATPase: Site-directed labeling with N-(1-Pyrenyl) cyclohexylcarbodiimide and fluorescence quenching analysis. Biochemistry 39, 7531-7537.
    • (2000) Biochemistry , vol.39 , pp. 7531-7537
    • Harrison, M.1    Powell, B.2    Finbow, M.E.3    Findlay, J.B.4
  • 25
    • 0035655285 scopus 로고    scopus 로고
    • Localization of bilirubin in phospholipid bilayers by parallax analysis of fluorescence quenching
    • Zucker, S.D., Goessling, W., Bootle, E.J. & Sterritt, C. (2001) Localization of bilirubin in phospholipid bilayers by parallax analysis of fluorescence quenching. J. Lipid Res. 42, 1377-1388.
    • (2001) J. Lipid Res. , vol.42 , pp. 1377-1388
    • Zucker, S.D.1    Goessling, W.2    Bootle, E.J.3    Sterritt, C.4
  • 30
    • 0024293219 scopus 로고
    • Characterization of the ATP synthase of Propionigenium modestum as a primary sodium pump
    • Laubinger, W. & Dimroth, P. (1988) Characterization of the ATP synthase of Propionigenium modestum as a primary sodium pump. Biochemistry 27, 7531-7537.
    • (1988) Biochemistry , vol.27 , pp. 7531-7537
    • Laubinger, W.1    Dimroth, P.2
  • 31
    • 0029897240 scopus 로고    scopus 로고
    • Unidirectional reconstitution into detergent-destabilized liposomes of the purified lactose transport system of Streptococcus thermophilus
    • Knol, J., Veenhoff, L., Liang, W.J., Henderson, P.J., Leblanc, G. & Poolman, B. (1996) Unidirectional reconstitution into detergent-destabilized liposomes of the purified lactose transport system of Streptococcus thermophilus. J. Biol. Chem. 271, 15358-15366.
    • (1996) J. Biol. Chem. , vol.271 , pp. 15358-15366
    • Knol, J.1    Veenhoff, L.2    Liang, W.J.3    Henderson, P.J.4    Leblanc, G.5    Poolman, B.6
  • 32
    • 0024962378 scopus 로고
    • The sodium ion translocating adenosinetriphosphatase of Propionigenium modestum pumps protons at low sodium ion concentrations
    • Laubinger, W. & Dimroth, P. (1989) The sodium ion translocating adenosinetriphosphatase of Propionigenium modestum pumps protons at low sodium ion concentrations. Biochemistry 28, 7194-7198.
    • (1989) Biochemistry , vol.28 , pp. 7194-7198
    • Laubinger, W.1    Dimroth, P.2
  • 34
    • 0027340171 scopus 로고
    • + concentration: Probing the binding site for the coupling ions
    • + concentration: Probing the binding site for the coupling ions. Biochemistry 32, 10378-10386.
    • (1993) Biochemistry , vol.32 , pp. 10378-10386
    • Kluge, C.1    Dimroth, P.2
  • 35
    • 0027518128 scopus 로고
    • Protein-lipid interactions and Torpedo californica nicotinic acetylcholine receptor function. 1. Spatial disposition of cysteine residues in the gamma subunit analyzed by fluorescence-quenching and energy-transfer measurements
    • Narayanaswami, V., Kim, J. & McNamee, M.G. (1993) Protein-lipid interactions and Torpedo californica nicotinic acetylcholine receptor function. 1. Spatial disposition of cysteine residues in the gamma subunit analyzed by fluorescence-quenching and energy-transfer measurements. Biochemistry 32, 12413-12419.
    • (1993) Biochemistry , vol.32 , pp. 12413-12419
    • Narayanaswami, V.1    Kim, J.2    McNamee, M.G.3
  • 36
    • 0030715561 scopus 로고    scopus 로고
    • ATP synthase: An electrochemical transducer with rotatory mechanics
    • Junge, W., Lill, H. & 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
  • 37
    • 0034737951 scopus 로고    scopus 로고
    • Structural interpretations of F(0) rotary function in the Escherichia coli F(1) F(0) ATP synthase
    • Fillingame, R.H., Jiang, W., Dmitriev, O.Y. & Jones, P.C. (2000) Structural interpretations of F(0) rotary function in the Escherichia coli F(1) F(0) ATP synthase. Biochim. Biophys. Acta 1458, 387-403.
    • (2000) Biochim. Biophys. Acta , vol.1458 , pp. 387-403
    • Fillingame, R.H.1    Jiang, W.2    Dmitriev, O.Y.3    Jones, P.C.4
  • 38
    • 0027279864 scopus 로고
    • 0-ATPase of Propionigenium modestum from the reaction with dicyclohexylcarbodiimide
    • 0-ATPase of Propionigenium modestum from the reaction with dicyclohexylcarbodiimide. J. Biol. Chem. 268, 14557-14560.
    • (1993) J. Biol. Chem. , vol.268 , pp. 14557-14560
    • Kluge, C.1    Dimroth, P.2
  • 39
    • 0032531926 scopus 로고    scopus 로고
    • Voltage-generated torque drives the motor of the ATP synthase
    • Kaim, G. & Dimroth, P. (1998) Voltage-generated torque drives the motor of the ATP synthase. EMBO J. 17, 5887-5895.
    • (1998) EMBO J. , vol.17 , pp. 5887-5895
    • Kaim, G.1    Dimroth, P.2
  • 41
    • 0035902609 scopus 로고    scopus 로고
    • Energy-driven subunit rotation at the interface between subunit a and the c oligomer in the F(0) sector of Escherichia coli ATP synthase
    • Hutcheon, M.L., Duncan, T.M., Ngai, H. & Cross, R.L. (2001) Energy-driven subunit rotation at the interface between subunit a and the c oligomer in the F(0) sector of Escherichia coli ATP synthase. Proc. Natl. Acad. Sci. USA 98, 8519-8524.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 8519-8524
    • Hutcheon, M.L.1    Duncan, T.M.2    Ngai, H.3    Cross, R.L.4
  • 42
    • 0037066772 scopus 로고    scopus 로고
    • 0 of ATP synthase is a rotary proton channel. Obligatory coupling of proton translocation with rotation of c-subunit ring
    • 0 of ATP synthase is a rotary proton channel. Obligatory coupling of proton translocation with rotation of c-subunit ring. J. Biol. Chem. 277, 13281-13285.
    • (2002) J. Biol. Chem. , vol.277 , pp. 13281-13285
    • Suzuki, T.1    Ueno, H.2    Mitome, N.3    Suzuki, J.4    Yoshida, M.5
  • 44
    • 0033609081 scopus 로고    scopus 로고
    • Energy transduction in the sodium F-ATPase of Propionigenium modestum
    • Dimroth, P., Wang, H., Grabe, M. & Oster, G. (1999) Energy transduction in the sodium F-ATPase of Propionigenium modestum. Proc. Natl. Acad. Sci. USA 96, 4924-4929.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 4924-4929
    • Dimroth, P.1    Wang, H.2    Grabe, M.3    Oster, G.4
  • 45
    • 0021772468 scopus 로고
    • +-translocating adenosinetriphosphatase complex of Escherichia coli by the water-soluble carbodiimide 1-ethyl-3-[3-(dimethylamino) propyl]carbodiimide and effect on the proton channeling function
    • +-translocating adenosinetriphosphatase complex of Escherichia coli by the water-soluble carbodiimide 1-ethyl-3-[3-(dimethylamino) propyl]carbodiimide and effect on the proton channeling function. Biochemistry 23, 4128-4134.
    • (1984) Biochemistry , vol.23 , pp. 4128-4134
    • Lötscher, H.R.1    DeJong, C.2    Capaldi, R.A.3
  • 49
    • 0018786840 scopus 로고
    • The proteolipid subunit of chloroplast adenosine triphosphatase complex. Mobility, accessibility, and interactions studied by a spin label technique
    • Sigrist-Nelson, K. & Azzi, A. (1979) The proteolipid subunit of chloroplast adenosine triphosphatase complex. Mobility, accessibility, and interactions studied by a spin label technique. J. Biol. Chem. 254, 4470-4474.
    • (1979) J. Biol. Chem. , vol.254 , pp. 4470-4474
    • Sigrist-Nelson, K.1    Azzi, A.2
  • 50
    • 0025175190 scopus 로고
    • Membrane-protein structural mapping of chloroplast coupling factor in asolectin vesicles
    • Mitra, B. & Hammes, G.G. (1990) Membrane-protein structural mapping of chloroplast coupling factor in asolectin vesicles. Biochemistry 29, 9879-9884.
    • (1990) Biochemistry , vol.29 , pp. 9879-9884
    • Mitra, B.1    Hammes, G.G.2
  • 51
    • 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
  • 52
    • 0037085021 scopus 로고    scopus 로고
    • pH dependent inactivation of solubilized F(1) F(0) ATP synthase by dicyclohexylcarbodiimide: pK(a) of detergent unmasked aspartyl-61 in Escherichia coli subunit c
    • Valiyaveetil, F., Hermolin, J. & Fillingame, R.H. (2002) pH dependent inactivation of solubilized F(1) F(0) ATP synthase by dicyclohexylcarbodiimide: pK(a) of detergent unmasked aspartyl-61 in Escherichia coli subunit c. Biochim. Biophys. Acta 1553, 296-301.
    • (2002) Biochim. Biophys. Acta , vol.1553 , pp. 296-301
    • Valiyaveetil, F.1    Hermolin, J.2    Fillingame, R.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.