메뉴 건너뛰기




Volumn 50, Issue , 1996, Pages 791-824

The F0F1-type ATP synthases of bacteria: Structure and function of the F0 complex

Author keywords

coupling; F0F1 ATPase; ion translocation; subunit interplay

Indexed keywords

BACTERIAL ENZYME; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; ADENOSINE TRIPHOSPHATE; MEMBRANE PROTEIN; PROTON PUMP; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE;

EID: 0029658688     PISSN: 00664227     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.micro.50.1.791     Document Type: Review
Times cited : (178)

References (187)
  • 3
    • 0028980158 scopus 로고
    • Arrangement of the ε subunit in the Escherichia coli ATP synthase from the reactivity of cysteine residues introduced at different positions in this subunit
    • Aggeler R, Weinreich F, Capaldi RA. 1995. Arrangement of the ε subunit in the Escherichia coli ATP synthase from the reactivity of cysteine residues introduced at different positions in this subunit. Biochim. Biophys. Acta 1230:62-68
    • (1995) Biochim. Biophys. Acta , vol.1230 , pp. 62-68
    • Aggeler, R.1    Weinreich, F.2    Capaldi, R.A.3
  • 7
    • 0028984806 scopus 로고
    • 0 complex of the ATP synthase of Escherichia coli contains a proton pathway with large proton polarizability caused by collective proton fluctuation
    • 0 complex of the ATP synthase of Escherichia coli contains a proton pathway with large proton polarizability caused by collective proton fluctuation. Biophys. J. 68:104-10
    • (1995) Biophys. J. , vol.68 , pp. 104-110
    • Bartl, F.1    Deckers-Hebestreit, G.2    Altendorf, K.3    Zundel, G.4
  • 8
    • 0028181851 scopus 로고
    • 0-ATP synthase in membrane vesicles of the archaeon Methanosarcina mazei Göl
    • 0-ATP synthase in membrane vesicles of the archaeon Methanosarcina mazei Göl. J. Bacteriol. 176:2543-50
    • (1994) J. Bacteriol. , vol.176 , pp. 2543-2550
    • Becher, B.1    Müller, V.2
  • 9
    • 0023135722 scopus 로고
    • Processing of the initiation methionine from proteins: Properties of the Escherichia coli methionine aminopeptidase and its gene structure
    • Ben-Bassat A, Bauer K, Chang S-Y, Myambo K, Boosman A, Chang S. 1987. Processing of the initiation methionine from proteins: properties of the Escherichia coli methionine aminopeptidase and its gene structure. J. Bacteriol. 169:751-57
    • (1987) J. Bacteriol. , vol.169 , pp. 751-757
    • Ben-Bassat, A.1    Bauer, K.2    Chang, S.-Y.3    Myambo, K.4    Boosman, A.5    Chang, S.6
  • 11
    • 0025098534 scopus 로고
    • The transmembrane topology of the a subunit from the ATPase in Escherichia coli analyzed by PhoA protein fusions
    • Bjørbæk C, Foërsom V, Michelsen O. 1990. The transmembrane topology of the a subunit from the ATPase in Escherichia coli analyzed by PhoA protein fusions. FEBS Lett. 260:31-34
    • (1990) FEBS Lett. , vol.260 , pp. 31-34
    • Bjørbæk, C.1    Foërsom, V.2    Michelsen, O.3
  • 12
    • 0027492268 scopus 로고
    • The binding change mechanism for ATP synthase - Some probabilities and possibilities
    • Boyer PD. 1993. The binding change mechanism for ATP synthase - some probabilities and possibilities. Biochim. Biophys. Acta 1140:215-50
    • (1993) Biochim. Biophys. Acta , vol.1140 , pp. 215-250
    • Boyer, P.D.1
  • 15
    • 0024977998 scopus 로고
    • 0-ATPase of Escherichia coli. Mutagenic analysis of the a subunit
    • 0-ATPase of Escherichia coli. Mutagenic analysis of the a subunit. J. Biol. Chem. 264:3292-3300
    • (1989) J. Biol. Chem. , vol.264 , pp. 3292-3300
    • Cain, B.D.1    Simoni, R.D.2
  • 18
    • 0025272940 scopus 로고
    • α-Helical coiled coils and bundles: How to design an α-helical protein
    • Cohen C, Parry DAD. 1990. α-Helical coiled coils and bundles: How to design an α-helical protein. Prot. Struct. Funct. Genet. 7:1-15
    • (1990) Prot. Struct. Funct. Genet. , vol.7 , pp. 1-15
    • Cohen, C.1    Parry, D.A.D.2
  • 19
    • 0022492015 scopus 로고
    • The mechanism of ATP synthase: A reassessment of the functions of the b and a subunits
    • Cox GB, Fimmel AL. Gibson F, Hatch L. 1986. The mechanism of ATP synthase: a reassessment of the functions of the b and a subunits. Biochim. Biophys. Acta 849:62-69
    • (1986) Biochim. Biophys. Acta , vol.849 , pp. 62-69
    • Cox, G.B.1    Fimmel, A.L.2    Gibson, F.3    Hatch, L.4
  • 23
    • 0026949636 scopus 로고
    • 0 complex of the proton-translocating F-type ATPase of Escherichia coli
    • 0 complex of the proton-translocating F-type ATPase of Escherichia coli. J. Exp. Biol. 172:451-59
    • (1992) J. Exp. Biol. , vol.172 , pp. 451-459
    • Deckers-Hebestreit, G.1    Altendorf, K.2
  • 24
    • 0026683291 scopus 로고
    • 0 complex of the ATP synthase of Escherichia coli. II. Effects of subunit c-specific polyclonal antibodies
    • 0 complex of the ATP synthase of Escherichia coli. II. Effects of subunit c-specific polyclonal antibodies. J. Biol. Chem. 267:12370-74
    • (1992) J. Biol. Chem. , vol.267 , pp. 12370-12374
    • Deckers-Hebestreit, G.1    Altendorf, K.2
  • 26
    • 0026694624 scopus 로고
    • Influence of subunit-specific antibodies on the activity of the Fo complex of the ATP synthase of Escherichia coli. I. Effects of subunit b-specific polyclonal antibodies
    • Deckers-Hebestreit G, Simoni RD, Altendorf K. 1992. Influence of subunit-specific antibodies on the activity of the Fo complex of the ATP synthase of Escherichia coli. I. Effects of subunit b-specific polyclonal antibodies. J. Biol. Chem. 267:12364-69
    • (1992) J. Biol. Chem. , vol.267 , pp. 12364-12369
    • Deckers-Hebestreit, G.1    Simoni, R.D.2    Altendorf, K.3
  • 27
    • 0022348605 scopus 로고
    • Structure of the protein subunits in the photosynthetic reaction centre of Rhodopseudomonas viridis at 3 Å resolution
    • Deisenhofer J, Epp O, Miki K, Huber R, Michel H. 1985. Structure of the protein subunits in the photosynthetic reaction centre of Rhodopseudomonas viridis at 3 Å resolution. Nature (London) 318:618-24
    • (1985) Nature (London) , vol.318 , pp. 618-624
    • Deisenhofer, J.1    Epp, O.2    Miki, K.3    Huber, R.4    Michel, H.5
  • 28
    • 0028972731 scopus 로고
    • 0 complex of Escherichia coli ATP synthase from isolated subunits. Varying the number of essential carboxylates by coincorporation 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 coincorporation of wild-type and mutant subunit c after purification in organic solvent. Eur. J. Biochem. 233:478-83
    • (1995) Eur. J. Biochem. , vol.233 , pp. 478-483
    • Dmitriev, O.Y.1    Altendorf, K.2    Fillingame, R.H.3
  • 32
    • 0028783369 scopus 로고
    • A barrel in the stalk
    • Dunn SD. 1995. A barrel in the stalk. Nature Struct. Biol. 2:915-18
    • (1995) Nature Struct. Biol. , vol.2 , pp. 915-918
    • Dunn, S.D.1
  • 38
    • 0026806896 scopus 로고
    • 0 sector of the ATP synthase: Insights into the molecular mechanism of function
    • 0 sector of the ATP synthase: Insights into the molecular mechanism of function. J. Bioenerg. Biomembr. 24:485-91
    • (1992) J. Bioenerg. Biomembr. , vol.24 , pp. 485-491
    • Fillingame, R.H.1
  • 41
    • 0025719966 scopus 로고
    • 0-ATP synthase reduces reactivity of aspartyl 61 with dicyclohexylcarbodiimide
    • 0-ATP synthase reduces reactivity of aspartyl 61 with dicyclohexylcarbodiimide. J. Biol. Chem. 266:20934-39
    • (1991) J. Biol. Chem. , vol.266 , pp. 20934-20939
    • Fillingame, R.H.1    Oldenburg, M.2    Fraga, D.3
  • 42
    • 0024980960 scopus 로고
    • 0-ATPase of Escherichia coli. The substitution of alanine by tyrosine at position 25 in the c-subunit affects function but not assembly
    • 0-ATPase of Escherichia coli. The substitution of alanine by tyrosine at position 25 in the c-subunit affects function but not assembly. Biochim. Biophys. Acta 978:299-304
    • (1989) Biochim. Biophys. Acta , vol.978 , pp. 299-304
    • Fimmel, A.L.1    Fordham, S.A.2
  • 43
    • 0022428004 scopus 로고
    • 0-ATPase of Escherichia coli. The substitution of alanine by threonine at position 25 in the c-subunit affects function but not assembly
    • 0-ATPase of Escherichia coli. The substitution of alanine by threonine at position 25 in the c-subunit affects function but not assembly. Biochim. Biophys. Acta 808:252-58
    • (1985) Biochim. Biophys. Acta , vol.808 , pp. 252-258
    • Fimmel, A.L.1    Jans, D.A.2    Hatch, L.3    James, L.B.4    Gibson, F.5    Cox, G.B.6
  • 44
    • 0020803047 scopus 로고
    • 0-ATPase of Escherichia coli. Substitution of proline by leucine at position 64 in the c-subunit causes loss of oxidative phosphorylation
    • 0-ATPase of Escherichia coli. Substitution of proline by leucine at position 64 in the c-subunit causes loss of oxidative phosphorylation. Biochem. J. 213:451-58
    • (1983) Biochem. J. , vol.213 , pp. 451-458
    • Fimmel, A.L.1    Jans, D.A.2    Langman, L.3    James, L.B.4    Ash, G.R.5
  • 46
    • 0024431207 scopus 로고
    • 0-ATPase of Escherichia coli. The substitution of glycine by valine at position 29 in the c-subunit affects function but not assembly
    • 0-ATPase of Escherichia coli. The substitution of glycine by valine at position 29 in the c-subunit affects function but not assembly. Biochim. Biophys. Acta 986:257-62
    • (1989) Biochim. Biophys. Acta , vol.986 , pp. 257-262
    • Fimmel, A.L.1    Norris, U.2
  • 48
    • 0029108735 scopus 로고
    • Ductin - A proton pump component, a gap junction channel and a neurotransmitter release channel
    • Finbow ME, Harrison M, Jones P. 1995. Ductin - a proton pump component, a gap junction channel and a neurotransmitter release channel. Bioessays 17:247-55
    • (1995) Bioessays , vol.17 , pp. 247-255
    • Finbow, M.E.1    Harrison, M.2    Jones, P.3
  • 50
  • 53
    • 0025877156 scopus 로고
    • 0 ATP synthase defined by random oligonucleotide-primed mutagenesis
    • 0 ATP synthase defined by random oligonucleotide-primed mutagenesis. J. Bacteriol. 173:2639-43
    • (1991) J. Bacteriol. , vol.173 , pp. 2639-2643
    • Fraga, D.1    Fillingame, R.H.2
  • 57
    • 0021136417 scopus 로고
    • Construction and characterization of an Escherichia coli strain with a uncI mutation
    • Gay NJ. 1984. Construction and characterization of an Escherichia coli strain with a uncI mutation. J. Bacteriol. 158:820-25
    • (1984) J. Bacteriol. , vol.158 , pp. 820-825
    • Gay, N.J.1
  • 58
  • 59
    • 0028044903 scopus 로고
    • 1H distance measurements to nitroxide-derivatized aspartyl-61
    • 1H distance measurements to nitroxide-derivatized aspartyl-61. Biochemistry 33:665-74
    • (1994) Biochemistry , vol.33 , pp. 665-674
    • Girvin, M.E.1    Fillingame, R.H.2
  • 61
    • 0024473883 scopus 로고
    • +-ATPase: The polar loop region of subunit c extends from the cytoplasmic face of the membrane
    • +-ATPase: The polar loop region of subunit c extends from the cytoplasmic face of the membrane. Biochemistry 28:4340-43
    • (1989) Biochemistry , vol.28 , pp. 4340-4343
    • Girvin, M.E.1    Hermolin, J.2    Pottorf, R.3    Fillingame, R.H.4
  • 62
    • 0028182747 scopus 로고
    • 0 ATP synthase: From structure to function
    • 0 ATP synthase: from structure to function. Microsc. Res. Tech. 27:294-306
    • (1994) Microsc. Res. Tech. , vol.27 , pp. 294-306
    • Gogol, E.P.1
  • 63
    • 0023666442 scopus 로고
    • 0 domains of ATP synthase visualized by electron microscopy of unstained specimens
    • 0 domains of ATP synthase visualized by electron microscopy of unstained specimens. FEBS Lett. 219:274-78
    • (1987) FEBS Lett. , vol.219 , pp. 274-278
    • Gogol, E.P.1    Lücken, U.2    Capaldi, R.A.3
  • 64
    • 0026651415 scopus 로고
    • Cooperative transient trapping of protons by structurally distorted chloroplast ATPase: Evidence for the proton well?
    • Griwatz C, Junge W. 1992. Cooperative transient trapping of protons by structurally distorted chloroplast ATPase: evidence for the proton well? Biochim. Biophys. Acta 1101:244-48
    • (1992) Biochim. Biophys. Acta , vol.1101 , pp. 244-248
    • Griwatz, C.1    Junge, W.2
  • 65
    • 0027301687 scopus 로고
    • Proton slip of the chloroplast ATPase: Its nucleotide dependence, energetic threshold, and relation to an alternating site mechanism of catalysis
    • Groth G, Junge W. 1993. Proton slip of the chloroplast ATPase: its nucleotide dependence, energetic threshold, and relation to an alternating site mechanism of catalysis. Biochemistry 32:8103-11
    • (1993) Biochemistry , vol.32 , pp. 8103-8111
    • Groth, G.1    Junge, W.2
  • 67
    • 0028855684 scopus 로고
    • ATP synthase: Activating versus catalytic proton transfer
    • Groth G, Junge W. 1995. ATP synthase: activating versus catalytic proton transfer. FEBS Lett. 358:142-44
    • (1995) FEBS Lett. , vol.358 , pp. 142-144
    • Groth, G.1    Junge, W.2
  • 68
    • 5344261738 scopus 로고    scopus 로고
    • 3H]-2-azido-ATP using the mutant βGlu381Cys:εSer108Cys to identify different β subunits by their interactions with γ and ε subunits
    • 3H]-2-azido-ATP using the mutant βGlu381Cys:εSer108Cys to identify different β subunits by their interactions with γ and ε subunits. Biochemistry 35:3875-79
    • (1996) Biochemistry , vol.35 , pp. 3875-3879
    • Grüber, G.1    Capaldi, R.A.2
  • 71
    • 0028880405 scopus 로고
    • The essential arginine residue at position 210 in the a subunit of the Escherichia coli ATP synthase can be transferred to position 252 with partial retention of activity
    • Hatch LP, Cox GB, Howitt SM. 1995. The essential arginine residue at position 210 in the a subunit of the Escherichia coli ATP synthase can be transferred to position 252 with partial retention of activity. J. Biol. Chem. 270:29407-12
    • (1995) J. Biol. Chem. , vol.270 , pp. 29407-29412
    • Hatch, L.P.1    Cox, G.B.2    Howitt, S.M.3
  • 73
    • 0029098126 scopus 로고
    • 1-ATPase as a function of the interaction of α-β subunit pairs with the γ and ε subunits
    • 1-ATPase as a function of the interaction of α-β subunit pairs with the γ and ε subunits. J. Biol. Chem. 270:20568-74
    • (1995) J. Biol. Chem. , vol.270 , pp. 20568-20574
    • Haughton, M.A.1    Capaldi, R.A.2
  • 75
  • 76
    • 0001129473 scopus 로고
    • Chloroplast ATP synthase of spinach contains nine nonidentical subunit species, six of which are encoded by plastid chromosomes in two operons in a phylogenetically conserved arrangement
    • Hennig J, Herrmann RG. 1986. Chloroplast ATP synthase of spinach contains nine nonidentical subunit species, six of which are encoded by plastid chromosomes in two operons in a phylogenetically conserved arrangement. Mol. Gen. Genet. 203:117-28
    • (1986) Mol. Gen. Genet. , vol.203 , pp. 117-128
    • Hennig, J.1    Herrmann, R.G.2
  • 77
    • 0025266245 scopus 로고
    • Orientation of subunit c of the ATP synthase of Escherichia coli - A study with peptide-specific antibodies
    • Hensel M, Deckers-Hebestreit G, Schmid R, Altendorf K. 1990. Orientation of subunit c of the ATP synthase of Escherichia coli - a study with peptide-specific antibodies. Biochim. Biophys. Acta 1016:63-70
    • (1990) Biochim. Biophys. Acta , vol.1016 , pp. 63-70
    • Hensel, M.1    Deckers-Hebestreit, G.2    Schmid, R.3    Altendorf, K.4
  • 78
    • 0028982625 scopus 로고
    • 0) of Streptomyces lividans: Sequencing of the atp operon and phylogenetic considerations with subunit β
    • 0) of Streptomyces lividans: sequencing of the atp operon and phylogenetic considerations with subunit β. Gene 152:11-17
    • (1995) Gene , vol.152 , pp. 11-17
    • Hensel, M.1    Lill, H.2    Schmid, R.3    Deckers-Hebestreit, G.4    Altendorf, K.5
  • 80
    • 0028984272 scopus 로고
    • + ATP synthase. Interdependence of subunit insertion into the membrane
    • + ATP synthase. Interdependence of subunit insertion into the membrane. J. Biol. Chem. 270:2815-17
    • (1995) J. Biol. Chem. , vol.270 , pp. 2815-2817
    • Hermolin, J.1    Fillingame, R.H.2
  • 87
    • 0023040738 scopus 로고
    • 0 ATP synthase from Neurospora crassa. Influence of oligomycin and dicyclohexylcarbodiimide
    • 0 ATP synthase from Neurospora crassa. Influence of oligomycin and dicyclohexylcarbodiimide. Eur. J. Biochem. 155:259-64
    • (1986) Eur. J. Biochem. , vol.155 , pp. 259-264
    • Hoppe, J.1    Gatti, D.2    Weber, H.3    Sebald, W.4
  • 88
    • 0020529996 scopus 로고
    • Labeling of subunit b of the ATP synthase from Escherichia coli with a photoreactive phospholipid analogue
    • Hoppe J, Montecucco C, Friedl P. 1983. Labeling of subunit b of the ATP synthase from Escherichia coli with a photoreactive phospholipid analogue. J. Biol. Chem. 258:2882-85
    • (1983) J. Biol. Chem. , vol.258 , pp. 2882-2885
    • Hoppe, J.1    Montecucco, C.2    Friedl, P.3
  • 89
    • 0019174082 scopus 로고
    • Identification of amino-acid substitutions in the proteolipid subunit of ATP synthase from dicyclohexylcarbodiimide-resistant mutants of Escherichia coli
    • Hoppe J, Schairer HU, Sebald W. 1980. Identification of amino-acid substitutions in the proteolipid subunit of ATP synthase from dicyclohexylcarbodiimide-resistant mutants of Escherichia coli. Eur. J. Biochem. 112:17-24
    • (1980) Eur. J. Biochem. , vol.112 , pp. 17-24
    • Hoppe, J.1    Schairer, H.U.2    Sebald, W.3
  • 90
    • 0022492360 scopus 로고
    • 0 is provided by amino acid residues accessible from the lipid phase
    • 0 is provided by amino acid residues accessible from the lipid phase. Biochimie 68:427-34
    • (1986) Biochimie , vol.68 , pp. 427-434
    • Hoppe, J.1    Sebald, W.2
  • 91
    • 0026661891 scopus 로고
    • 1-ATPase from Escherichia coli: Implications for structure
    • 1-ATPase from Escherichia coli: implications for structure. Proc. Natl. Acad. Sci. USA 89:9799-9803
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 9799-9803
    • Howitt, S.M.1    Cox, G.B.2
  • 93
    • 0020775144 scopus 로고
    • Mutations in the uncE gene affecting assembly of the c-subunit of the adenosine triphosphatase of Escherichia coli
    • Jans DA, Fimmel AL, Langman L, James LB, Downie JA, et al. 1983. Mutations in the uncE gene affecting assembly of the c-subunit of the adenosine triphosphatase of Escherichia coli. Biochem. J. 211:717-26
    • (1983) Biochem. J. , vol.211 , pp. 717-726
    • Jans, D.A.1    Fimmel, A.L.2    Langman, L.3    James, L.B.4    Downie, J.A.5
  • 96
    • 0027144899 scopus 로고
    • 0 ATPase in Escherichia cou by homologous recombination
    • 0 ATPase in Escherichia cou by homologous recombination. Eur. J. Biochem. 218:937-44
    • (1993) Eur. J. Biochem. , vol.218 , pp. 937-944
    • Kaim, G.1    Dimroth, P.2
  • 98
    • 0028844612 scopus 로고
    • +-coupled ATP synthesis in the Escherichia coli host cells
    • +-coupled ATP synthesis in the Escherichia coli host cells. J. Mol. Biol. 253:726-38
    • (1995) J. Mol. Biol. , vol.253 , pp. 726-738
    • Kaim, G.1    Dimroth, P.2
  • 100
    • 0026317406 scopus 로고
    • Substitution of the cysteinyl residue (Cys21) of subunit b of the ATP synthase from Eschericlna coli
    • Kauffer S, Deckers-Hebestreit G, Altendorf K. 1991. Substitution of the cysteinyl residue (Cys21) of subunit b of the ATP synthase from Eschericlna coli. Eur. J. Biochem. 202:1307-12
    • (1991) Eur. J. Biochem. , vol.202 , pp. 1307-1312
    • Kauffer, S.1    Deckers-Hebestreit, G.2    Altendorf, K.3
  • 101
    • 0027052393 scopus 로고
    • 0 ATPase from Propionigenium modestum: Discovery of a membrane potential dependent step
    • 0 ATPase from Propionigenium modestum: discovery of a membrane potential dependent step. Biochemistry 31:12665-72
    • (1992) Biochemistry , vol.31 , pp. 12665-12672
    • Kluge, C.1    Dimroth, P.2
  • 102
    • 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. 268:14557-60
    • (1993) J. Biol Chem. , vol.268 , pp. 14557-14560
    • Kluge, C.1    Dimroth, P.2
  • 103
    • 0027340171 scopus 로고
    • + concentration: Probing the binding site for the coupling ions
    • + concentration: probing the binding site for the coupling ions. Biochemistry 32:10378-86
    • (1993) Biochemistry , vol.32 , pp. 10378-10386
    • Kluge, C.1    Dimroth, P.2
  • 104
    • 0026793279 scopus 로고
    • Energy-dependent changes in conformation and catalytic activity of the chloroplast ATP synthase
    • Komatsu-Takaki M. 1992. Energy-dependent changes in conformation and catalytic activity of the chloroplast ATP synthase. J. Biol. Chem. 267:2360-63
    • (1992) J. Biol. Chem. , vol.267 , pp. 2360-2363
    • Komatsu-Takaki, M.1
  • 105
    • 0029875024 scopus 로고    scopus 로고
    • Energizing effects of illumination on the reactivities of lysine residues on the γ subunit of chloroplast ATP synthase
    • Komatsu-Takaki M. 1996. Energizing effects of illumination on the reactivities of lysine residues on the γ subunit of chloroplast ATP synthase. Eur. J. Biochem. 236:470-75
    • (1996) Eur. J. Biochem. , vol.236 , pp. 470-475
    • Komatsu-Takaki, M.1
  • 106
    • 0022835820 scopus 로고
    • 0 portion of the Escherichia coli proton translocating ATPase
    • 0 portion of the Escherichia coli proton translocating ATPase. J. Biol. Chem. 261:10037-42
    • (1986) J. Biol. Chem. , vol.261 , pp. 10037-10042
    • Kumamoto, C.A.1    Simoni, R.D.2
  • 107
    • 0023644619 scopus 로고
    • A mutation of the c subunit of the Escherichia coli proton-translocating ATPase that suppresses the effects of a mutant b subunit
    • Kumamoto CA, Simoni RD. 1987. A mutation of the c subunit of the Escherichia coli proton-translocating ATPase that suppresses the effects of a mutant b subunit. J. Biol. Chem. 262:3060-64
    • (1987) J. Biol. Chem. , vol.262 , pp. 3060-3064
    • Kumamoto, C.A.1    Simoni, R.D.2
  • 108
    • 0026512826 scopus 로고
    • 0 ATP synthase affect its inhibitory properties
    • 0 ATP synthase affect its inhibitory properties. J. Bacteriol. 174:633-37
    • (1992) J. Bacteriol. , vol.174 , pp. 633-637
    • LaRoe, D.J.1    Vik, S.B.2
  • 110
    • 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 27:7531-37
    • (1988) Biochemistry , vol.27 , pp. 7531-7537
    • Laubinger, W.1    Dimroth, P.2
  • 111
    • 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 28:7194-98
    • (1989) Biochemistry , vol.28 , pp. 7194-7198
    • Laubinger, W.1    Dimroth, P.2
  • 112
    • 0023907575 scopus 로고
    • Synthetic amphiphilic peptide models for protein ion channels
    • Lear JD, Wasserman ZR, DeGrado WF. 1988. Synthetic amphiphilic peptide models for protein ion channels. Science 240:1177-81
    • (1988) Science , vol.240 , pp. 1177-1181
    • Lear, J.D.1    Wasserman, Z.R.2    DeGrado, W.F.3
  • 113
    • 0029053721 scopus 로고
    • Experimental evidence for hydrogen-bonded network proton transfer in bacteriorhodopsin shown by Fourier-transform infrared spectroscopy using azide as catalyst
    • Le Coutre J, Tittor J, Oesterhelt D, Gerwert K. 1995. Experimental evidence for hydrogen-bonded network proton transfer in bacteriorhodopsin shown by Fourier-transform infrared spectroscopy using azide as catalyst. Proc. Natl. Acad. Sci. USA 92:4962-66
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 4962-4966
    • Le Coutre, J.1    Tittor, J.2    Oesterhelt, D.3    Gerwert, K.4
  • 118
    • 0026602025 scopus 로고
    • Water structural changes in the bacteriorhodopsin photocycle: Analysis by Fourier transform infrared spectroscopy
    • Maeda A, Sasaki J, Shichida Y, Yoshizawa T. 1992. Water structural changes in the bacteriorhodopsin photocycle: analysis by Fourier transform infrared spectroscopy. Biochemistry 31:462-67
    • (1992) Biochemistry , vol.31 , pp. 462-467
    • Maeda, A.1    Sasaki, J.2    Shichida, Y.3    Yoshizawa, T.4
  • 121
    • 0025789653 scopus 로고
    • 0 ATP synthase in Escherichia coli: Glu-77 through Gin-85
    • 0 ATP synthase in Escherichia coli: Glu-77 through Gin-85. J. Bacteriol. 173:7240-48
    • (1991) J. Bacteriol. , vol.173 , pp. 7240-7248
    • McCormick, K.A.1    Cain, B.D.2
  • 123
    • 0025855423 scopus 로고
    • Catalytic site nucleotide and inorganic phosphate dependence of the conformation of the ε subunit in Escherichia coli adenosinetriphosphatase
    • Mendel-Hartvig J, Capaldi RA. 1991. Catalytic site nucleotide and inorganic phosphate dependence of the conformation of the ε subunit in Escherichia coli adenosinetriphosphatase. Biochemistry 30:1278-84
    • (1991) Biochemistry , vol.30 , pp. 1278-1284
    • Mendel-Hartvig, J.1    Capaldi, R.A.2
  • 124
    • 0026334742 scopus 로고
    • Nucleotide-dependent and dicyclohexylcarbodiimide-sensitive conformational changes in the ε subunit of Escherichia coli ATP synthase
    • Mendel-Hartvig J, Capaldi RA. 1991. Nucleotide-dependent and dicyclohexylcarbodiimide-sensitive conformational changes in the ε subunit of Escherichia coli ATP synthase. Biochemistry 30:10987-91
    • (1991) Biochemistry , vol.30 , pp. 10987-10991
    • Mendel-Hartvig, J.1    Capaldi, R.A.2
  • 125
    • 0025871645 scopus 로고
    • Structure-function relationships of domains of the δ subunit in Escherichia coli adenosine triphosphatase
    • Mendel-Hartvig J, Capaldi RA. 1991. Structure-function relationships of domains of the δ subunit in Escherichia coli adenosine triphosphatase. Biochim. Biophys. Acta 1060:115-24
    • (1991) Biochim. Biophys. Acta , vol.1060 , pp. 115-124
    • Mendel-Hartvig, J.1    Capaldi, R.A.2
  • 128
    • 0026406805 scopus 로고
    • Foundations of vectorial metabolism and osmochemistry
    • Mitchell P. 1991. Foundations of vectorial metabolism and osmochemistry. Biosci. Rep. 11:297-346
    • (1991) Biosci. Rep. , vol.11 , pp. 297-346
    • Mitchell, P.1
  • 131
    • 0020967882 scopus 로고
    • Hydrogen bonded chain mechanisms for proton conduction and proton pumping
    • Nagle JF, Tristram-Nagle S. 1983. Hydrogen bonded chain mechanisms for proton conduction and proton pumping. J. Membr. Biol. 74:1-14
    • (1983) J. Membr. Biol. , vol.74 , pp. 1-14
    • Nagle, J.F.1    Tristram-Nagle, S.2
  • 132
    • 0023960320 scopus 로고
    • 0 sector of mitochondrial ATP synthase
    • 0 sector of mitochondrial ATP synthase. Trends Genet. 4:46-52
    • (1988) Trends Genet. , vol.4 , pp. 46-52
    • Nagley, P.1
  • 133
    • 0029040551 scopus 로고
    • The ATP synthase γ subunit. Suppressor mutagenesis reveals three helical regions involved in energy coupling
    • Nakamoto RK, Al-Shawi MK, Futai M. 1995. The ATP synthase γ subunit. Suppressor mutagenesis reveals three helical regions involved in energy coupling. J. Biol. Chem. 270:14042-46
    • (1995) J. Biol. Chem. , vol.270 , pp. 14042-14046
    • Nakamoto, R.K.1    Al-Shawi, M.K.2    Futai, M.3
  • 134
    • 0027471965 scopus 로고
    • The γ subunit of the Escherichia coli ATP synthase. Mutations in the carboxyl-terminal region restore energy coupling to the amino-terminal mutant γMet-23 → Lys
    • Nakamoto RK, Maeda M, Futai M. 1993. The γ subunit of the Escherichia coli ATP synthase. Mutations in the carboxyl-terminal region restore energy coupling to the amino-terminal mutant γMet-23 → Lys. J. Biol. Chem. 268:867-72
    • (1993) J. Biol. Chem. , vol.268 , pp. 867-872
    • Nakamoto, R.K.1    Maeda, M.2    Futai, M.3
  • 135
    • 0026563170 scopus 로고
    • Evolution of organellar proton-ATPases
    • Nelson N. 1992. Evolution of organellar proton-ATPases. Biochim. Biophys. Acta 1100:109-24
    • (1992) Biochim. Biophys. Acta , vol.1100 , pp. 109-124
    • Nelson, N.1
  • 136
    • 0000531571 scopus 로고
    • A proton pathway with large proton polarizability and the proton pumping mechanism in bacteriorhodopsin - Fourier transform difference spectra of photoproducts of bacteriorhodopsin and its pentademethyl analogue
    • Olejnik J, Brzezinski B, Zundel G. 1992. A proton pathway with large proton polarizability and the proton pumping mechanism in bacteriorhodopsin - Fourier transform difference spectra of photoproducts of bacteriorhodopsin and its pentademethyl analogue. J. Mol. Struct. 271:157-73
    • (1992) J. Mol. Struct. , vol.271 , pp. 157-173
    • Olejnik, J.1    Brzezinski, B.2    Zundel, G.3
  • 137
    • 0028339083 scopus 로고
    • +-ATPase (ATP synthase). An Escherichia coli α subunit mutation (Arg-α296 → Cys) restores coupling efficiency to the deleterious β subunit mutant (Ser-β174 → Phe)
    • +-ATPase (ATP synthase). An Escherichia coli α subunit mutation (Arg-α296 → Cys) restores coupling efficiency to the deleterious β subunit mutant (Ser-β174 → Phe). J. Biol. Chem. 269:10265-69
    • (1994) J. Biol. Chem. , vol.269 , pp. 10265-10269
    • Omote, H.1    Park, M.Y.2    Maeda, M.3    Futai, M.4
  • 139
    • 0025298852 scopus 로고
    • Water molecules and exchangeable hydrogen ions at the active centre of bacteriorhodopsin localized by neutron diffraction. Elements of the proton pathway?
    • Papadopoulos G, Dencher NA, Zaccai G, Büldt G. 1990. Water molecules and exchangeable hydrogen ions at the active centre of bacteriorhodopsin localized by neutron diffraction. Elements of the proton pathway? J. Mol. Biol. 214:15-19
    • (1990) J. Mol. Biol. , vol.214 , pp. 15-19
    • Papadopoulos, G.1    Dencher, N.A.2    Zaccai, G.3    Büldt, G.4
  • 141
    • 0021825076 scopus 로고
    • Mechanism of inhibition of mitochondrial adenosine triphosphatase by dicyclohexylcarbodiimide and oligomycin: Relationship to ATP synthesis
    • Penefsky HS. 1985. Mechanism of inhibition of mitochondrial adenosine triphosphatase by dicyclohexylcarbodiimide and oligomycin: relationship to ATP synthesis. Proc. Natl. Acad. Sci. USA 82:1589-93
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 1589-1593
    • Penefsky, H.S.1
  • 142
    • 0021112492 scopus 로고
    • 1 and the membrane sector of the proton-ATPase of Escherichia coli. Role of subunit "b" (uncF protein)
    • 1 and the membrane sector of the proton-ATPase of Escherichia coli. Role of subunit "b" (uncF protein). J. Biol. Chem. 258:9793-9800
    • (1983) J. Biol. Chem. , vol.258 , pp. 9793-9800
    • Perlin, D.S.1    Cox, D.N.2    Senior, A.E.3
  • 143
    • 0022020183 scopus 로고
    • Functional effects and cross-reactivity of antibody to purified subunit b (uncF protein) of Escherichia coli proton-ATPase
    • Perlin DS, Senior AE. 1985. Functional effects and cross-reactivity of antibody to purified subunit b (uncF protein) of Escherichia coli proton-ATPase. Arch. Biochem. Biophys. 236:603-11
    • (1985) Arch. Biochem. Biophys. , vol.236 , pp. 603-611
    • Perlin, D.S.1    Senior, A.E.2
  • 145
  • 146
    • 0023645804 scopus 로고
    • Energy-dependent changes in the conformation of the ε subunit of the chloroplast ATP synthase
    • Richter ML, McCarty RE. 1987. Energy-dependent changes in the conformation of the ε subunit of the chloroplast ATP synthase. J. Biol Chem. 262:15037-40
    • (1987) J. Biol Chem. , vol.262 , pp. 15037-15040
    • Richter, M.L.1    McCarty, R.E.2
  • 147
    • 0029893335 scopus 로고    scopus 로고
    • Intersubunit rotation in active F-ATPase
    • In press
    • Sabbert D, Engelbrecht S, Junge W. 1996. Intersubunit rotation in active F-ATPase. Nature. In press
    • (1996) Nature
    • Sabbert, D.1    Engelbrecht, S.2    Junge, W.3
  • 151
    • 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. 51:477-97
    • (1987) Microbiol. Rev. , vol.51 , pp. 477-497
    • Schneider, E.1    Altendorf, K.2
  • 152
    • 0025058420 scopus 로고
    • Overproduction and purification of the uncI gene product of the ATP synthase of Escherichia coli
    • Schneppe B, Deckers-Hebestreit G, Altendorf K. 1990. Overproduction and purification of the uncI gene product of the ATP synthase of Escherichia coli. J. Biol. Chem. 265:389-95
    • (1990) J. Biol. Chem. , vol.265 , pp. 389-395
    • Schneppe, B.1    Deckers-Hebestreit, G.2    Altendorf, K.3
  • 153
    • 0026075014 scopus 로고
    • Detection and localization of the i protein in Escherichia coli cells using antibodies
    • Schneppe B, Deckers-Hebestreit G, Altendorf K. 1991. Detection and localization of the i protein in Escherichia coli cells using antibodies. FEBS Lett. 292:145-47
    • (1991) FEBS Lett. , vol.292 , pp. 145-147
    • Schneppe, B.1    Deckers-Hebestreit, G.2    Altendorf, K.3
  • 154
    • 0025833905 scopus 로고
    • Translation of the first gene of the Escherichia coli unc operon. Selection of the start codon and control of initiation efficiency
    • Schneppe B, Deckers-Hebestreit G, McCarthy JEG, Altendorf K. 1991. Translation of the first gene of the Escherichia coli unc operon. Selection of the start codon and control of initiation efficiency. J. Biol. Chem. 266:21090-98
    • (1991) J. Biol. Chem. , vol.266 , pp. 21090-21098
    • Schneppe, B.1    Deckers-Hebestreit, G.2    McCarthy, J.E.G.3    Altendorf, K.4
  • 156
    • 0025338413 scopus 로고
    • The proton-translocating ATPase of Escherichia coli
    • Senior AE. 1990. The proton-translocating ATPase of Escherichia coli. Annu. Rev. Biophys. Biophys. Chem. 19:7-41
    • (1990) Annu. Rev. Biophys. Biophys. Chem. , vol.19 , pp. 7-41
    • Senior, A.E.1
  • 157
    • 0029099451 scopus 로고
    • +-translocating ATPases in Methanobacterium thermoautotrophicum and their possible function under alkaline conditions
    • +-translocating ATPases in Methanobacterium thermoautotrophicum and their possible function under alkaline conditions. FEBS Lett. 371:119-22
    • (1995) FEBS Lett. , vol.371 , pp. 119-122
    • Smigán, P.1    Majernik, A.2    Polák, P.3    Hapala, I.4    Greksák, M.5
  • 158
    • 0023929766 scopus 로고
    • Effect of an uncE ribosome-binding site mutation on the synthesis and assembly of the Escherichia coli proton-translocating ATPase
    • Solomon KA, Brusilow WSA. 1988. Effect of an uncE ribosome-binding site mutation on the synthesis and assembly of the Escherichia coli proton-translocating ATPase. J. Biol. Chem. 263:5402-7
    • (1988) J. Biol. Chem. , vol.263 , pp. 5402-5407
    • Solomon, K.A.1    Brusilow, W.S.A.2
  • 159
    • 0024307717 scopus 로고
    • Use of lacZ fusions to measure in vivo expression of the first three genes of the Escherichia coli unc operon
    • Solomon KA, Hsu DKW, Brusilow WSA. 1989. Use of lacZ fusions to measure in vivo expression of the first three genes of the Escherichia coli unc operon. J. Bacteriol. 171:3039-45
    • (1989) J. Bacteriol. , vol.171 , pp. 3039-3045
    • Solomon, K.A.1    Hsu, D.K.W.2    Brusilow, W.S.A.3
  • 160
    • 0024277334 scopus 로고
    • 0 part of the ATP synthase from Escherichia coli. Influence of subunits a, and b, on the structure of subunit c
    • 0 part of the ATP synthase from Escherichia coli. Influence of subunits a, and b, on the structure of subunit c. Eur. J. Biochem. 170:627-30
    • (1988) Eur. J. Biochem. , vol.170 , pp. 627-630
    • Steffens, K.1    Hoppe, J.2    Altendorf, K.3
  • 162
    • 0006151486 scopus 로고
    • 0) as revealed by chemical protein cross-linking
    • 0) as revealed by chemical protein cross-linking. FEBS Lett. 201:63-68
    • (1986) FEBS Lett. , vol.201 , pp. 63-68
    • Süss, K.H.1
  • 166
    • 0028803285 scopus 로고
    • Cation-selectivity of the L-glutamate transporters of Escherichia coli, Bacillus stearothermophilus and Bacillus caldotenax: Dependence on the environment in which the proteins are expressed
    • Tolner B, Ubbink-Kok T, Poolman B, Konings WN. 1995. Cation-selectivity of the L-glutamate transporters of Escherichia coli, Bacillus stearothermophilus and Bacillus caldotenax: dependence on the environment in which the proteins are expressed. Mol. Microbiol. 18:123-33
    • (1995) Mol. Microbiol. , vol.18 , pp. 123-133
    • Tolner, B.1    Ubbink-Kok, T.2    Poolman, B.3    Konings, W.N.4
  • 167
    • 0027478779 scopus 로고
    • The topological analysis of integral cytoplasmic membrane proteins
    • Traxler B, Boyd D, Beckwith J. 1993. The topological analysis of integral cytoplasmic membrane proteins. J. Membr. Biol. 132:1-11
    • (1993) J. Membr. Biol. , vol.132 , pp. 1-11
    • Traxler, B.1    Boyd, D.2    Beckwith, J.3
  • 168
    • 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. 269:30364-69
    • (1994) J. Biol. Chem. , vol.269 , pp. 30364-30369
    • Vik, S.B.1    Antonio, B.J.2
  • 169
    • 0023819093 scopus 로고
    • 0-ATPase from Escherichia coli. Mutations at Glu-196, Pro-190, and Ser-199
    • 0-ATPase from Escherichia coli. Mutations at Glu-196, Pro-190, and Ser-199. J. Biol. Chem. 263:6599-605
    • (1988) J. Biol. Chem. , vol.263 , pp. 6599-6605
    • Vik, S.B.1    Cain, B.D.2    Chun, K.T.3    Simoni, R.D.4
  • 170
    • 0026479944 scopus 로고
    • 0 ATP synthase using variational and hydrophobic moment analyses
    • 0 ATP synthase using variational and hydrophobic moment analyses. Biochim. Biophys. Acta 1140:199-207
    • (1992) Biochim. Biophys. Acta , vol.1140 , pp. 199-207
    • Vik, S.B.1    Dao, N.N.2
  • 171
    • 0030044336 scopus 로고    scopus 로고
    • +/ATP coupling ratio of the ATP synthase from thiol-modulated chloroplasts and two cyanobacterial strains is four
    • +/ATP coupling ratio of the ATP synthase from thiol-modulated chloroplasts and two cyanobacterial strains is four. FEBS Lett. 379:309-13
    • (1996) FEBS Lett. , vol.379 , pp. 309-313
    • Van Walraven, H.S.1    Strotmann, H.2    Schwarz, O.3    Rumberg, B.4
  • 172
    • 0026716643 scopus 로고
    • Membrane protein structure prediction. Hydrophobicity analysis and the positive-inside rule
    • von Heijne G. 1992. Membrane protein structure prediction. Hydrophobicity analysis and the positive-inside rule. J. Mol. Biol. 225:487-94
    • (1992) J. Mol. Biol. , vol.225 , pp. 487-494
    • Von Heijne, G.1
  • 173
    • 0020439660 scopus 로고
    • The membrane bound ATP synthase of Escherichia coli: A review of structural and functional analyses of the atp operon
    • von Meyenburg K, Jørgensen BB, Nielsen J, Hansen FG, Michelsen O. 1982. The membrane bound ATP synthase of Escherichia coli: a review of structural and functional analyses of the atp operon. Tokai. J. Exp. Clin. Med. 7:23-31
    • (1982) Tokai. J. Exp. Clin. Med. , vol.7 , pp. 23-31
    • Von Meyenburg, K.1    Jørgensen, B.B.2    Nielsen, J.3    Hansen, F.G.4    Michelsen, O.5
  • 174
    • 0020002423 scopus 로고
    • 1-ATPase interacts with a membrane protein component of a proton channel
    • 1-ATPase interacts with a membrane protein component of a proton channel. Nature (London) 298:867-69
    • (1982) Nature (London) , vol.298 , pp. 867-869
    • Walker, J.E.1    Saraste, M.2    Gay, N.J.3
  • 175
    • 0021756359 scopus 로고
    • The unc operon. Nucleotide sequence, regulation and structure of ATP-synthase
    • Walker JE, Saraste M, Gay NJ. 1984. The unc operon. Nucleotide sequence, regulation and structure of ATP-synthase. Biochim. Biophys. Acta 768:164-200
    • (1984) Biochim. Biophys. Acta , vol.768 , pp. 164-200
    • Walker, J.E.1    Saraste, M.2    Gay, N.J.3
  • 178
    • 12044253201 scopus 로고
    • Aspects of subunit interactions in the chloroplast ATP synthase. I. Isolation of a chloroplast coupling factor 1-subunit III complex from spinach thylakoids
    • Wetzel CM, McCarty RE. 1993. Aspects of subunit interactions in the chloroplast ATP synthase. I. Isolation of a chloroplast coupling factor 1-subunit III complex from spinach thylakoids. Plant Physiol. 102:241-49
    • (1993) Plant Physiol. , vol.102 , pp. 241-249
    • Wetzel, C.M.1    McCarty, R.E.2
  • 179
    • 0028970620 scopus 로고
    • Structural features of the ε subunit of the Escherichia coli ATP synthase determined by NMR spectroscopy
    • Wilkens S, Dahlquist FW, McIntosh LP, Donaldson LW, Capaldi RA. 1995. Structural features of the ε subunit of the Escherichia coli ATP synthase determined by NMR spectroscopy. Nature Struct. Biol. 2:961-67
    • (1995) Nature Struct. Biol. , vol.2 , pp. 961-967
    • Wilkens, S.1    Dahlquist, F.W.2    McIntosh, L.P.3    Donaldson, L.W.4    Capaldi, R.A.5
  • 182
    • 0027508170 scopus 로고
    • 2+-binding site on the lumenal side of the thylakoid membrane
    • 2+-binding site on the lumenal side of the thylakoid membrane. FEBS Lett. 336:95-99
    • (1993) FEBS Lett. , vol.336 , pp. 95-99
    • Zakharov, S.D.1    Ewy, R.G.2    Dilley, R.A.3
  • 184
    • 0028800799 scopus 로고
    • +-transporting ATP synthase by directed mutagenesis of subunit c
    • +-transporting ATP synthase by directed mutagenesis of subunit c. J. Biol. Chem. 270:87-93
    • (1995) J. Biol. Chem. , vol.270 , pp. 87-93
    • Zhang, Y.1    Fillingame, R.H.2
  • 187
    • 0342637132 scopus 로고
    • Proton polarizability of hydrogen bonded systems due to collective proton motion - With a remark to the proton pathways in bacteriorhodopsin
    • ed. T Bountis, New York: Plenum
    • Zundel G, Brzezinski B. 1992. Proton polarizability of hydrogen bonded systems due to collective proton motion - with a remark to the proton pathways in bacteriorhodopsin. In Proton Transfer in Hydrogen-Bonded Systems, ed. T Bountis, pp. 153-66. New York: Plenum
    • (1992) Proton Transfer in Hydrogen-Bonded Systems , pp. 153-166
    • Zundel, G.1    Brzezinski, B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.