메뉴 건너뛰기




Volumn 10, Issue 6, 2011, Pages 2703-2714

Identification of chromatophore membrane protein complexes formed under different nitrogen availability conditions in Rhodospirillum rubrum

Author keywords

amphiphile; Blue Native; chromatophore subproteome; nitrogen metabolism; Orbitrap; Rhodospirillum rubrum

Indexed keywords

AMPHOPHILE; BACTERIAL PROTEIN; ELECTRON TRANSFERRING FLAVOPROTEIN; MEMBRANE PROTEIN; NITROGEN; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE; SUCCINATE DEHYDROGENASE;

EID: 79958199290     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr100838x     Document Type: Article
Times cited : (11)

References (73)
  • 1
    • 4844225111 scopus 로고    scopus 로고
    • Magnetosome formation in prokaryotes
    • DOI 10.1038/nrmicro842
    • Bazylinski, D. A.; Frankel, R. B. Magnetosome formation in prokaryotes Nat. Rev. Microbiol. 2004, 2 (3) 217-30 (Pubitemid 39496780)
    • (2004) Nature Reviews Microbiology , vol.2 , Issue.3 , pp. 217-230
    • Bazylinski, D.A.1    Frankel, R.B.2
  • 2
    • 30844471175 scopus 로고    scopus 로고
    • Magnetosomes are cell membrane imaginations organized by the actin-like protein MamK
    • DOI 10.1126/science.1123231
    • Komeili, A.; Li, Z.; Newman, D. K.; Jensen, G. J. Magnetosomes are cell membrane invaginations organized by the actin-like protein MamK Science 2006, 311 (5758) 242-5 (Pubitemid 43108192)
    • (2006) Science , vol.311 , Issue.5758 , pp. 242-245
    • Komeili, A.1    Li, Z.2    Newman, D.K.3    Jensen, G.J.4
  • 3
    • 33751202658 scopus 로고    scopus 로고
    • Development of the bacterial photosynthetic apparatus
    • DOI 10.1016/j.mib.2006.10.005, PII S1369527406001573, Growth and Development
    • Tavano, C. L.; Donohue, T. J. Development of the bacterial photosynthetic apparatus Curr. Opin. Microbiol. 2006, 9 (6) 625-31 (Pubitemid 44791988)
    • (2006) Current Opinion in Microbiology , vol.9 , Issue.6 , pp. 625-631
    • Tavano, C.L.1    Donohue, T.J.2
  • 4
    • 0242603733 scopus 로고
    • Chromatophores of Rhodospirillum rubrum
    • Pardee, A. B.; Schachman, H. K.; Stanier, R. Y. Chromatophores of Rhodospirillum rubrum Nature 1952, 169 (4294) 282-3
    • (1952) Nature , vol.169 , Issue.4294 , pp. 282-3
    • Pardee, A.B.1    Schachman, H.K.2    Stanier, R.Y.3
  • 5
    • 49749191013 scopus 로고
    • Photophosphorylation by isolated chromatophores of the purple sulfur bacteria
    • Anderson, I. C.; Fuller, R. C. Photophosphorylation by isolated chromatophores of the purple sulfur bacteria Arch. Biochem. Biophys. 1958, 76 (1) 168-79
    • (1958) Arch. Biochem. Biophys. , vol.76 , Issue.1 , pp. 168-79
    • Anderson, I.C.1    Fuller, R.C.2
  • 6
    • 50549155053 scopus 로고
    • Studies on bacterial photophosphorylation. I. Kinetics of photophosphorylation in Rhodospirillum rubrum chromatophores by flashing light
    • Nishimura, M. Studies on bacterial photophosphorylation. I. Kinetics of photophosphorylation in Rhodospirillum rubrum chromatophores by flashing light Biochim. Biophys. Acta 1962, 57 (1) 88-95
    • (1962) Biochim. Biophys. Acta , vol.57 , Issue.1 , pp. 88-95
    • Nishimura, M.1
  • 7
    • 0035852875 scopus 로고    scopus 로고
    • A
    • DOI 10.1021/bi001686a
    • Ginet, N.; Lavergne, J. Equilibrium and kinetic parameters for the binding of inhibitors to the QB pocket in bacterial chromatophores: dependence on the state of QA Biochemistry 2001, 40 (6) 1812-23 (Pubitemid 32144054)
    • (2001) Biochemistry , vol.40 , Issue.6 , pp. 1812-1823
    • Ginet, N.1    Lavergne, J.2
  • 8
    • 0029088139 scopus 로고
    • Direct observation of sub-picosecond equilibration of excitation energy in the light-harvesting antenna of Rhodospirillum rubrum
    • Visser, H. M.; Somsen, O. J.; van Mourik, F.; Lin, S.; van Stokkum, I. H.; van Grondelle, R. Direct observation of sub-picosecond equilibration of excitation energy in the light-harvesting antenna of Rhodospirillum rubrum Biophys. J. 1995, 69 (3) 1083-99
    • (1995) Biophys. J. , vol.69 , Issue.3 , pp. 1083-99
    • Visser, H.M.1    Somsen, O.J.2    Van Mourik, F.3    Lin, S.4    Van Stokkum, I.H.5    Van Grondelle, R.6
  • 9
    • 0024789682 scopus 로고
    • 1-ATPase and the stoichiometry of its inhibition by oligomycin in Rhodospirillum rubrum chromatophores
    • DOI 10.1111/j.1432-1033.1989.tb15213.x
    • 1-ATPase and the stoichiometry of its inhibition by oligomycin in Rhodospirillum rubrum chromatophores Eur. J. Biochem. 1989, 186 (1-2) 333-7 (Pubitemid 20015162)
    • (1989) European Journal of Biochemistry , vol.186 , Issue.1-2 , pp. 333-337
    • Norling, B.1    Strid, A.2    Tourikas, C.3    Nyren, P.4
  • 11
    • 61649091917 scopus 로고
    • Metabolic patterns in photosynthetic bacteria
    • Gest, H. Metabolic patterns in photosynthetic bacteria Bacteriol. Rev. 1951, 15 (4) 183-210
    • (1951) Bacteriol. Rev. , vol.15 , Issue.4 , pp. 183-210
    • Gest, H.1
  • 12
    • 0001035440 scopus 로고
    • Evidence for a nitrogenase system in the photosynthetic bacterium Rhodospirillum rubrum
    • Kamen, M. D.; Gest, H. Evidence for a nitrogenase system in the photosynthetic bacterium Rhodospirillum rubrum Science 1949, 109 (2840) 560
    • (1949) Science , vol.109 , Issue.2840 , pp. 560
    • Kamen, M.D.1    Gest, H.2
  • 14
    • 4344704870 scopus 로고    scopus 로고
    • Genetic regulation of biological nitrogen fixation
    • DOI 10.1038/nrmicro954
    • Dixon, R.; Kahn, D. Genetic regulation of biological nitrogen fixation Nat. Rev. Microbiol. 2004, 2 (8) 621-31 (Pubitemid 39200045)
    • (2004) Nature Reviews Microbiology , vol.2 , Issue.8 , pp. 621-631
    • Dixon, R.1    Kahn, D.2
  • 15
    • 1542357694 scopus 로고    scopus 로고
    • Identification of critical residues in GlnB for its activation of NifA activity in the photosynthetic bacterium Rhodospirillum rubrum
    • DOI 10.1073/pnas.0306763101
    • Zhang, Y.; Pohlmann, E. L.; Roberts, G. P. Identification of critical residues in GlnB for its activation of NifA activity in the photosynthetic bacterium Rhodospirillum rubrum Proc. Natl. Acad. Sci. U.S.A. 2004, 101 (9) 2782-7 (Pubitemid 38327688)
    • (2004) Proceedings of the National Academy of Sciences of the United States of America , vol.101 , Issue.9 , pp. 2782-2787
    • Zhang, Y.1    Pohlmann, E.L.2    Roberts, G.P.3
  • 16
    • 3142566473 scopus 로고    scopus 로고
    • GlnB is specifically required for Azospirillum brasilense NifA activity in Escherichia coli
    • DOI 10.1016/j.resmic.2004.03.002, PII S0923250804000725
    • Araujo, L. M.; Monteiro, R. A.; Souza, E. M.; Steffens, M. B.; Rigo, L. U.; Pedrosa, F. O.; Chubatsu, L. S. GlnB is specifically required for Azospirillum brasilense NifA activity in Escherichia coli Res. Microbiol. 2004, 155 (6) 491-5 (Pubitemid 38900830)
    • (2004) Research in Microbiology , vol.155 , Issue.6 , pp. 491-495
    • Araujo, L.M.1    Monteiro, R.A.2    Souza, E.M.3    Steffens, M.B.R.4    Rigo, L.U.5    Pedrosa, F.O.6    Chubatsu, L.S.7
  • 17
    • 2642524290 scopus 로고    scopus 로고
    • 2 assimilation, nitrogen fixation, hydrogen metabolism and energy generation
    • DOI 10.1016/j.femsre.2004.01.002, PII S0168644504000130
    • 2 assimilation, nitrogen fixation, hydrogen metabolism and energy generation FEMS Microbiol. Rev. 2004, 28 (3) 353-76 (Pubitemid 38721409)
    • (2004) FEMS Microbiology Reviews , vol.28 , Issue.3 , pp. 353-376
    • Dubbs, J.M.1    Tabita, F.R.2
  • 18
    • 0036882111 scopus 로고    scopus 로고
    • 2 fixation operons of Rhodobacter sphaeroides by the Prr/Reg two-component system during chemoautotrophic growth
    • DOI 10.1128/JB.184.23.6654-6664.2002
    • 2 fixation operons of Rhodobacter sphaeroides by the Prr/Reg two-component system during chemoautotrophic growth J. Bacteriol. 2002, 184 (23) 6654-64 (Pubitemid 35332570)
    • (2002) Journal of Bacteriology , vol.184 , Issue.23 , pp. 6654-6664
    • Gibson, J.L.1    Dubbs, J.M.2    Tabita, F.R.3
  • 19
    • 0029855868 scopus 로고    scopus 로고
    • A global two component signal transduction system that integrates the control of photosynthesis, carbon dioxide assimilation, and nitrogen fixation
    • DOI 10.1073/pnas.93.25.14515
    • Joshi, H. M.; Tabita, F. R. A global two component signal transduction system that integrates the control of photosynthesis, carbon dioxide assimilation, and nitrogen fixation Proc. Natl. Acad. Sci. U.S.A. 1996, 93 (25) 14515-20 (Pubitemid 26418998)
    • (1996) Proceedings of the National Academy of Sciences of the United States of America , vol.93 , Issue.25 , pp. 14515-14520
    • Joshi, H.M.1    Tabita, F.R.2
  • 20
    • 53049090836 scopus 로고    scopus 로고
    • Comparative proteomic studies in Rhodospirillum rubrum grown under different nitrogen conditions
    • Selao, T. T.; Nordlund, S.; Noren, A. Comparative proteomic studies in Rhodospirillum rubrum grown under different nitrogen conditions J. Proteome Res. 2008, 7 (8) 3267-75
    • (2008) J. Proteome Res. , vol.7 , Issue.8 , pp. 3267-75
    • Selao, T.T.1    Nordlund, S.2    Noren, A.3
  • 21
    • 1642391439 scopus 로고    scopus 로고
    • The fixABCX Genes in Rhodospirillum rubrum Encode a Putative Membrane Complex Participating in Electron Transfer to Nitrogenase
    • DOI 10.1128/JB.186.7.2052-2060.2004
    • Edgren, T.; Nordlund, S. The fixABCX genes in Rhodospirillum rubrum encode a putative membrane complex participating in electron transfer to nitrogenase J. Bacteriol. 2004, 186 (7) 2052-60 (Pubitemid 38381193)
    • (2004) Journal of Bacteriology , vol.186 , Issue.7 , pp. 2052-2060
    • Edgren, T.1    Nordlund, S.2
  • 22
    • 33745023377 scopus 로고    scopus 로고
    • Two pathways of electron transport to nitrogenase in Rhodospirillum rubrum: The major pathway is dependent on the fix gene products
    • DOI 10.1111/j.1574-6968.2006.00297.x
    • Edgren, T.; Nordlund, S. Two pathways of electron transport to nitrogenase in Rhodospirillum rubrum: the major pathway is dependent on the fix gene products FEMS Microbiol. Lett. 2006, 260 (1) 30-5 (Pubitemid 43873568)
    • (2006) FEMS Microbiology Letters , vol.260 , Issue.1 , pp. 30-35
    • Edgren, T.1    Nordlund, S.2
  • 23
    • 17144366135 scopus 로고    scopus 로고
    • Electron transport to nitrogenase in Rhodospirillum rubrum: Identification of a new fdxN gene encoding the primary electron donor to nitrogenase
    • DOI 10.1016/j.femsle.2005.03.024
    • Edgren, T.; Nordlund, S. Electron transport to nitrogenase in Rhodospirillum rubrum: identification of a new fdxN gene encoding the primary electron donor to nitrogenase FEMS Microbiol. Lett. 2005, 245 (2) 345-51 (Pubitemid 40523653)
    • (2005) FEMS Microbiology Letters , vol.245 , Issue.2 , pp. 345-351
    • Edgren, T.1    Nordlund, S.2
  • 24
    • 0030727913 scopus 로고    scopus 로고
    • Electron transport to nitrogenase in Rhodospirillum rubrum: Role of energization of the chromatophore membrane
    • DOI 10.1023/A:1005812611204
    • Lindblad, A.; Nordlund, S. Electron transport to nitrogenase in Rhodospirillum rubrum: Role of energization of the chromatophore membrane Photosynth. Res. 1997, 53 (1) 23-8 (Pubitemid 27490943)
    • (1997) Photosynthesis Research , vol.53 , Issue.1 , pp. 23-28
    • Lindblad, A.1    Nordlund, S.2
  • 25
    • 0030914611 scopus 로고    scopus 로고
    • Electron transport to nitrogenase in Rhodospirillum rubrum: The role of NAD(P)H as electron donor and the effect of fluoroacetate on nitrogenase activity
    • DOI 10.1016/S0378-1097(97)00127-4, PII S0378109797001274
    • Brostedt, E.; Lindblad, A.; Jansson, J.; Nordlund, S. Electron transport to nitrogenase in Rhodospirillum rubrum: the role of NAD(P)H as electron donor and the effect of fluoroacetate on nitrogenase activity FEMS Microbiol. Lett. 1997, 150 (2) 263-7 (Pubitemid 27241560)
    • (1997) FEMS Microbiology Letters , vol.150 , Issue.2 , pp. 263-267
    • Brostedt, E.1    Lindblad, A.2    Jansson, J.3    Nordlund, S.4
  • 26
    • 0002503112 scopus 로고
    • Photometabolism of Rhodospirillum rubrum: Light-dependent dissimilation of organic compounds to carbon dioxide and molecular hydrogen by an anaerobic citric acid cycle
    • Gest, H.; Ormerod, J. G.; Ormerod, K. S. Photometabolism of Rhodospirillum rubrum: light-dependent dissimilation of organic compounds to carbon dioxide and molecular hydrogen by an anaerobic citric acid cycle Arch. Biochem. Biophys. 1962, 97 (1) 21-33
    • (1962) Arch. Biochem. Biophys. , vol.97 , Issue.1 , pp. 21-33
    • Gest, H.1    Ormerod, J.G.2    Ormerod, K.S.3
  • 27
    • 33947462871 scopus 로고
    • Simultaneous reduction of diphosphopyridine nucleotide and oxidation of reduced flavin mononucleotide by illuminated bacterial chromatophores
    • Frenkel, A. W. Simultaneous reduction of diphosphopyridine nucleotide and oxidation of reduced flavin mononucleotide by illuminated bacterial chromatophores J. Am. Chem. Soc. 1958, 80 (13) 3479-80
    • (1958) J. Am. Chem. Soc. , vol.80 , Issue.13 , pp. 3479-80
    • Frenkel, A.W.1
  • 29
    • 30744476222 scopus 로고    scopus 로고
    • Performance of a linear ion trap-orbitrap hybrid for peptide analysis
    • DOI 10.1021/ac0514624
    • Yates, J. R.; Cociorva, D.; Liao, L.; Zabrouskov, V. Performance of a linear ion trap-Orbitrap hybrid for peptide analysis Anal. Chem. 2006, 78 (2) 493-500 (Pubitemid 43100382)
    • (2006) Analytical Chemistry , vol.78 , Issue.2 , pp. 493-500
    • Yates, J.R.1    Cociorva, D.2    Liao, L.3    Zabrouskov, V.4
  • 30
    • 50549188450 scopus 로고
    • Light-dependent utilization of organic compounds and photoproduction of molecular hydrogen by photosynthetic bacteria; Relationships with nitrogen metabolism
    • Ormerod, J. G.; Ormerod, K. S.; Gest, H. Light-dependent utilization of organic compounds and photoproduction of molecular hydrogen by photosynthetic bacteria; relationships with nitrogen metabolism Arch. Biochem. Biophys. 1961, 94 (3) 449-63
    • (1961) Arch. Biochem. Biophys. , vol.94 , Issue.3 , pp. 449-63
    • Ormerod, J.G.1    Ormerod, K.S.2    Gest, H.3
  • 32
    • 0017071382 scopus 로고
    • Membranes of Rhodospirillum rubrum: Physicochemical properties of chromatophore fractions isolated from osmotically and mechanically disrupted cells
    • Collins, M. L.; Niederman, R. A. Membranes of Rhodospirillum rubrum: physicochemical properties of chromatophore fractions isolated from osmotically and mechanically disrupted cells J. Bacteriol. 1976, 126 (3) 1326-38
    • (1976) J. Bacteriol. , vol.126 , Issue.3 , pp. 1326-38
    • Collins, M.L.1    Niederman, R.A.2
  • 33
    • 0017671931 scopus 로고
    • Purification of protein a, an outer membrane component missing in Escherichia coli K 12 ompA mutants
    • Chai, T. J.; Foulds, J. Purification of protein A, an outer membrane component missing in Escherichia coli K-12 ompA mutants Biochim. Biophys. Acta 1977, 493 (1) 210-5 (Pubitemid 8179461)
    • (1977) Biochimica et Biophysica Acta , vol.493 , Issue.1 , pp. 210-215
    • Chai, T.1    Foulds, J.2
  • 34
    • 0025752365 scopus 로고
    • Proton-pumping N,N′-dicyclohexylcarbodiimide-sensitive inorganic pyrophosphate synthase from Rhodospirillum rubrum - Purification, characterization and reconstitution
    • Nyren, P.; Nore, B. F.; Strid, A. Proton-pumping N,N′- dicyclohexylcarbodiimide-sensitive inorganic pyrophosphate synthase from Rhodospirillum rubrum-purification, characterization and reconstitution Biochemistry 1991, 30 (11) 2883-7
    • (1991) Biochemistry , vol.30 , Issue.11 , pp. 2883-7
    • Nyren, P.1    Nore, B.F.2    Strid, A.3
  • 35
    • 78649693871 scopus 로고    scopus 로고
    • Maltose-neopentyl glycol (MNG) amphiphiles for solubilization, stabilization and crystallization of membrane proteins
    • Chae, et al., Maltose-neopentyl glycol (MNG) amphiphiles for solubilization, stabilization and crystallization of membrane proteins Nat. Methods 2010, 7, 1003-1008
    • (2010) Nat. Methods , vol.7 , pp. 1003-1008
    • Chae1
  • 36
    • 0026409298 scopus 로고
    • Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form
    • Schagger, H.; von Jagow, G. Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form Anal. Biochem. 1991, 199 (2) 223-31
    • (1991) Anal. Biochem. , vol.199 , Issue.2 , pp. 223-31
    • Schagger, H.1    Von Jagow, G.2
  • 37
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • DOI 10.1016/0003-2697(87)90587-2
    • Schagger, H.; von Jagow, G. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa Anal. Biochem. 1987, 166 (2) 368-79 (Pubitemid 18004907)
    • (1987) Analytical Biochemistry , vol.166 , Issue.2 , pp. 368-379
    • Schagger, H.1    Von Jagow, G.2
  • 39
    • 0015523228 scopus 로고
    • Mechanism of assembly of the outer membrane of Salmonella typhimurium. Isolation and characterization of cytoplasmic and outer membrane
    • Osborn, M. J.; Gander, J. E.; Parisi, E.; Carson, J. Mechanism of assembly of the outer membrane of Salmonella typhimurium. Isolation and characterization of cytoplasmic and outer membrane J. Biol. Chem. 1972, 247 (12) 3962-72
    • (1972) J. Biol. Chem. , vol.247 , Issue.12 , pp. 3962-72
    • Osborn, M.J.1    Gander, J.E.2    Parisi, E.3    Carson, J.4
  • 40
    • 0021989093 scopus 로고
    • Molecular basis of bacterial outer membrane permeability
    • Nikaido, H.; Vaara, M. Molecular basis of bacterial outer membrane permeability Microbiol. Rev. 1985, 49 (1) 1-32 (Pubitemid 15134118)
    • (1985) Microbiological Reviews , vol.49 , Issue.1 , pp. 1-32
    • Nikaido, H.1    Vaara, M.2
  • 41
    • 0017746644 scopus 로고
    • Defective growth functions in mutants of Escherichia coli K12 lacking a major outer membrane protein
    • Manning, P. A.; Pugsley, A. P.; Reeves, P. Defective growth functions in mutants of Escherichia coli K12 lacking a major outer membrane protein J. Mol. Biol. 1977, 116 (2) 285-300 (Pubitemid 8215108)
    • (1977) Journal of Molecular Biology , vol.116 , Issue.2 , pp. 285-300
    • Manning, P.A.1    Pugsley, A.P.2    Reeves, P.3
  • 42
    • 0347597840 scopus 로고    scopus 로고
    • Shotgun proteomic analysis of a chromatophore-enriched preparation from the purple phototrophic bacterium Rhodopseudomonas palustris
    • DOI 10.1023/B:PRES.0000006752.81486.74
    • Fejes, A. P.; Beatty, T. J. Shotgun proteomic analysis of a chromatophore-enriched preparation from the purple phototrophic bacterium Rhodopseudomonas palustris Photosynth. Res. 2003, 78, 195-203 (Pubitemid 38042911)
    • (2003) Photosynthesis Research , vol.78 , Issue.3 SPEC. ISSUE , pp. 195-203
    • Fejes, A.P.1    Yi, E.C.2    Goodlett, D.R.3    Beatty, J.T.4
  • 43
    • 0842307336 scopus 로고    scopus 로고
    • Towards Functional Proteomics of Membrane Protein Complexes in Synechocystis sp. 6803
    • Herranen, M., A., E-M Towards Functional Proteomics of Membrane Protein Complexes in Synechocystis sp. 6803 Plant Physiol. 2004, 134, 470-481
    • (2004) Plant Physiol. , vol.134 , pp. 470-481
    • Herranen, M..A..E.-M.1
  • 44
    • 73649097970 scopus 로고    scopus 로고
    • Oligomeric characterization of the photosynthetic apparatus of Rhodobacter sphaeroides R26.1 by nondenaturing electrophoresis methods
    • D'Amici, G. M.; Rinalducci, S.; Murgiano, L.; Italiano, F.; Zolla, L. Oligomeric characterization of the photosynthetic apparatus of Rhodobacter sphaeroides R26.1 by nondenaturing electrophoresis methods J. Proteome Res. 2010, 9 (1) 192-203
    • (2010) J. Proteome Res. , vol.9 , Issue.1 , pp. 192-203
    • D'Amici, G.M.1    Rinalducci, S.2    Murgiano, L.3    Italiano, F.4    Zolla, L.5
  • 45
    • 66049101792 scopus 로고    scopus 로고
    • Atomic force microscopy studies of native photosynthetic membranes
    • Sturgis, J. N.; Tucker, J. D.; Olsen, J. D.; Hunter, C. N.; Niederman, R. A. Atomic force microscopy studies of native photosynthetic membranes Biochemistry 2009, 48 (17) 3679-98
    • (2009) Biochemistry , vol.48 , Issue.17 , pp. 3679-98
    • Sturgis, J.N.1    Tucker, J.D.2    Olsen, J.D.3    Hunter, C.N.4    Niederman, R.A.5
  • 46
    • 46649110611 scopus 로고    scopus 로고
    • Three-dimensional reconstruction of a membrane-bending complex: The RC-LH1-PufX core dimer of Rhodobacter sphaeroides
    • Qian, P.; Bullough, P. A.; Hunter, C. N. Three-dimensional reconstruction of a membrane-bending complex: the RC-LH1-PufX core dimer of Rhodobacter sphaeroides J. Biol. Chem. 2008, 283 (20) 14002-11
    • (2008) J. Biol. Chem. , vol.283 , Issue.20 , pp. 14002-11
    • Qian, P.1    Bullough, P.A.2    Hunter, C.N.3
  • 47
    • 0023423225 scopus 로고
    • Molecular organization of photochemical reaction complex in chromatophore membrane from Rhodospirillum rubrum as detected by immunochemical and proteolytic analyses
    • Ueda, T.; Ideguchi, T.; Kaino, N.; Kakuno, T.; Yamashita, J.; Horio, T. Molecular organization of photochemical reaction complex in chromatophore membrane from Rhodospirillum rubrum as detected by immunochemical and proteolytic analyses J. Biochem. 1987, 102 (4) 755-65
    • (1987) J. Biochem. , vol.102 , Issue.4 , pp. 755-65
    • Ueda, T.1    Ideguchi, T.2    Kaino, N.3    Kakuno, T.4    Yamashita, J.5    Horio, T.6
  • 48
    • 0029866405 scopus 로고    scopus 로고
    • Comparison of the structural requirements for bacteriochlorophyll binding in the core light-harvesting complexes of Rhodospirillum rubrum and Rhodobacter sphaeroides using reconstitution methodology with bacteriochlorophyll analogs
    • Davis, C. M.; Parkes-Loach, P. S.; Cook, C. K.; Meadows, K. A.; Bandilla, M.; Scheer, H.; Loach, P. A. Comparison of the structural requirements for bacteriochlorophyll binding in the core light-harvesting complexes of Rhodospirillum rubrum and Rhodobacter sphaeroides using reconstitution methodology with bacteriochlorophyll analogs Biochemistry 1996, 35 (9) 3072-84
    • (1996) Biochemistry , vol.35 , Issue.9 , pp. 3072-84
    • Davis, C.M.1    Parkes-Loach, P.S.2    Cook, C.K.3    Meadows, K.A.4    Bandilla, M.5    Scheer, H.6    Loach, P.A.7
  • 49
    • 0347717833 scopus 로고    scopus 로고
    • Structural Analysis of the Reaction Center Light-harvesting Complex I Photosynthetic Core Complex of Rhodospirillum rubrum Using Atomic Force Microscopy
    • DOI 10.1074/jbc.M310382200
    • Fotiadis, D.; Qian, P.; Philippsen, A.; Bullough, P. A.; Engel, A.; Hunter, C. N. Structural analysis of the reaction center light-harvesting complex I photosynthetic core complex of Rhodospirillum rubrum using atomic force microscopy J. Biol. Chem. 2004, 279 (3) 2063-8 (Pubitemid 38084478)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.3 , pp. 2063-2068
    • Fotiadis, D.1    Qian, P.2    Philippsen, A.3    Bullough, P.A.4    Engel, A.5    Hunter, C.N.6
  • 50
    • 0028953308 scopus 로고
    • The 8.5 A projection map of the light-harvesting complex i from Rhodospirillum rubrum reveals a ring composed of 16 subunits
    • Karrasch, S.; Bullough, P. A.; Ghosh, R. The 8.5 A projection map of the light-harvesting complex I from Rhodospirillum rubrum reveals a ring composed of 16 subunits EMBO J. 1995, 14 (4) 631-8
    • (1995) EMBO J. , vol.14 , Issue.4 , pp. 631-8
    • Karrasch, S.1    Bullough, P.A.2    Ghosh, R.3
  • 51
    • 0032483080 scopus 로고    scopus 로고
    • Isolation of the PufX protein from Rhodobacter capsulatus and Rhodobacter sphaeroides: Evidence for its interaction with the α- polypeptide of the core light-harvesting complex
    • DOI 10.1021/bi980657l, PII S0006296098006576
    • Recchia, P. A.; Davis, C. M.; Lilburn, T. G.; Beatty, J. T.; Parkes-Loach, P. S.; Hunter, C. N.; Loach, P. A. Isolation of the PufX protein from Rhodobacter capsulatus and Rhodobacter sphaeroides: evidence for its interaction with the alpha-polypeptide of the core light-harvesting complex Biochemistry 1998, 37 (31) 11055-63 (Pubitemid 28368932)
    • (1998) Biochemistry , vol.37 , Issue.31 , pp. 11055-11063
    • Recchia, P.A.1    Davis, C.M.2    Lilburn, T.G.3    Beatty, J.T.4    Parkes-Loach, P.S.5    Hunter, C.N.6    Loach, P.A.7
  • 52
    • 0028863491 scopus 로고
    • Role of the PufX protein in photosynthetic growth of Rhodobacter sphaeroides. 2. PufX is required for efficient ubiquinone/ubiquinol exchange between the reaction center QB site and the cytochrome bc1 complex
    • Barz, W. P.; Vermeglio, A.; Francia, F.; Venturoli, G.; Melandri, B. A.; Oesterhelt, D. Role of the PufX protein in photosynthetic growth of Rhodobacter sphaeroides. 2. PufX is required for efficient ubiquinone/ubiquinol exchange between the reaction center QB site and the cytochrome bc1 complex Biochemistry 1995, 34 (46) 15248-58
    • (1995) Biochemistry , vol.34 , Issue.46 , pp. 15248-58
    • Barz, W.P.1    Vermeglio, A.2    Francia, F.3    Venturoli, G.4    Melandri, B.A.5    Oesterhelt, D.6
  • 53
    • 15744405284 scopus 로고    scopus 로고
    • - membranes
    • DOI 10.1074/jbc.M412089200
    • Comayras, F.; Jungas, C.; Lavergne, J. Functional consequences of the organization of the photosynthetic apparatus in Rhodobacter sphaeroides: II. A study of PufX- membranes J. Biol. Chem. 2005, 280 (12) 11214-23 (Pubitemid 40418428)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.12 , pp. 11214-11223
    • Comayras, F.1    Jungas, C.2    Lavergne, J.3
  • 54
    • 14644440750 scopus 로고    scopus 로고
    • Solution structures of the core light-harvesting α and β polypeptides from rhodospirillum rubrum: Implications for the pigment-protein and protein-protein interactions
    • DOI 10.1016/j.jmb.2005.01.017
    • Wang, Z. Y.; Gokan, K.; Kobayashi, M.; Nozawa, T. Solution structures of the core light-harvesting alpha and beta polypeptides from Rhodospirillum rubrum: implications for the pigment-protein and protein-protein interactions J. Mol. Biol. 2005, 347 (2) 465-77 (Pubitemid 40312471)
    • (2005) Journal of Molecular Biology , vol.347 , Issue.2 , pp. 465-477
    • Wang, Z.-Y.1    Gokan, K.2    Kobayashi, M.3    Nozawa, T.4
  • 55
    • 0034532649 scopus 로고    scopus 로고
    • ATP synthases in the year 2000: Evolving views about the structures of these remarkable enzyme complexes
    • DOI 10.1023/A:1005594800983
    • Pedersen, P. L.; Ko, Y. H.; Hong, S. ATP synthases in the year 2000: evolving views about the structures of these remarkable enzyme complexes J. Bioenerg. Biomembr. 2000, 32 (4) 325-32 (Pubitemid 32001395)
    • (2000) Journal of Bioenergetics and Biomembranes , vol.32 , Issue.4 , pp. 325-332
    • Pedersen, P.L.1    Ko, Y.H.2    Hong, S.3
  • 56
    • 0035830452 scopus 로고    scopus 로고
    • Specific heterodimer formation by the cytoplasmic domains of the b and b′ subunits of cyanobacterial ATP synthase
    • DOI 10.1021/bi001821j
    • Dunn, S. D.; Kellner, E.; Lill, H. Specific heterodimer formation by the cytoplasmic domains of the b and b′ subunits of cyanobacterial ATP synthase Biochemistry 2001, 40 (1) 187-92 (Pubitemid 32052691)
    • (2001) Biochemistry , vol.40 , Issue.1 , pp. 187-192
    • Dunn, S.D.1    Kellner, E.2    Lill, H.3
  • 57
    • 34248676587 scopus 로고    scopus 로고
    • Biophysics and bioinformatics reveal structural differences of the two peripheral stalk subunits in chloroplast ATP synthase
    • DOI 10.1093/jb/mvm045
    • Poetsch, A.; Berzborn, R. J.; Heberle, J.; Link, T. A.; Dencher, N. A.; Seelert, H. Biophysics and bioinformatics reveal structural differences of the two peripheral stalk subunits in chloroplast ATP synthase J. Biochem. 2007, 141 (3) 411-20 (Pubitemid 46770393)
    • (2007) Journal of Biochemistry , vol.141 , Issue.3 , pp. 411-420
    • Poetsch, A.1    Berzborn, R.J.2    Heberle, J.3    Link, T.A.4    Dencher, N.A.5    Seelert, H.6
  • 58
    • 0024288490 scopus 로고
    • DNA sequence of a gene cluster coding for subunits of the F0 membrane sector of ATP synthase in Rhodospirillum rubrum. Support for modular evolution of the F1 and F0 sectors
    • Falk, G.; Walker, J. E. DNA sequence of a gene cluster coding for subunits of the F0 membrane sector of ATP synthase in Rhodospirillum rubrum. Support for modular evolution of the F1 and F0 sectors Biochem. J. 1988, 254 (1) 109-22
    • (1988) Biochem. J. , vol.254 , Issue.1 , pp. 109-22
    • Falk, G.1    Walker, J.E.2
  • 59
    • 0027104114 scopus 로고
    • The NADH: Ubiquinone oxidoreductase (complex I) of respiratory chains
    • Walker, J. E. The NADH:ubiquinone oxidoreductase (complex I) of respiratory chains Q. Rev. Biophys. 1992, 25 (3) 253-324 (Pubitemid 23014370)
    • (1992) Quarterly Reviews of Biophysics , vol.25 , Issue.3 , pp. 253-324
    • Walker, J.E.1
  • 60
    • 0038482064 scopus 로고    scopus 로고
    • A role for native lipids in the stabilization and two-dimensional crystallization of the Escherichia coli NADH-ubiquinone oxidoreductase (complex I)
    • DOI 10.1074/jbc.M208959200
    • Sazanov, L. A.; Carroll, J.; Holt, P.; Toime, L.; Fearnley, I. M. A role for native lipids in the stabilization and two-dimensional crystallization of the Escherichia coli NADH-ubiquinone oxidoreductase (complex I) J. Biol. Chem. 2003, 278 (21) 19483-91 (Pubitemid 36799345)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.21 , pp. 19483-19491
    • Sazanov, L.A.1    Carroll, J.2    Holt, P.3    Toime, L.4    Fearnley, I.M.5
  • 64
    • 27944489552 scopus 로고    scopus 로고
    • Reversible membrane association of dinitrogenase reductase activating glycohydrolase in the regulation of nitrogenase activity in Rhodospirillum rubrum; Dependence on GlnJ and AmtB1
    • DOI 10.1016/j.femsle.2005.09.049, PII S0378109705006841
    • Wang, H.; Franke, C. C.; Nordlund, S.; Noren, A. Reversible membrane association of dinitrogenase reductase activating glycohydrolase in the regulation of nitrogenase activity in Rhodospirillum rubrum; dependence on GlnJ and AmtB1 FEMS Microbiol. Lett. 2005, 253 (2) 273-9 (Pubitemid 41674526)
    • (2005) FEMS Microbiology Letters , vol.253 , Issue.2 , pp. 273-279
    • Wang, H.1    Franke, C.C.2    Nordlund, S.3    Noren, A.4
  • 65
    • 47249127306 scopus 로고    scopus 로고
    • Redox-state dynamics of ubiquinone-10 imply cooperative regulation of photosynthetic membrane expression in Rhodospirillum rubrum
    • DOI 10.1128/JB.00423-08
    • Grammel, H.; Ghosh, R. Redox-state dynamics of ubiquinone-10 imply cooperative regulation of photosynthetic membrane expression in Rhodospirillum rubrum J. Bacteriol. 2008, 190 (14) 4912-21 (Pubitemid 351991059)
    • (2008) Journal of Bacteriology , vol.190 , Issue.14 , pp. 4912-4921
    • Grammel, H.1    Ghosh, R.2
  • 66
    • 0024586535 scopus 로고
    • Supramolecular organization of tricarboxylic acid cycle enzymes
    • DOI 10.1016/0303-2647(89)90038-5
    • Lyubarev, A. E.; Kurganov, B. I. Supramolecular organization of tricarboxylic acid cycle enzymes Biosystems 1989, 22 (2) 91-102 (Pubitemid 19053323)
    • (1989) BioSystems , vol.22 , Issue.2 , pp. 91-102
    • Lyubarev, A.E.1    Kurganov, B.I.2
  • 68
    • 0014076120 scopus 로고
    • Photosynthesis in Rhodospirillum rubrum. 3. Metabolic control of reductive pentose phosphate and tricarboxylic acid cycle enzymes
    • Anderson, L.; Fuller, R. C. Photosynthesis in Rhodospirillum rubrum. 3. Metabolic control of reductive pentose phosphate and tricarboxylic acid cycle enzymes Plant Physiol. 1967, 42 (4) 497-509
    • (1967) Plant Physiol. , vol.42 , Issue.4 , pp. 497-509
    • Anderson, L.1    Fuller, R.C.2
  • 69
    • 34047164005 scopus 로고    scopus 로고
    • Crystal structures of an extracytoplasmic solute receptor from a TRAP transporter in its open and closed forms reveal a helix-swapped dimer requiring a cation for alpha-keto acid binding
    • Gonin, S.; Arnoux, P.; Pierru, B.; Lavergne, J.; Alonso, B.; Sabaty, M.; Pignol, D. Crystal structures of an extracytoplasmic solute receptor from a TRAP transporter in its open and closed forms reveal a helix-swapped dimer requiring a cation for alpha-keto acid binding BMC Struct. Biol. 2007, 7, 11
    • (2007) BMC Struct. Biol. , vol.7 , pp. 11
    • Gonin, S.1    Arnoux, P.2    Pierru, B.3    Lavergne, J.4    Alonso, B.5    Sabaty, M.6    Pignol, D.7
  • 70
    • 0028929883 scopus 로고
    • Regulation of succinate dehydrogenase (sdhCDAB) operon expression in Escherichia coli in response to carbon supply and anaerobiosis: Role of ArcA and Fnr
    • Park, S. J.; Tseng, C. P.; Gunsalus, R. P. Regulation of succinate dehydrogenase (sdhCDAB) operon expression in Escherichia coli in response to carbon supply and anaerobiosis: role of ArcA and Fnr Mol. Microbiol. 1995, 15 (3) 473-82
    • (1995) Mol. Microbiol. , vol.15 , Issue.3 , pp. 473-82
    • Park, S.J.1    Tseng, C.P.2    Gunsalus, R.P.3
  • 71
    • 0015373383 scopus 로고
    • The photoreduction of nicotinamide-adenine dinucleotide by chromatophore fractions from Rhodospirillum rubrum
    • Govindjee, R.; Sybesma, C. The photoreduction of nicotinamide-adenine dinucleotide by chromatophore fractions from Rhodospirillum rubrum Biophys. J. 1972, 12 (7) 897-908
    • (1972) Biophys. J. , vol.12 , Issue.7 , pp. 897-908
    • Govindjee, R.1    Sybesma, C.2
  • 72
    • 0242405762 scopus 로고    scopus 로고
    • Microaerophilic Cooperation of Reductive and Oxidative Pathways Allows Maximal Photosynthetic Membrane Biosynthesis in Rhodospirillum rubrum
    • DOI 10.1128/AEM.69.11.6577-6586.2003
    • Grammel, H.; Gilles, E. D.; Ghosh, R. Microaerophilic cooperation of reductive and oxidative pathways allows maximal photosynthetic membrane biosynthesis in Rhodospirillum rubrum Appl. Environ. Microbiol. 2003, 69 (11) 6577-86 (Pubitemid 37420193)
    • (2003) Applied and Environmental Microbiology , vol.69 , Issue.11 , pp. 6577-6586
    • Grammel, H.1    Gilles, E.-D.2    Ghosh, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.