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Volumn 48, Issue 17, 2009, Pages 3679-3698

Atomic force microscopy studies of native photosynthetic membranes

Author keywords

[No Author keywords available]

Indexed keywords

AFM; AFM IMAGE; ATOMIC-RESOLUTION; ATP SYNTHASE; BACTERIOCHLOROPHYLL; CORE COMPLEX; CYTOPLASMIC MEMBRANE; GREEN PLANTS; IN-SITU; INTERCONNECTED NETWORK; LH2 COMPLEXES; LIGHT-HARVESTING; OXYGEN-EVOLVING COMPLEXES; PURPLE BACTERIA; RADIANT ENERGY; REACTION CENTER; RHODOBACTER SPHAEROIDES; RHODOPSEUDOMONAS PALUSTRIS; SPHAEROIDES; STRUCTURAL MODELS; SUB-MOLECULAR RESOLUTION; SURFACE IMAGE; THYLAKOIDS;

EID: 66049101792     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi900045x     Document Type: Review
Times cited : (86)

References (106)
  • 1
    • 20444382012 scopus 로고    scopus 로고
    • Watching the components of photosynthetic bacterial membranes and their in situ organisation by atomic force microscopy
    • DOI 10.1016/j.bbamem.2005.04.005, PII S0005273605001033
    • Scheuring, S., Levy, D., and Rigaud, J. L. (2005) Watching the components of photosynthetic bacterial membranes and their in situ organisation by atomic force microscopy. Biochim. Biophys. Acta 1712, 109-127. (Pubitemid 40799298)
    • (2005) Biochimica et Biophysica Acta - Biomembranes , vol.1712 , Issue.2 , pp. 109-127
    • Scheuring, S.1    Levy, D.2    Rigaud, J.-L.3
  • 2
    • 37749035035 scopus 로고    scopus 로고
    • Atomic force microscopy reveals multiple patterns of antenna organization in purple bacteria: Implications for energy transduction mechanisms and membrane modeling
    • Sturgis, J. N., and Niederman, R. A. (2008) Atomic force microscopy reveals multiple patterns of antenna organization in purple bacteria: Implications for energy transduction mechanisms and membrane modeling. Photosynth. Res. 95, 269-278.
    • (2008) Photosynth. Res. , vol.95 , pp. 269-278
    • Sturgis, J.N.1    Niederman, R.A.2
  • 3
    • 66049095346 scopus 로고    scopus 로고
    • Organization and Assembly of Light-Harvesting Complexes in the Purple Bacterial Membrane
    • (Hunter, C. N., Daldal, F., Thurnauer, M. C., and Beatty, J. T., Eds.) Springer, Dordrecht, The Netherlands
    • Sturgis, J. N., and Niederman, R. A. (2008) Organization and Assembly of Light-Harvesting Complexes in the Purple Bacterial Membrane. In The Purple Phototrophic Bacteria. Advances in Photosynthesis and Respiration (Hunter, C. N., Daldal, F., Thurnauer, M. C., and Beatty, J. T., Eds.) Vol.28, pp 253-273, Springer, Dordrecht, The Netherlands.
    • (2008) The Purple Phototrophic Bacteria. Advances in Photosynthesis and Respiration , vol.28 , pp. 253-273
    • Sturgis, J.N.1    Niederman, R.A.2
  • 4
    • 84912130176 scopus 로고    scopus 로고
    • The Supramolecular Assembly of the Photosynthetic Apparatus of Purple Bacteria Investigated by High-Resolution Atomic Force Microscopy
    • (Hunter, C. N., Daldal, F., Thurnauer, M. C., and Beatty, J. T., Eds.) Springer, Dordrecht, The Netherlands
    • Scheuring, S. (2008) The Supramolecular Assembly of the Photosynthetic Apparatus of Purple Bacteria Investigated by High-Resolution Atomic Force Microscopy. In The Purple Phototrophic Bacteria. Advances in Photosynthesis and Respiration (Hunter, C. N., Daldal, F., Thurnauer, M. C., and Beatty, J. T., Eds.) Vol.28, pp 941-952, Springer, Dordrecht, The Netherlands.
    • (2008) The Purple Phototrophic Bacteria. Advances in Photosynthesis and Respiration , vol.28 , pp. 941-952
    • Scheuring, S.1
  • 6
    • 0000132996 scopus 로고
    • The structure of the photoreceptor unit of Rhodopseudomonas viridis
    • Stark, W., Kühlbrandt, W., Wildhaber, I., Wehrli, E., and Mühlethaler, K. (1984) The structure of the photoreceptor unit of Rhodopseudomonas viridis. EMBO J. 3, 777-783.
    • (1984) EMBO J. , vol.3 , pp. 777-783
    • Stark, W.1    Kühlbrandt, W.2    Wildhaber, I.3    Wehrli, E.4    Mühlethaler, K.5
  • 7
    • 0020376605 scopus 로고
    • Formation, structure and composition of a planar hexagonal lattice composed of specific protein-lipid complexes in the thylakoid membranes of Rhodopseudomonas viridis
    • Welte, W., and Kreutz, W. (1982) Formation, structure and composition of a planar hexagonal lattice composed of specific proteinlipid complexes in the thylakoid membranes of Rhodopseudomonas viridis. Biochim. Biophys. Acta 692, 479-488. (Pubitemid 13166367)
    • (1982) Biochimica et Biophysica Acta , vol.692 , Issue.3 , pp. 479-488
    • Welte, W.1    Kreutz, W.2
  • 8
    • 0001289077 scopus 로고
    • The organisation of the photosynthetic apparatus of Rhodobacter sphaeroides: Studies of antenna mutants using singlet-singlet quenching
    • Vos, M., van Dorssen, R. J., Amesz, J., van Grondelle, R., and Hunter, C. N. (1988) The organisation of the photosynthetic apparatus of Rhodobacter sphaeroides: Studies of antenna mutants using singlet-singlet quenching. Biochim. Biophys. Acta 933, 132-140.
    • (1988) Biochim. Biophys. Acta , vol.933 , pp. 132-140
    • Vos, M.1    Van Dorssen, R.J.2    Amesz, J.3    Van Grondelle, R.4    Hunter, C.N.5
  • 9
    • 0022448709 scopus 로고
    • Singlet-singlet annihilation at low temperatures in the antenna of purple bacteria
    • DOI 10.1016/0005-2728(86)90119-2
    • Vos, M., van Grondelle, R., van der Kooij, F. W., van de Poll, D., Amesz, J., and Duysens, L. M. N. (1986) Singlet-singlet annihilation at low temperatures in the antenna of purple bacteria. Biochim. Biophys. Acta 850, 501-512. (Pubitemid 16077552)
    • (1986) Biochimica et Biophysica Acta - Bioenergetics , vol.850 , Issue.3 , pp. 501-512
    • Vos, M.1    Van Grondelle, R.2    Van Der Kooij, F.W.3
  • 10
    • 0032494284 scopus 로고    scopus 로고
    • Altered organization of light-harvesting complexes in phospholipid-enriched Rhodobacter sphaeroides chromatophores as determined by fluorescence yield and singlet-singlet annihilation measurements
    • DOI 10.1016/S0005-2728(98)00132-7, PII S0005272898001327
    • Westerhuis, W. H. J., Vos, M., van Grondelle, R., Amesz, J., and Niederman, R. A. (1998) Altered organization of light-harvesting complexes in phospholipid-enriched Rhodobacter sphaeroides chromatophores as determined by fluorescence yield and singlet-singlet annihilation measurements. Biochim. Biophys. Acta 1366, 317-329. (Pubitemid 29164405)
    • (1998) Biochimica et Biophysica Acta - Bioenergetics , vol.1366 , Issue.3 , pp. 317-329
    • Westerhuis, W.H.J.1    Vos, M.2    Van Grondelle, R.3    Amesz, J.4    Niederman, R.A.5
  • 11
    • 0043095535 scopus 로고    scopus 로고
    • Lipidic cubic phase crystal structure of the photosynthetic reaction centre from Rhodobacter sphaeroides at 2.35 Å resolution
    • DOI 10.1016/S0022-2836(03)00751-4
    • Katona, G., Andreasson, U., Landau, E. M., Andreasson, L. E., and Neutze, R. (2003) Lipidic cubic phase crystal structure of the photosynthetic reaction centre from Rhodobacter sphaeroides at 2.35 Å resolution. J. Mol. Biol. 331, 681-692. (Pubitemid 36937154)
    • (2003) Journal of Molecular Biology , vol.331 , Issue.3 , pp. 681-692
    • Katona, G.1    Andreasson, U.2    Landau, E.M.3    Andreasson, L.-E.4    Neutze, R.5
  • 13
    • 0030585121 scopus 로고    scopus 로고
    • The crystal structure of the light-harvesting complex II (B800-850) from Rhodospirillum molischianum
    • Koepke, J., Hu, X. C., Muenke, C., Schulten, K., and Michel, H. (1996) The crystal structure of the light-harvesting complex II (B800-850) from Rhodospirillum molischianum. Structure 4, 581-597. (Pubitemid 126657551)
    • (1996) Structure , vol.4 , Issue.5 , pp. 581-597
    • Koepke, J.1    Hu, X.2    Muenke, C.3    Schulten, K.4    Michel, H.5
  • 14
    • 34447638509 scopus 로고    scopus 로고
    • From high-resolution AFM topographs to atomic models of supramolecular assemblies
    • DOI 10.1016/j.jsb.2007.01.021, PII S1047847707000251
    • Scheuring, S., Boudier, T., and Sturgis, J. N. (2007) From high-resolution AFM topographs to atomic models of supramolecular assemblies. J. Struct. Biol. 159, 268-276. (Pubitemid 47095394)
    • (2007) Journal of Structural Biology , vol.159 , Issue.2 SPEC. ISS , pp. 268-276
    • Scheuring, S.1    Boudier, T.2    Sturgis, J.N.3
  • 15
    • 28944431668 scopus 로고    scopus 로고
    • Architecture of the native photosynthetic apparatus of Phaeospirillum molischianum
    • DOI 10.1016/j.jsb.2005.10.002, PII S1047847705002261
    • Gonçalves, R. P., Bernadac, A., Sturgis, J. N., and Scheuring, S. (2005) Architecture of the native photosynthetic apparatus of Phaeospirillum molischianum. J. Struct. Biol. 152, 221-228. (Pubitemid 41785519)
    • (2005) Journal of Structural Biology , vol.152 , Issue.3 , pp. 221-228
    • Goncalves, R.P.1    Bernadac, A.2    Sturgis, J.N.3    Scheuring, S.4
  • 21
    • 59649125384 scopus 로고    scopus 로고
    • From Atomic-Level Structure to Supramolecular Organization in the Photosynthetic Unit of Purple Bacteria
    • (Hunter, C. N., Daldal, F., Thurnauer, M. C., and Beatty, J. T., Eds.) Springer, Dordrecht, The Netherlands
    • Sener, M. K., and Schulten, K. (2008) From Atomic-Level Structure to Supramolecular Organization in the Photosynthetic Unit of Purple Bacteria. In The Purple Phototrophic Bactria. Advances in Photosynthesis and Respiration (Hunter, C. N., Daldal, F., Thurnauer, M. C., and Beatty, J. T., Eds.) Vol.28, pp 275-294, Springer, Dordrecht, The Netherlands.
    • (2008) The Purple Phototrophic Bactria. Advances in Photosynthesis and Respiration , vol.28 , pp. 275-294
    • Sener, M.K.1    Schulten, K.2
  • 22
    • 57649171108 scopus 로고    scopus 로고
    • The organization of LH2 complexes in membranes from Rhodobacter spaheroides
    • Olsen, J. D., Tucker, J. D., Timney, J. A., Qian, P., Vassilev, C., and Hunter, C. N. (2008) The organization of LH2 complexes in membranes from Rhodobacter spaheroides. J. Biol. Chem. 283, 30772-30779.
    • (2008) J. Biol. Chem. , vol.283 , pp. 30772-30779
    • Olsen, J.D.1    Tucker, J.D.2    Timney, J.A.3    Qian, P.4    Vassilev, C.5    Hunter, C.N.6
  • 23
    • 0024433591 scopus 로고
    • The photosynthetic reaction center from this purple bacterium Rhodopseudomonas viridis
    • Deisenhofer, J., and Michel, H. (1989) The photosynthetic reaction center from the purple bacterium Rhodopseudomonas vridis. Science 245, 1463-1473. (Pubitemid 19243235)
    • (1989) Science , vol.245 , Issue.4925 , pp. 1463-1473
    • Deisenhofer, J.1    Michel, H.2
  • 24
    • 0023408258 scopus 로고
    • Structure of the reaction center from Rhodobacter sphaeroides R26: The protein subunits
    • Allen, J. P., Feher, G., Yeates, T. O., Komiya, H., and Rees, D. C. (1987) Structure of the reaction center from Rhodobacter sphaeroides R26: The protein subunits. Proc. Natl. Acad. Sci. U.S.A. 84, 6162-6166.
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 6162-6166
    • Allen, J.P.1    Feher, G.2    Yeates, T.O.3    Komiya, H.4    Rees, D.C.5
  • 25
    • 0346874216 scopus 로고    scopus 로고
    • Crystal Structure of the RC-LH1 Core Complex from Rhodopseudomonas palustris
    • DOI 10.1126/science.1088892
    • Roszak, A. W., Howard, T. D., Southall, J., Gardiner, A. T., Law, C. J., Isaacs, N. W., and Cogdell, R. J. (2003) Crystal structure of the RC-LH1 core complex from Rhodopseudomonas palustris. Science 302, 1969-1972. (Pubitemid 37523505)
    • (2003) Science , vol.302 , Issue.5652 , pp. 1969-1972
    • Roszak, A.W.1    Howard, T.D.2    Southall, J.3    Gardiner, A.T.4    Law, C.J.5    Isaacs, N.W.6    Cogdell, R.J.7
  • 26
    • 0035876215 scopus 로고    scopus 로고
    • High-resolution AFM topographs of Rubrivivax gelatinosus light-harvesting complex LH2
    • DOI 10.1093/emboj/20.12.3029
    • Scheuring, S., Reiss-Husson, F., Engel, A., Rigaud, J. L., and Ranck, J. L. (2001) High-resolution AFM topographs of Rubrivivax gelatinosus light-harvesting complex LH2. EMBO J. 20, 3029-3035. (Pubitemid 32611990)
    • (2001) EMBO Journal , vol.20 , Issue.12 , pp. 3029-3035
    • Scheuring, S.1    Reiss-Husson, F.2    Engel, A.3    Rigaud, J.-L.4    Ranck, J.-L.5
  • 27
    • 0037227427 scopus 로고    scopus 로고
    • AFM characterization of tilt and intrinsic flexibility of Rhodobacter sphaeroides light harvesting complex 2 (LH2)
    • DOI 10.1016/S0022-2836(02)01241-X
    • Scheuring, S., Seguin, J., Marco, S., Levy, D., Breyton, C., Robert, B., and Rigaud, J. L. (2003) AFM characterization of tilt and intrinsic flexibility of Rhodobacter sphaeroides light harvesting complex 2 (LH2). J. Mol. Biol. 325, 569-580. (Pubitemid 36062683)
    • (2003) Journal of Molecular Biology , vol.325 , Issue.3 , pp. 569-580
    • Scheuring, S.1    Seguin, J.2    Marco, S.3    Levy, D.4    Breyton, C.5    Robert, B.6    Rigaud, J.-L.7
  • 28
    • 2442667942 scopus 로고    scopus 로고
    • Flexibility and size heterogeneity of the LH1 light harvesting complex revealed by atomic force microscopy: Functional significance for bacterial photosynthesis
    • DOI 10.1074/jbc.M313039200
    • Bahatyrova, S., Frese, R. N., van der Werf, K. O., Otto, C., Hunter, C. N., and Olsen, J. D. (2004) Flexibility and size heterogeneity of the LH1 light harvesting complex revealed by atomic force microscopy: Functional significance for bacterial photosynthesis. J. Biol. Chem. 279, 21327-21333. (Pubitemid 38656540)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.20 , pp. 21327-21333
    • Bahatyrova, S.1    Frese, R.N.2    Van Der Werf, K.O.3    Otto, C.4    Hunter, C.N.5    Olsen, J.D.6
  • 29
    • 11144246948 scopus 로고    scopus 로고
    • Membrane insertion of Rhodopseudomonas acidophila light harvesting complex 2 investigated by high resolution AFM
    • DOI 10.1016/j.jsb.2004.09.001, PII S1047847704001728
    • Gonçalves, R. P., Busselez, J., Lévy, D., Seguin, J., and Scheuring, S. (2005) Membrane insertion of Rhodopseudomonas acidophila light harvesting complex 2 investigated by high resolution AFM. J. Struct. Biol. 149, 79-86. (Pubitemid 40051402)
    • (2005) Journal of Structural Biology , vol.149 , Issue.1 , pp. 79-86
    • Goncalves, R.P.1    Busselez, J.2    Levy, D.3    Seguin, J.4    Scheuring, S.5
  • 30
    • 0037379701 scopus 로고    scopus 로고
    • The ring structure and organization of light harvesting 2 complexes in a reconstituted lipid bilayer, resolved by atomic force microscopy
    • Stamouli, A., Kafi, S., Klein, D. C. G., Oosterkamp, T. H., Frenken, J. W. M., Cogdell, R. J., and Aartsma, T. J. (2003) The ring structure and organization of light harvesting 2 complexes in a reconstituted lipid bilayer, resolved by atomic force microscopy. Biophys. J. 84, 2483-2491. (Pubitemid 36373570)
    • (2003) Biophysical Journal , vol.84 , Issue.4 , pp. 2483-2491
    • Stamouli, A.1    Kafi, S.2    Klein, D.C.G.3    Oosterkamp, T.H.4    Frenken, J.W.M.5    Cogdell, R.J.6    Aartsma, T.J.7
  • 31
    • 44349116040 scopus 로고    scopus 로고
    • Dimers of light-harvesting complex 2 from Rhodobacter sphaeroides characterized in reconstituted 2D crystals with atomic force microscopy
    • Liu, L. N., Aartsma, T. J., and Frese, R. N. (2008) Dimers of light-harvesting complex 2 from Rhodobacter sphaeroides characterized in reconstituted 2D crystals with atomic force microscopy. FEBS J. 275, 3157-3166.
    • (2008) FEBS J. , vol.275 , pp. 3157-3166
    • Liu, L.N.1    Aartsma, T.J.2    Frese, R.N.3
  • 32
    • 1842510034 scopus 로고    scopus 로고
    • Molecular architecture of photosynthetic membranes in Rhodobacter sphaeroides: The role of PufX
    • DOI 10.1038/sj.emboj.7600092
    • Siebert, C. A., Qian, P., Fotiadis, D., Engel, A., Hunter, C. N., and Bullough, P. A. (2004) Molecular architecture of photosynthetic membranes in Rhodobacter sphaeroides: The role of PufX. EMBO J. 23, 690-700. (Pubitemid 38418737)
    • (2004) EMBO Journal , vol.23 , Issue.4 , pp. 690-700
    • Siebert, C.A.1    Qian, P.2    Fotiadis, D.3    Engel, A.4    Hunter, C.N.5    Bullough, P.A.6
  • 33
    • 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., and Hunter, C. N. (2004) Structural analysis of the reaction center light-harvesting complex I photosynthetic core complex of Rhodospirillum rubrum using atomic force microscopy. J. Biol. Chem. 279, 2063-2068. (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
  • 34
    • 12544254339 scopus 로고    scopus 로고
    • Structure of the dimeric PufX-containing core complex of Rhodobacter blasticus by in situ atomic force microscopy
    • Scheuring, S., Busselez, J., and Lévy, D. (2005) Structure of the dimeric PufX-containing core complex of Rhodobacter blasticus by in situ atomic force microscopy. J. Biol. Chem. 280, 1426-1431.
    • (2005) J. Biol. Chem. , vol.280 , pp. 1426-1431
    • Scheuring, S.1    Busselez, J.2    Lévy, D.3
  • 37
    • 33645100807 scopus 로고    scopus 로고
    • The photosynthetic apparatus of Rhodopseudomonas palustris: Structures and organization
    • Scheuring, S., Goncalves, R. P., Prima, V., and Sturgis, J. N. (2006) The photosynthetic apparatus of Rhodopseudomonas palustris: Structures and organization. J. Mol. Biol. 358, 83-96.
    • (2006) J. Mol. Biol. , vol.358 , pp. 83-96
    • Scheuring, S.1    Goncalves, R.P.2    Prima, V.3    Sturgis, J.N.4
  • 38
    • 0020530933 scopus 로고
    • Spatial differentiation in photosynthetic and non-photosynthetic membranes of Rhodopseudomonas palustris
    • Varga, A. R., and Staehelin, L. A. (1983) Spatial differentiation in photosynthetic and non-photosynthetic membranes of Rhodopseudomonas palustris. J. Bacteriol. 154, 1414-1430.
    • (1983) J. Bacteriol. , vol.154 , pp. 1414-1430
    • Varga, A.R.1    Staehelin, L.A.2
  • 39
    • 22344456559 scopus 로고    scopus 로고
    • Chromatic adaptation of photosynthetic membranes
    • Scheuring, S., and Sturgis, J. N. (2005) Chromatic adaptation of photosynthetic membranes. Science 309, 484-487.
    • (2005) Science , vol.309 , pp. 484-487
    • Scheuring, S.1    Sturgis, J.N.2
  • 40
    • 0042877260 scopus 로고    scopus 로고
    • Characterization of expressed pigmented core light harvesting complex (LH 1) in a reaction center deficient mutant of Blastochloris viridis
    • DOI 10.1023/A:1024921115267
    • Ostafin, A. E., Ponomarenko, N. S., Popova, J. A., Jäger, M., Bylina, E. J., and Norris, J. R. (2003) Characterization of expressed pigmented core light-harvesting complex (LH 1) in a reaction center deficient mutant of Blastochloris viridis. Photosynth. Res. 77, 53-68. (Pubitemid 37078108)
    • (2003) Photosynthesis Research , vol.77 , Issue.1 , pp. 53-68
    • Ostafin, A.E.1    Ponomarenko, N.S.2    Popova, J.A.3    Jager, M.4    Bylina, E.J.5    Norris Jr., J.R.6
  • 41
    • 0032478682 scopus 로고    scopus 로고
    • Projection map of the reaction center-light harvesting 1 complex from Rhodopseudomonas viridis at 10 Å resolution
    • DOI 10.1016/S0014-5793(98)00300-7, PII S0014579398003007
    • Ikeda-Yamasaki, I., Odahara, T., Mitsuoka, K., Fujiyoshi, Y., and Murata, K. (1998) Projection map of the reaction center-light harvesting 1 complex from Rhodopseudomonas viridis at 10 Å resolution. FEBS Lett. 425, 505-508. (Pubitemid 28178860)
    • (1998) FEBS Letters , vol.425 , Issue.3 , pp. 505-508
    • Ikeda-Yamasaki, I.1    Odahara, T.2    Mitsuoka, K.3    Fujiyoshi, Y.4    Murata, K.5
  • 42
    • 29144509559 scopus 로고    scopus 로고
    • The assembly and organisation of photosynthetic membranes in Rhodobacter sphaeroides
    • DOI 10.1039/b506099k
    • Hunter, C. N., Tucker, J. D., and Niederman, R. A. (2005) The assembly and organisation of photosynthetic membranes in Rhodobacter sphaeroides. Photochem. Photobiol. Sci. 4, 1023-1027. (Pubitemid 41811366)
    • (2005) Photochemical and Photobiological Sciences , vol.4 , Issue.12 , pp. 1023-1027
    • Hunter, C.N.1    Tucker, J.D.2    Niederman, R.A.3
  • 43
    • 4043096374 scopus 로고    scopus 로고
    • Rings, ellipses and horseshoes: How purple bacteria harvest solar energy
    • DOI 10.1023/B:PRES.0000036883.56959.a9
    • Cogdell, R. J., Gardiner, A. T., Roszak, A. W., Law, C. J., Southall, J., and Isaacs, N. W. (2004) Rings, ellipses and horseshoes: How purple bacteria harvest solar energy. Photosynth. Res. 81, 207-214. (Pubitemid 39059685)
    • (2004) Photosynthesis Research , vol.81 , Issue.3 , pp. 207-214
    • Cogdell, R.J.1    Gardiner, A.T.2    Roszak, A.W.3    Law, C.J.4    Southall, J.5    Isaacs, N.W.6
  • 44
    • 0001753915 scopus 로고
    • Oligomerization states and associations of light-harvesting pigment-protein complexes of Rhodobacter sphaeroides as analyzed by lithium dodecyl sulfate-polyacrylamide gel electrophoresis
    • Hunter, C. N., Pennoyer, J. D., Sturgis, J. N., Farrelly, D., and Niederman, R. A. (1988) Oligomerization states and associations of light-harvesting pigment-protein complexes of Rhodobacter sphaeroides as analyzed by lithium dodecyl sulfate-polyacrylamide gel electrophoresis. Biochemistry 27, 3459-3467.
    • (1988) Biochemistry , vol.27 , pp. 3459-3467
    • Hunter, C.N.1    Pennoyer, J.D.2    Sturgis, J.N.3    Farrelly, D.4    Niederman, R.A.5
  • 45
    • 0023972876 scopus 로고
    • Physiological and structural analysis of light-harvesing mutants of Rhodobacter sphaeroides
    • Kiley, P. J., Varga, A., and Kaplan, S. (1988) Physiological and structural analysis of light-harvesing mutants of Rhodobacter sphaeroides. J. Bacteriol. 170, 1103-1115.
    • (1988) J. Bacteriol. , vol.170 , pp. 1103-1115
    • Kiley, P.J.1    Varga, A.2    Kaplan, S.3
  • 46
    • 0037047004 scopus 로고    scopus 로고
    • Isolation, size estimates, and spectral heterogeneity of an oligomeric series of light-harvesting 1 complexes from Rhodobacter sphaeroides
    • DOI 10.1021/bi011663b
    • Westerhuis, W. H. J., Sturgis, J. N., Ratcliffe, E. C., Hunter, C. N., and Niederman, R. A. (2002) Isolation, size estimates, and spectral heterogeneity of an oligomeric series of light-harvesting 1 complexes from Rhodobacter sphaeroides. Biochemistry 41, 8698-8707. (Pubitemid 34743310)
    • (2002) Biochemistry , vol.41 , Issue.27 , pp. 8698-8707
    • Westerhuis, W.H.J.1    Sturgis, J.N.2    Ratcliffe, E.C.3    Hunter, C.N.4    Niederman, R.A.5
  • 47
    • 0033081638 scopus 로고    scopus 로고
    • Supramolecular organization of the photosynthetic apparatus of Rhodobacter sphaeroides
    • DOI 10.1093/emboj/18.3.534
    • Jungas, C., Ranck, J.-L., Rigaud, J.-L., Joliot, P., and Vermeglio, A. (1999) Supramolecular organization of the photosynthetic apparatus of Rhodobacter sphaeroides. EMBO J. 18, 534-542. (Pubitemid 29057238)
    • (1999) EMBO Journal , vol.18 , Issue.3 , pp. 534-542
    • Jungas, C.1    Ranck, J.-L.2    Rigaud, J.-L.3    Joliot, P.4    Vermeglio, A.5
  • 48
    • 66049131773 scopus 로고    scopus 로고
    • Reaction Center-Light Harvesting Core Complexes of Purple Bacteria
    • (Hunter, C. N., Daldal, F., Thurnauer, M. C., and Beatty, J. T., Eds.) Springer, Dordrecht, The Netherlands
    • Bullough, P. A., Qian, P., and Hunter, C. N. (2008) Reaction Center-Light Harvesting Core Complexes of Purple Bacteria. In The Purple Phototrophic Bactria. Advances in Photosynthesis and Respiration (Hunter, C. N., Daldal, F., Thurnauer, M. C., and Beatty, J. T., Eds.) Vol.28, pp 155-179, Springer, Dordrecht, The Netherlands.
    • (2008) The Purple Phototrophic Bactria. Advances in Photosynthesis and Respiration , vol.28 , pp. 155-179
    • Bullough, P.A.1    Qian, P.2    Hunter, C.N.3
  • 49
    • 20344374627 scopus 로고    scopus 로고
    • The 8.5 Å projection structure of the core RC-LH1-PufX dimer of Rhodobacter sphaeroides
    • DOI 10.1016/j.jmb.2005.04.032, PII S0022283605004419
    • Qian, P., Hunter, C. N., and Bullough, P. A. (2005) The 8.5 Å projection structure of the core RC-LH1-PufX dimer of Rhodobacter sphaeroides. J. Mol. Biol. 349, 948-960. (Pubitemid 40779618)
    • (2005) Journal of Molecular Biology , vol.349 , Issue.5 , pp. 948-960
    • Qian, P.1    Hunter, C.N.2    Bullough, P.A.3
  • 50
    • 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., and Hunter, C. N. (2008) Three-dimensional reconstruction of a membrane-bending complex: The RC-LH1-PufX core dimer of Rhodobacter sphaeroides. J. Biol. Chem. 283, 14002-14011.
    • (2008) J. Biol. Chem. , vol.283 , pp. 14002-14011
    • Qian, P.1    Bullough, P.A.2    Hunter, C.N.3
  • 51
    • 0037424652 scopus 로고    scopus 로고
    • The structure and thermal motion of the B800-850 LH2 complex from Rps. acidophila at 2.0 Å resolution and 100 K: New structural features and functionally relevant motions
    • DOI 10.1016/S0022-2836(03)00024-X
    • Papiz, M. Z., Prince, S. M., Howard, T., Cogdell, R. J., and Isaacs, N. W. (2003) The structure and thermal motion of the B800-850 LH2 complex from Rhodopsedomonas acidophila at 2.0 Å resolution and 100 K: New structural features and functionally relevant motions. J. Mol. Biol. 326, 1523-1538. (Pubitemid 36277668)
    • (2003) Journal of Molecular Biology , vol.326 , Issue.5 , pp. 1523-1538
    • Papiz, M.Z.1    Prince, S.M.2    Howard, T.3    Cogdell, R.J.4    Isaacs, N.W.5
  • 52
    • 0942287196 scopus 로고    scopus 로고
    • Structural Role of PufX in the Dimerization of the Photosynthetic Core Complex of Rhodobacter sphaeroides
    • DOI 10.1074/jbc.M310050200
    • Scheuring, S., Francia, F., Busselez, J., Melandri, B. A., Rigaud, J.-L., and Lévy, D. (2004) Structural role of PufX in the dimerization of the photosynthetic core complex of Rhodobacter sphaeroides. J. Biol. Chem. 279, 3620-3626. (Pubitemid 38140603)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.5 , pp. 3620-3626
    • Scheuring, S.1    Francia, F.2    Busselez, J.3    Melandri, B.A.4    Rigaud, J.-L.5    Levy, D.6
  • 53
    • 0032483080 scopus 로고    scopus 로고
    • Isolation of the PufX protein from Rhodobacter capsulatus and Rhodobacter sphaeroides: Evidence for its interaction with the R- 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., and Loach, P. A. (1998) Isolation of the PufX protein from Rhodobacter capsulatus and Rhodobacter sphaeroides: Evidence for its interaction with the R-polypeptide of the core light-harvesting complex. Biochemistry 37, 11055-11063. (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
  • 54
    • 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., and Oesterhelt, D. (1995) 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 34, 15248-15258.
    • (1995) Biochemistry , vol.34 , pp. 15248-15258
    • Barz, W.P.1    Vermeglio, A.2    Francia, F.3    Venturoli, G.4    Melandri, B.A.5    Oesterhelt, D.6
  • 55
    • 33845433893 scopus 로고    scopus 로고
    • The solution structure of the PufX polypeptide from Rhodobacter sphaeroides
    • Tunnicliffe, R. B., Ratcliffe, E. C., Hunter, C. N., and Williamson, M. P. (2006) The solution structure of the PufX polypeptide from Rhodobacter sphaeroides. FEBS Lett. 580, 6967-6971.
    • (2006) FEBS Lett. , vol.580 , pp. 6967-6971
    • Tunnicliffe, R.B.1    Ratcliffe, E.C.2    Hunter, C.N.3    Williamson, M.P.4
  • 57
    • 34547111087 scopus 로고    scopus 로고
    • Stabilization of charge separation and cardiolipin confinement in antenna-reaction center complexes purified from Rhodobacter sphaeroides
    • Dezi, M., Francia, F., Mallardi, A., Colafemmina, G., Palazzo, G., and Venturoli, G. (2007) Stabilization of charge separation and cardiolipin confinement in antenna-reaction center complexes purified from Rhodobacter sphaeroides. Biochim. Biophys. Acta 1767, 1041-1056.
    • (2007) Biochim. Biophys. Acta , vol.1767 , pp. 1041-1056
    • Dezi, M.1    Francia, F.2    Mallardi, A.3    Colafemmina, G.4    Palazzo, G.5    Venturoli, G.6
  • 58
    • 0033603006 scopus 로고    scopus 로고
    • The reaction center-LH1 antenna complex of Rhodobacter sphaeroides contains one PufX molecule which is involved in dimerization of this complex
    • Francia, F., Wang, J., Venturoli, G., Melandri, B. A., Barz, W. P., and Oesterhelt, D. (1999) The reaction center-LH1 antenna complex of Rhodobacter sphaeroides contains one PufX molecule which is involved in dimerization of this complex. Biochemistry 38, 6834-6845. (Pubitemid 129514985)
    • (1999) Biochemistry , vol.38 , Issue.21 , pp. 6834-6845
    • Francia, F.1    Wang, J.2    Venturoli, G.3    Melandri, B.A.4    Barz, W.P.5    Oesterhelt, D.6
  • 59
    • 85047694996 scopus 로고    scopus 로고
    • Role of the N- And C-terminal regions of the PufX protein in the structural organization of the photosynthetic core complex of Rhodobacter sphaeroides
    • DOI 10.1046/j.1432-1327.2002.02834.x
    • Francia, F., Wang, J., Zischka, H., Venturoli, G., and Oesterhelt, D. (2002) Role of the N- and C-terminal regions of the PufX protein in the structural organization of the photosynthetic core complex of Rhodobacter sphaeroides. Eur. J. Biochem. 269, 1877-1885. (Pubitemid 34429669)
    • (2002) European Journal of Biochemistry , vol.269 , Issue.7 , pp. 1877-1885
    • Francia, F.1    Wang, J.2    Zischka, H.3    Venturoli, G.4    Oesterhelt, D.5
  • 60
    • 0001864802 scopus 로고
    • A Rhodobacter sphaeroides puf L, M and X deletion mutant and its complementation in trans with a 5.3 kb puf operon shuttle fragment
    • Farchaus, J. W., and Oesterhelt, D. (1989) A Rhodobacter sphaeroides puf L, M and X deletion mutant and its complementation in trans with a 5.3 kb puf operon shuttle fragment. EMBO J. 8, 47-54.
    • (1989) EMBO J. , vol.8 , pp. 47-54
    • Farchaus, J.W.1    Oesterhelt, D.2
  • 61
    • 0026534726 scopus 로고
    • Pleiotropic effects of pufX gene deletion on the structure and function of the photosynthetic apparatus of Rhodobacter capsulatus
    • Lilburn, T. G., Haith, C. E., Prince, R. C., and Beatty, J. T. (1992) Pleiotropic effects of pufX gene deletion on the structure and function of the photosynthetic apparatus of Rhodobacter capsulatus. Biochim. Biophys. Acta 1100, 160-170.
    • (1992) Biochim. Biophys. Acta , vol.1100 , pp. 160-170
    • Lilburn, T.G.1    Haith, C.E.2    Prince, R.C.3    Beatty, J.T.4
  • 62
    • 46349084478 scopus 로고    scopus 로고
    • Structure, function and interactions of the PufX protein
    • Holden-Dye, K., Crouch, L. I., and Jones, M. R. (2008) Structure, function and interactions of the PufX protein. Biochim. Biophys. Acta 1777, 613-630.
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 613-630
    • Holden-Dye, K.1    Crouch, L.I.2    Jones, M.R.3
  • 63
    • 0023395661 scopus 로고
    • Structure of the reaction center from Rhodobacter sphaeroides R-26: The cofactors
    • Allen, J. P., Feher, G., Yeates, T. O., Komiya, H., and Rees, D. C. (1987) Structure of the reaction center from Rhodobacter sphaeroides R-26: The cofactors. Proc. Natl. Acad. Sci. U.S.A. 84, 5730-5734.
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 5730-5734
    • Allen, J.P.1    Feher, G.2    Yeates, T.O.3    Komiya, H.4    Rees, D.C.5
  • 64
    • 12044253563 scopus 로고
    • Entropy-driven formation of a superlattice in hard-sphere binary mixture
    • Eldridge, M. D., Madden, P. A., and Frenkel, D. (1993) Entropy-driven formation of a superlattice in hard-sphere binary mixture. Nature 365, 35-37.
    • (1993) Nature , vol.365 , pp. 35-37
    • Eldridge, M.D.1    Madden, P.A.2    Frenkel, D.3
  • 65
    • 0030012293 scopus 로고    scopus 로고
    • The effect of different levels of the B800-850 light-harvesting complex on intracytoplasmic membrane development in Rhodobacter sphaeroides
    • DOI 10.1007/s002030050321
    • Sturgis, J. N., and Niederman, R. A. (1996) The effect of different levels of the B800-850 light-harvesting complex on intracytoplasmic membrane development in Rhodobacter sphaeroides. Arch. Microbiol. 165, 235-242. (Pubitemid 26153405)
    • (1996) Archives of Microbiology , vol.165 , Issue.4 , pp. 235-242
    • Sturgis, J.N.1    Niederman, R.A.2
  • 66
    • 55549109763 scopus 로고    scopus 로고
    • Intrinsic curvature properties of photosynthetic proteins in chromatophores
    • Chandler, D. E., Hsin, J., Harrison, C. B., Gumbart, J., and Schulten, K. (2008) Intrinsic curvature properties of photosynthetic proteins in chromatophores. Biophys. J. 95, 2822-2836.
    • (2008) Biophys. J. , vol.95 , pp. 2822-2836
    • Chandler, D.E.1    Hsin, J.2    Harrison, C.B.3    Gumbart, J.4    Schulten, K.5
  • 67
    • 36849078156 scopus 로고    scopus 로고
    • Mutation of a single residue, β-glutamate-20, alters protein-lipid interactions of light harvesting complex II
    • DOI 10.1111/j.1365-2958.2007.06017.x
    • Kwa, L. G., Wegmann, D., Brügger, B., Wieland, F. T., Wanner, G., and Braun, P. (2008) Mutation of a single residue, β-glutamate-20, alters protein-lipid interactions of light harvesting complex II. Mol. Microbiol. 67, 63-77. (Pubitemid 350231135)
    • (2008) Molecular Microbiology , vol.67 , Issue.1 , pp. 63-77
    • Kwa, L.G.1    Wegmann, D.2    Brugger, B.3    Wieland, F.T.4    Wanner, G.5    Braun, P.6
  • 68
    • 0037158935 scopus 로고    scopus 로고
    • Nature of disorder and inter-complex energy transfer in LH2 at room temperature: A three pulse photon echo peak shift study
    • DOI 10.1021/jp014054m
    • Agarwal, R., Rizvi, A. H., Prall, B. S., Olsen, J. D., Hunter, C. N., and Fleming, G. R. (2002) Nature of disorder and inter-complex energy transfer in LH2 at room temperature: A three pulse photon echo peak shift study. J. Phys. Chem. A 106, 7573-7578. (Pubitemid 35382557)
    • (2002) Journal of Physical Chemistry a , vol.106 , Issue.33 , pp. 7573-7578
    • Agarwal, R.1    Rizvi, A.H.2    Prall, B.S.3    Olsen, J.D.4    Hunter, C.N.5    Fleming, G.R.6
  • 69
    • 33751257776 scopus 로고    scopus 로고
    • Dynamics and diffusion in photosynthetic membranes from Rhodospirillum photometricum
    • Scheuring, S., and Sturgis, J. N. (2006) Dynamics and diffusion in photosynthetic membranes from Rhodospirillum photometricum. Biophys. J. 91, 3707-3717.
    • (2006) Biophys. J. , vol.91 , pp. 3707-3717
    • Scheuring, S.1    Sturgis, J.N.2
  • 70
    • 9144264281 scopus 로고    scopus 로고
    • Variable LH2 stoichiometry and core clustering in native membranes of Rhodospirillum photometricum
    • DOI 10.1038/sj.emboj.7600429
    • Scheuring, S., Rigaud, J. L., and Sturgis, J. N. (2004) Variable LH2 stoichiometry and core clustering in native membranes of Rhodospirillum photometricum. EMBO J. 23, 4127-4133. (Pubitemid 39546151)
    • (2004) EMBO Journal , vol.23 , Issue.21 , pp. 4127-4133
    • Scheuring, S.1    Rigaud, J.-L.2    Sturgis, J.N.3
  • 71
    • 0042406100 scopus 로고
    • Oligomerization-State Dependent Spectroscopic Properties of the B850 Light-Harvesting Complex of Rhodobacter sphaeroides R-26.1
    • (Murata, N., Ed.) Kluwer Academic Publishers, Boston
    • Westerhuis, W. H. J., Xiao, Z., and Niederman, R. A. (1992) Oligomerization-State Dependent Spectroscopic Properties of the B850 Light-Harvesting Complex of Rhodobacter sphaeroides R-26.1. In Research in Photosynthesis (Murata, N., Ed.) pp 93-96, Kluwer Academic Publishers, Boston.
    • (1992) Research in Photosynthesis , pp. 93-96
    • Westerhuis, W.H.J.1    Xiao, Z.2    Niederman, R.A.3
  • 73
    • 13444267399 scopus 로고    scopus 로고
    • Sequential assembly of photosynthetic units in Rhodobacter sphaeroides as revealed by fast repetition rate analysis of variable bacteriochlorophyll a fluorescence
    • DOI 10.1016/j.bbabio.2004.11.004
    • Koblízek, M., Shih, J. D., Breitbart, S. I., Ratcliffe, E. C., Kolber, Z. S., Hunter, C. N., and Niederman, R. A. (2005) Sequential assembly of photosynthetic units in Rhodobacter sphaeroides as revealed by fast repetition rate analysis of variable bacteriochlorophyll a fluorescence. Biochim. Biophys. Acta 1706, 220-231. (Pubitemid 40208431)
    • (2005) Biochimica et Biophysica Acta - Bioenergetics , vol.1706 , Issue.3 , pp. 220-231
    • Koblizek, M.1    Shih, J.D.2    Breitbart, S.I.3    Ratcliffe, E.C.4    Kolber, Z.S.5    Hunter, C.N.6    Niederman, R.A.7
  • 74
    • 0036007349 scopus 로고    scopus 로고
    • The 7.5-Å electron density and spectroscopic properties of a novel low-light B800 LH2 from Rhodopseudomonas palustris
    • Hartigan, N., Tharia, H. A., Sweeney, F., Lawless, A. M., and Papiz, M. Z. (2002) The 7.5-Å electron density and spectroscopic properties of a novel low-light B800 LH2 from Rhodopseudomonas palustris. Biophys. J. 82, 963-977. (Pubitemid 34111234)
    • (2002) Biophysical Journal , vol.82 , Issue.2 , pp. 963-977
    • Hartigan, N.1    Tharia, H.A.2    Sweeney, F.3    Lawless, A.M.4    Papiz, M.Z.5
  • 75
    • 23944495805 scopus 로고    scopus 로고
    • A bacteriophytochrome regulates the synthesis of LH4 complexes in Rhodopseudomonas palustris
    • DOI 10.1007/s11120-005-1369-7
    • Evans, K., Fordham-Skelton, A. P., Mistry, H., Reynolds, C. D., Lawless, A. M., and Papiz, M. Z. (2005) A bacteriophytochrome regulates the synthesis of LH4 complexes in Rhodopseudomonas palustris. Photosynth. Res. 85, 169-180. (Pubitemid 41187658)
    • (2005) Photosynthesis Research , vol.85 , Issue.2 , pp. 169-180
    • Evans, K.1    Fordham-Skelton, A.P.2    Mistry, H.3    Reynolds, C.D.4    Lawless, A.M.5    Papiz, M.Z.6
  • 76
    • 25444438210 scopus 로고    scopus 로고
    • A new type of bacteriophytochrome acts in tandem with a classical bacteriophytochrome to control the antennae synthesis in Rhodopseudomonas palustris
    • DOI 10.1074/jbc.M506890200
    • Giraud, E., Zappa, S., Vuillet, L., Adriano, J. M., Hannibal, L., Fardoux, J., Berthomieu, C., Bouyer, P., Pignol, D., and Verméglio, A. (2005) A new type of bacteriophytochrome acts in tandem with a classical bacteriophytochrome to control the antennae synthesis in Rhodopseudomonas palustris. J. Biol. Chem. 280, 32389-32397. (Pubitemid 41361849)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.37 , pp. 32389-32397
    • Giraud, E.1    Zappa, S.2    Vuillet, L.3    Adriano, J.-M.4    Hannibal, L.5    Fardoux, J.6    Berthomieu, C.7    Bouyer, P.8    Pignol, D.9    Vermeglio, A.10
  • 77
    • 33746753346 scopus 로고    scopus 로고
    • 1 complex
    • DOI 10.1529/biophysj.105.078501
    • Geyer, T., and Helms, V. (2006) A spatial model of the chromatophore vesicles of Rhodobacter sphaeroides and the position of the cytochrome bc1 complex. Biophys. J. 91, 921-926. (Pubitemid 44161924)
    • (2006) Biophysical Journal , vol.91 , Issue.3 , pp. 921-926
    • Geyer, T.1    Helms, V.2
  • 78
    • 0036415211 scopus 로고    scopus 로고
    • Membrane biogenesis in anoxygenic photosynthetic prokaryotes
    • DOI 10.1023/A:1020481132492
    • Drews, G., and Niederman, R. A. (2002) Membrane biogenesis in anoxygenic photosynthetic prokaryotes. Photosynth. Res. 73, 87-94. (Pubitemid 35293692)
    • (2002) Photosynthesis Research , vol.73 , Issue.1-3 , pp. 87-94
    • Drews, G.1    Niederman, R.A.2
  • 80
    • 35548991850 scopus 로고    scopus 로고
    • Heterogeneity of photosynthetic membranes from Rhodobacter capsulatus: Size dispersion and ATP synthase distribution
    • Gubellini, F., Francia, F., Turina, P., Lévy, D., Venturoli, G., and Melandri, B. A. (2007) Heterogeneity of photosynthetic membranes from Rhodobacter capsulatus: Size dispersion and ATP synthase distribution. Biochim. Biophys. Acta 1767, 1340-1352.
    • (2007) Biochim. Biophys. Acta , vol.1767 , pp. 1340-1352
    • Gubellini, F.1    Francia, F.2    Turina, P.3    Lévy, D.4    Venturoli, G.5    Melandri, B.A.6
  • 81
    • 56749177094 scopus 로고    scopus 로고
    • Organisation and function of the Phaeospirillum molischianum photosynthetic apparatus
    • Mascle-Allemand, C., Lavergne, J., Bernadac, A., and Sturgis, J. N. (2008) Organisation and function of the Phaeospirillum molischianum photosynthetic apparatus. Biochim. Biophys. Acta 1777, 1552-1559.
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 1552-1559
    • Mascle-Allemand, C.1    Lavergne, J.2    Bernadac, A.3    Sturgis, J.N.4
  • 82
    • 35349015148 scopus 로고    scopus 로고
    • Rows of ATP synthase dimers in native mitochondrial inner membranes
    • DOI 10.1529/biophysj.107.109728
    • Buzhynskyy, N., Sens, P., Prima, V., Sturgis, J. N., and Scheuring, S. (2007) Rows of ATP synthase dimers in native mitochondrial inner membranes. Biophys. J. 93, 2870-2876. (Pubitemid 47607823)
    • (2007) Biophysical Journal , vol.93 , Issue.8 , pp. 2870-2876
    • Buzhynsky, N.1    Sens, P.2    Prima, V.3    Sturgis, J.N.4    Scheuring, S.5
  • 83
    • 41949123425 scopus 로고    scopus 로고
    • Dimer ribbons of ATP synthase shape the inner mitochondrial membrane
    • Strauss, M., Hofhaus, G., Schröder, R. R., and Kühlbrandt, W. (2008) Dimer ribbons of ATP synthase shape the inner mitochondrial membrane. EMBO J. 27, 1154-1160.
    • (2008) EMBO J. , vol.27 , pp. 1154-1160
    • Strauss, M.1    Hofhaus, G.2    Schröder, R.R.3    Kühlbrandt, W.4
  • 84
    • 0018356319 scopus 로고
    • Orientation of chromatophores and spheroplast-derived membrane vesicles of Rhodopseudomonas sphaeroides: Analysis by localization of enzyme activities
    • DOI 10.1016/0003-9861(79)90379-5
    • Takemoto, J., and Bachmann, R. C. (1979) Orientation of chromatophores and spheroplast-derived membrane vesicles of Rhodopseudomonas sphaeroides: Analysis by localization of enzyme activities. Arch. Biochem. Biophys. 195, 526-534. (Pubitemid 9235085)
    • (1979) Archives of Biochemistry and Biophysics , vol.195 , Issue.2 , pp. 526-534
    • Takemoto, J.1    Bachmann, R.C.2
  • 85
    • 0028926367 scopus 로고
    • 1 complex of Rhodobacter sphaeroides
    • 1 complex of Rhodobacter sphaeroides. Biochem. J. 305, 823-828.
    • (1995) Biochem. J. , vol.305 , pp. 823-828
    • Wu, J.1    Niederman, R.A.2
  • 86
    • 0034686023 scopus 로고    scopus 로고
    • 1 complex from Rhodobacter sphaeroides: Localization of regions essential for interaction with the three-subunit core complex
    • 1 complex from Rhodobacter sphaeroides: Localization of regions essential for interaction with the three-subunit core complex. J. Biol. Chem. 275, 15287-15294.
    • (2000) J. Biol. Chem. , vol.275 , pp. 15287-15294
    • Tso, S.C.1    Shenoy, S.K.2    Quinn, B.N.3    Yu, L.4
  • 88
    • 0021913479 scopus 로고
    • Photosynthetic membrane development in rhodopseudomonas sphaeroides. Spectral and kinetic characterization of redox components of light-driven electron flow in apparent photosynthetic membrane growth initiation sites
    • Bowyer, J. R., Hunter, C. N., Ohnishi, T., and Niederman, R. A. (1985) Photosynthetic membrane development in Rhodopseudomonas sphaeroides: Spectral and kinetic characterization of redox components of light-driven electron flow in apparent photosynthetic membrane growth initiation sites. J. Biol. Chem. 260, 3295-3304. (Pubitemid 15115242)
    • (1985) Journal of Biological Chemistry , vol.260 , Issue.6 , pp. 3295-3304
    • Bowyer, J.R.1    Hunter, C.N.2    Ohnishi, T.3    Niederman, R.A.4
  • 89
    • 13444287778 scopus 로고    scopus 로고
    • Fast oxidation of the primary electron acceptor under anaerobic conditions requires the organization of the photosynthetic chain of Rhodobacter sphaeroides in supercomplexes
    • DOI 10.1016/j.bbabio.2004.11.002
    • Joliot, P., Joliot, A., and Verméglio, A. (2005) Fast oxidation of the primary electron acceptor under anaerobic conditions requires the organization of the photosynthetic chain of Rhodobacter sphaeroides in supercomplexes. Biochim. Biophys. Acta 1706, 204-214. (Pubitemid 40208429)
    • (2005) Biochimica et Biophysica Acta - Bioenergetics , vol.1706 , Issue.3 , pp. 204-214
    • Joliot, P.1    Joliot, A.2    Vermeglio, A.3
  • 90
    • 0031877116 scopus 로고    scopus 로고
    • Chromatophore heterogeneity explains phenomena seen in Rhodobacter sphaeroides previously attributed to supercomplexes
    • Crofts, A., Guergova-Kuras, M., and Hong, S. J. (1998) Chromatophore heterogeneity explains phenomena seen in Rhodobacter sphaeroides previously attributed to supercomplexes. Photosynth. Res. 55, 357-362. (Pubitemid 28351426)
    • (1998) Photosynthesis Research , vol.55 , Issue.2-3 , pp. 357-362
    • Crofts, A.1    Guergova-Kuras, M.2    Hong, S.3
  • 91
    • 56749157545 scopus 로고    scopus 로고
    • Functional Coupling between Reaction Centers and Cytochrome bc1 Complexes
    • (Hunter, C. N., Daldal, F., Thurnauer, M. C., and Beatty, J. T., Eds.) Springer, Dordrecht, The Netherlands
    • Lavergne, J., Verméglio, A., and Joliot, P. (2008) Functional Coupling Between Reaction Centers and Cytochrome bc1 Complexes. In The Purple Phototrophic Bactria. Advances in Photosynthesis and Respiration (Hunter, C. N., Daldal, F., Thurnauer, M. C., and Beatty, J. T., Eds.) Vol.28, pp 509-536, Springer, Dordrecht, The Netherlands.
    • (2008) The Purple Phototrophic Bactria. Advances in Photosynthesis and Respiration , vol.28 , pp. 509-536
    • Lavergne, J.1    Verméglio, A.2    Joliot, P.3
  • 92
    • 33644687594 scopus 로고    scopus 로고
    • Three-dimensional organization of higher-plant chloroplast thylakoid membranes revealed by electron tomography
    • Shimoni, E., Rav-Hon, O., Ohad, I., Brumfeld, V., and Reich, Z. (2005) Three-dimensional organization of higher-plant chloroplast thylakoid membranes revealed by electron tomography. Plant Cell 17, 2580-2586.
    • (2005) Plant Cell , vol.17 , pp. 2580-2586
    • Shimoni, E.1    Rav-Hon, O.2    Ohad, I.3    Brumfeld, V.4    Reich, Z.5
  • 93
    • 0037112863 scopus 로고    scopus 로고
    • From chloroplasts to photosystems: In situ scanning force microscopy on intact thylakoid membranes
    • DOI 10.1093/emboj/cdf624
    • Kaftan, D., Brumfeld, V., Nevo, R., Scherz, A., and Reich, Z. (2002) From chloroplasts to photosystems: In situ scanning force microscopy on intact thylakoid membranes. EMBO J. 21, 6146-6153. (Pubitemid 35415331)
    • (2002) EMBO Journal , vol.21 , Issue.22 , pp. 6146-6153
    • Kaftan, D.1    Brumfeld, V.2    Nevo, R.3    Scherz, A.4    Reich, Z.5
  • 94
    • 2442503725 scopus 로고    scopus 로고
    • Simultaneous atomic-force and two-photon fluorescence imaging of biological specimens in vivo
    • DOI 10.1016/j.ultramic.2003.12.009, PII S0304399104000105
    • Gradinaru, C. C., Martinsson, P., Aartsma, T. J., and Schmidt, T. (2004) Simultaneous atomic-force and two-photon fluorescence imaging of biological specimens in vivo. Ultramicroscopy 99, 235-245. (Pubitemid 38626129)
    • (2004) Ultramicroscopy , vol.99 , Issue.4 , pp. 235-245
    • Gradinaru, C.C.1    Martinsson, P.2    Aartsma, T.J.3    Schmidt, T.4
  • 95
    • 8544240147 scopus 로고    scopus 로고
    • Transversal and lateral exciton energy transfer in grana thylakoids of spinach
    • DOI 10.1021/bi048473w
    • Kirchhoff, H., Borinski, M., Lenhert, S., Chi, L. F., and Büchel, C. (2004) Transversal and lateral exciton energy transfer in grana thylakoids of spinach. Biochemistry 43, 14508-14516. (Pubitemid 39491985)
    • (2004) Biochemistry , vol.43 , Issue.45 , pp. 14508-14516
    • Kirchhoff, H.1    Borinski, M.2    Lenhert, S.3    Chi, L.4    Buchel, C.5
  • 96
    • 37849002062 scopus 로고    scopus 로고
    • Probing the organization of photosystem II in photosynthetic membranes by atomic force microscopy
    • Kirchhoff, H., Lenhert, S., Büchel, C., Chi, L., and Nield, J. (2008) Probing the organization of photosystem II in photosynthetic membranes by atomic force microscopy. Biochemistry 47, 431-440.
    • (2008) Biochemistry , vol.47 , pp. 431-440
    • Kirchhoff, H.1    Lenhert, S.2    Büchel, C.3    Chi, L.4    Nield, J.5
  • 97
    • 43049156431 scopus 로고    scopus 로고
    • Molecular crowding and order in photosynthetic membranes
    • Kirchhoff, H. (2008) Molecular crowding and order in photosynthetic membranes. Trends Plant Sci. 13, 201-207.
    • (2008) Trends Plant Sci. , vol.13 , pp. 201-207
    • Kirchhoff, H.1
  • 98
    • 43049166553 scopus 로고    scopus 로고
    • Protein diffusion and macromolecular crowding in thylakoid membranes
    • DOI 10.1104/pp.107.115170
    • Kirchhoff, H., Haferkamp, S., Allen, J. F., Epstein, D. B. A., and Mullineaux, C. W. (2008) Protein diffusion and macromolecular crowding in thylakoid membranes. Plant Physiol. 146, 1571-1578. (Pubitemid 352844058)
    • (2008) Plant Physiology , vol.146 , Issue.4 , pp. 1571-1578
    • Kirchhoff, H.1    Haferkamp, S.2    Allen, J.F.3    Epstein, D.B.A.4    Mullineaux, C.W.5
  • 99
    • 0037117740 scopus 로고    scopus 로고
    • Molecular architecture of the thylakoid membrane: Lipid diffusion space for plastoquinone
    • DOI 10.1021/bi011650y
    • Kirchhoff, H., Mukherjee, U., and Galla, H. J. (2002) Molecular architecture of the thylakoid membrane: Lipid diffusion space for plastoquinone. Biochemistry 41, 4872-4882. (Pubitemid 34298654)
    • (2002) Biochemistry , vol.41 , Issue.15 , pp. 4872-4882
    • Kirchhoff, H.1    Mukherjee, U.2    Galla, H.-J.3
  • 100
    • 33846014316 scopus 로고    scopus 로고
    • The supramolecular architecture of junctional microdomains in native lens membranes
    • DOI 10.1038/sj.embor.7400858, PII 7400858
    • Buzhynskyy, N., Hite, R. K., Walz, T., and Scheuring, S. (2007) The supramolecular architecture of junctional microdomains in native lens membranes. EMBO Rep. 8, 51-55. (Pubitemid 46043800)
    • (2007) EMBO Reports , vol.8 , Issue.1 , pp. 51-55
    • Buzhynskyy, N.1    Hite, R.K.2    Walz, T.3    Scheuring, S.4
  • 101
    • 34247567854 scopus 로고    scopus 로고
    • Supramolecular Assembly of VDAC in Native Mitochondrial Outer Membranes
    • DOI 10.1016/j.jmb.2007.03.063, PII S0022283607004299
    • Goncalves, R. P., Buzhynskyy, N., Prima, V., Sturgis, J. N., and Scheuring, S. (2007) Supramolecular assembly of VDAC in native mitochondrial outer membranes. J. Mol. Biol. 369, 413-418. (Pubitemid 46678059)
    • (2007) Journal of Molecular Biology , vol.369 , Issue.2 , pp. 413-418
    • Goncalves, R.P.1    Buzhynskyy, N.2    Prima, V.3    Sturgis, J.N.4    Scheuring, S.5
  • 104
    • 33646021951 scopus 로고    scopus 로고
    • Detection and localization of single molecular recognition events using atomic force microscopy
    • Hinterdorfer, P., and Dufrene, Y. F. (2006) Detection and localization of single molecular recognition events using atomic force microscopy. Nat. Methods 3, 347-355.
    • (2006) Nat. Methods , vol.3 , pp. 347-355
    • Hinterdorfer, P.1    Dufrene, Y.F.2
  • 105
    • 48649106769 scopus 로고    scopus 로고
    • AFM: A nanotool in membrane biology
    • Muller, D. J. (2008) AFM: A nanotool in membrane biology. Biochemistry 47, 7986-7998.
    • (2008) Biochemistry , vol.47 , pp. 7986-7998
    • Muller, D.J.1
  • 106
    • 13244259258 scopus 로고    scopus 로고
    • Combined AFM and confocal fluorescence microscope for applications in bio-nanotechnology
    • DOI 10.1111/j.0022-2720.2005.01428.x
    • Kassies, R., Van der Werf, K. O., Lenferink, A., Hunter, C. N., Olsen, J. D., Subramaniam, V., and Otto, C. (2005) Combined AFM and confocal fluorescence microscope for applications in bio-nanotechnology. J. Microsc. (Oxford, U.K.) 217, 109-116. (Pubitemid 40188366)
    • (2005) Journal of Microscopy , vol.217 , Issue.1 , pp. 109-116
    • Kassies, R.1    Van Der Werf, K.O.2    Lenferink, A.3    Hunter, C.N.4    Olsen, J.D.5    Subramaniam, V.6    Otto, C.7


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