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Volumn 1777, Issue 7-8, 2008, Pages 613-630

Structure, function and interactions of the PufX protein

Author keywords

Light harvesting; Photosynthesis; Photosystem; PufX; Purple bacteria

Indexed keywords

CAROTENOID; OLIGOMER; PROTEIN; PUFX PROTEIN;

EID: 46349084478     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2008.04.015     Document Type: Review
Times cited : (46)

References (154)
  • 1
    • 0032568640 scopus 로고    scopus 로고
    • Architecture and mechanism of the light-harvesting apparatus of purple bacteria
    • Hu X., Damjanović A., Ritz T., and Schulten K. Architecture and mechanism of the light-harvesting apparatus of purple bacteria. Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 5935-5941
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 5935-5941
    • Hu, X.1    Damjanović, A.2    Ritz, T.3    Schulten, K.4
  • 5
    • 20444382012 scopus 로고    scopus 로고
    • Watching the components of photosynthetic bacterial membranes and their in situ organisation by atomic force microscopy
    • Scheuring S., Lévy D., and Rigaud J.-L. Watching the components of photosynthetic bacterial membranes and their in situ organisation by atomic force microscopy. Biochim. Biophys. Acta 1712 (2005) 109-127
    • (2005) Biochim. Biophys. Acta , vol.1712 , pp. 109-127
    • Scheuring, S.1    Lévy, D.2    Rigaud, J.-L.3
  • 6
    • 33845698300 scopus 로고    scopus 로고
    • The architecture and function of the light-harvesting apparatus of purple bacteria: from single molecules to in vivo membranes
    • Cogdell R.J., Gall A., and Kohler J. The architecture and function of the light-harvesting apparatus of purple bacteria: from single molecules to in vivo membranes. Quart. Rev. Biophys. 39 (2006) 227-324
    • (2006) Quart. Rev. Biophys. , vol.39 , pp. 227-324
    • Cogdell, R.J.1    Gall, A.2    Kohler, J.3
  • 7
    • 33748578027 scopus 로고    scopus 로고
    • AFM studies of the supramolecular assembly of bacterial photosynthetic core-complexes
    • Scheuring S. AFM studies of the supramolecular assembly of bacterial photosynthetic core-complexes. Curr. Op. Chem. Biol. 10 (2006) 387-393
    • (2006) Curr. Op. Chem. Biol. , vol.10 , pp. 387-393
    • Scheuring, S.1
  • 8
    • 0030780277 scopus 로고    scopus 로고
    • Femtosecond spectroscopy of photosynthetic light harvesting systems
    • Fleming G.R., and van Grondelle R. Femtosecond spectroscopy of photosynthetic light harvesting systems. Curr. Opin. Str. Biol. 7 (1997) 738-748
    • (1997) Curr. Opin. Str. Biol. , vol.7 , pp. 738-748
    • Fleming, G.R.1    van Grondelle, R.2
  • 9
    • 0000220848 scopus 로고    scopus 로고
    • Photosynthetic light-harvesting: reconciling dynamics and structure of purple bacterial LH2 reveals function of photosynthetic unit
    • Sundström V., Pullerits T., and van Grondelle R. Photosynthetic light-harvesting: reconciling dynamics and structure of purple bacterial LH2 reveals function of photosynthetic unit. J. Phys. Chem. B 103 (1999) 2327-2346
    • (1999) J. Phys. Chem. B , vol.103 , pp. 2327-2346
    • Sundström, V.1    Pullerits, T.2    van Grondelle, R.3
  • 11
    • 0008990302 scopus 로고    scopus 로고
    • The mechanism of energy transfer in the antenna of photosynthetic purple bacteria
    • Yang M., Agarwal R., and Fleming G.R. The mechanism of energy transfer in the antenna of photosynthetic purple bacteria. J. Photochem. Photobiol. A-Chem. 142 (2001) 107-119
    • (2001) J. Photochem. Photobiol. A-Chem. , vol.142 , pp. 107-119
    • Yang, M.1    Agarwal, R.2    Fleming, G.R.3
  • 12
    • 0001337010 scopus 로고
    • The pathway, kinetics and thermodynamics of electron transfer in wild type and mutant bacterial reaction centers of purple nonsulfur bacteria
    • Blankenship R.E., Madigan M.T., and Bauer C.E. (Eds), Kluwer Academic Publishers, The Netherlands
    • Woodbury N.W., and Allen J.P. The pathway, kinetics and thermodynamics of electron transfer in wild type and mutant bacterial reaction centers of purple nonsulfur bacteria. In: Blankenship R.E., Madigan M.T., and Bauer C.E. (Eds). Anoxygenic Photosynthetic Bacteria (1995), Kluwer Academic Publishers, The Netherlands 527-557
    • (1995) Anoxygenic Photosynthetic Bacteria , pp. 527-557
    • Woodbury, N.W.1    Allen, J.P.2
  • 13
    • 0001124818 scopus 로고    scopus 로고
    • Photosynthetic bacterial reaction centers
    • Bendall D.S. (Ed), BIOS Scientific Publishers, Oxford, UK
    • Parson W.W. Photosynthetic bacterial reaction centers. In: Bendall D.S. (Ed). Protein Electron Transfer (1996), BIOS Scientific Publishers, Oxford, UK 125-160
    • (1996) Protein Electron Transfer , pp. 125-160
    • Parson, W.W.1
  • 14
    • 0031208887 scopus 로고    scopus 로고
    • Photophysics of photosynthesis: Structure and spectroscopy of reaction centres of purple bacteria
    • Hoff A.J., and Deisenhofer J. Photophysics of photosynthesis: Structure and spectroscopy of reaction centres of purple bacteria. Phys. Rep. 287 (1997) 2-247
    • (1997) Phys. Rep. , vol.287 , pp. 2-247
    • Hoff, A.J.1    Deisenhofer, J.2
  • 15
    • 0034577649 scopus 로고    scopus 로고
    • Reaction centres of purple bacteria
    • Scrutton N.S., and Holzenburg A. (Eds), Kluwer Academic/Plenum Publishers, New York, USA
    • Van Brederode M.E., and Jones M.R. Reaction centres of purple bacteria. In: Scrutton N.S., and Holzenburg A. (Eds). Enzyme-Catalysed Electron and Radical Transfer (2000), Kluwer Academic/Plenum Publishers, New York, USA 621-676
    • (2000) Enzyme-Catalysed Electron and Radical Transfer , pp. 621-676
    • Van Brederode, M.E.1    Jones, M.R.2
  • 17
    • 1242347393 scopus 로고    scopus 로고
    • Proton and electron transfer in the acceptor quinone complex of photosynthetic reaction centers from Rhodobacter sphaeroides
    • Wraight C.A. Proton and electron transfer in the acceptor quinone complex of photosynthetic reaction centers from Rhodobacter sphaeroides. Front. Biosci. 9 (2004) 309-337
    • (2004) Front. Biosci. , vol.9 , pp. 309-337
    • Wraight, C.A.1
  • 18
    • 0016690480 scopus 로고
    • 1 complex in the respiratory chain: proton motive ubiquinone cycle
    • 1 complex in the respiratory chain: proton motive ubiquinone cycle. FEBS Lett. 56 (1975) 1-6
    • (1975) FEBS Lett. , vol.56 , pp. 1-6
    • Mitchell, P.1
  • 19
    • 0017148721 scopus 로고
    • Possible molecular mechanisms of the protonmotive function of cytochrome systems
    • Mitchell P. Possible molecular mechanisms of the protonmotive function of cytochrome systems. J. Theor. Biol. 62 (1976) 327-367
    • (1976) J. Theor. Biol. , vol.62 , pp. 327-367
    • Mitchell, P.1
  • 20
    • 0001104663 scopus 로고
    • The role of the quinone pool in the cyclic electron transfer chain of Rps. sphaeroides: a modified Q-cycle mechanism
    • Crofts A.R., Meinhardt S.W., Jones K.R., and Snozzi M. The role of the quinone pool in the cyclic electron transfer chain of Rps. sphaeroides: a modified Q-cycle mechanism. Biochim. Biophys. Acta 723 (1983) 202-218
    • (1983) Biochim. Biophys. Acta , vol.723 , pp. 202-218
    • Crofts, A.R.1    Meinhardt, S.W.2    Jones, K.R.3    Snozzi, M.4
  • 22
    • 3042767574 scopus 로고    scopus 로고
    • The Q-cycle - a personal perspective
    • Crofts A.R. The Q-cycle - a personal perspective. Photosynth. Res. 80 (2004) 223-243
    • (2004) Photosynth. Res. , vol.80 , pp. 223-243
    • Crofts, A.R.1
  • 23
    • 1942447877 scopus 로고    scopus 로고
    • 1 complex: Function in the context of structure
    • 1 complex: Function in the context of structure. Ann. Rev. Physiol. 66 (2004) 689-733
    • (2004) Ann. Rev. Physiol. , vol.66 , pp. 689-733
    • Crofts, A.R.1
  • 25
    • 0021755973 scopus 로고
    • X-ray structure analysis of a membrane protein complex - electron-density map at 3 Å resolution and a model of the chromophores of the photosynthetic reaction center from Rhodopseudomonas viridis
    • Deisenhofer J., Epp O., Miki K., Huber R., and Michel H. X-ray structure analysis of a membrane protein complex - electron-density map at 3 Å resolution and a model of the chromophores of the photosynthetic reaction center from Rhodopseudomonas viridis. J. Mol. Biol. 180 (1984) 385-398
    • (1984) J. Mol. Biol. , vol.180 , pp. 385-398
    • Deisenhofer, J.1    Epp, O.2    Miki, K.3    Huber, R.4    Michel, H.5
  • 26
    • 0022348605 scopus 로고
    • Structure of the protein subunits in the photosynthetic reaction center of Rhodopseudomonas viridis at 3 Angstrom resolution
    • Deisenhofer J., Epp O., Miki K., Huber R., and Michel H. Structure of the protein subunits in the photosynthetic reaction center of Rhodopseudomonas viridis at 3 Angstrom resolution. Nature 318 (1985) 618-624
    • (1985) Nature , vol.318 , pp. 618-624
    • Deisenhofer, J.1    Epp, O.2    Miki, K.3    Huber, R.4    Michel, H.5
  • 27
    • 0028957690 scopus 로고
    • Crystallographic refinement at 2.3-angstrom resolution and refined model of the photosynthetic reaction center from Rhodopseudomonas viridis
    • Deisenhofer J., Epp O., Sinning I., and Michel H. Crystallographic refinement at 2.3-angstrom resolution and refined model of the photosynthetic reaction center from Rhodopseudomonas viridis. J. Mol. Biol. 246 (1995) 429-457
    • (1995) J. Mol. Biol. , vol.246 , pp. 429-457
    • Deisenhofer, J.1    Epp, O.2    Sinning, I.3    Michel, H.4
  • 28
    • 0000840344 scopus 로고
    • Structural homology of reaction centers from Rhodopseudomonas sphaeroides and Rhodopseudomonas viridis as determined by X-ray diffraction
    • Allen J.P., Feher G., Yeates T.O., Rees D.C., Deisenhofer J., Michel H., and Huber R. Structural homology of reaction centers from Rhodopseudomonas sphaeroides and Rhodopseudomonas viridis as determined by X-ray diffraction. Proc. Natl. Acad. Sci. U. S. A. 83 (1986) 8589-8593
    • (1986) Proc. Natl. Acad. Sci. U. S. A. , vol.83 , pp. 8589-8593
    • Allen, J.P.1    Feher, G.2    Yeates, T.O.3    Rees, D.C.4    Deisenhofer, J.5    Michel, H.6    Huber, R.7
  • 30
    • 0023408258 scopus 로고
    • Structure of the reaction center from Rhodobacter-sphaeroides R-26: the protein subunits
    • Allen J.P., Feher G., Yeates T.O., Komiya H., and Rees D.C. Structure of the reaction center from Rhodobacter-sphaeroides R-26: the protein subunits. Proc. Natl. Acad. Sci. U. S. A. 84 (1987) 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
  • 31
    • 0025784505 scopus 로고
    • Structure of the membrane-bound protein photosynthetic reaction center from Rhodobacter sphaeroides
    • Chang C.-H., El-Kabbani O., Tiede D., Norris J., and Schiffer M. Structure of the membrane-bound protein photosynthetic reaction center from Rhodobacter sphaeroides. Biochemistry 30 (1991) 5352-5360
    • (1991) Biochemistry , vol.30 , pp. 5352-5360
    • Chang, C.-H.1    El-Kabbani, O.2    Tiede, D.3    Norris, J.4    Schiffer, M.5
  • 32
    • 0028774335 scopus 로고
    • Structure of the photosynthetic reaction center from Rhodobacter sphaeroides at 2.65-angstrom resolution - cofactors and protein-cofactor interactions
    • Ermler U., Fritzsch G., Buchanan S.K., and Michel H. Structure of the photosynthetic reaction center from Rhodobacter sphaeroides at 2.65-angstrom resolution - cofactors and protein-cofactor interactions. Structure 2 (1994) 925-936
    • (1994) Structure , vol.2 , pp. 925-936
    • Ermler, U.1    Fritzsch, G.2    Buchanan, S.K.3    Michel, H.4
  • 33
    • 0028210159 scopus 로고
    • Structure and function of the photosynthetic reaction center from Rhodobacter sphaeroides
    • Ermler U., Michel H., and Schiffer M. Structure and function of the photosynthetic reaction center from Rhodobacter sphaeroides. J. Bioenerg. Biomemb. 26 (1994) 5-15
    • (1994) J. Bioenerg. Biomemb. , vol.26 , pp. 5-15
    • Ermler, U.1    Michel, H.2    Schiffer, M.3
  • 34
    • 0034610266 scopus 로고    scopus 로고
    • Crystal structures of photosynthetic reaction centre and high-potential iron-sulfur protein from Thermochromatium tepidum: thermostability and electron transfer
    • Nogi T., Fathir I., Kobayashi M., Nozawa T., and Miki K. Crystal structures of photosynthetic reaction centre and high-potential iron-sulfur protein from Thermochromatium tepidum: thermostability and electron transfer. Proc. Natl. Acad. Sci. USA 97 (2000) 13561-13566
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 13561-13566
    • Nogi, T.1    Fathir, I.2    Kobayashi, M.3    Nozawa, T.4    Miki, K.5
  • 35
    • 0034843272 scopus 로고    scopus 로고
    • Structure of the H subunit of the photosynthetic reaction center from the thermophilic purple sulfur bacterium, Thermochromatium tepidum - implications for the specific binding of the lipid molecule to the membrane protein complex
    • Fathir I., Mori T., Nogi T., Kobayashi M., Miki K., and Nozawa T. Structure of the H subunit of the photosynthetic reaction center from the thermophilic purple sulfur bacterium, Thermochromatium tepidum - implications for the specific binding of the lipid molecule to the membrane protein complex. Eur. J. Biochem. 268 (2001) 2652-2657
    • (2001) Eur. J. Biochem. , vol.268 , pp. 2652-2657
    • Fathir, I.1    Mori, T.2    Nogi, T.3    Kobayashi, M.4    Miki, K.5    Nozawa, T.6
  • 37
    • 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. The crystal structure of the light-harvesting complex II (B800-850) from Rhodospirillum molischianum. Structure 4 (1996) 581-597
    • (1996) Structure , vol.4 , pp. 581-597
    • Koepke, J.1    Hu, X.C.2    Muenke, C.3    Schulten, K.4    Michel, H.5
  • 38
    • 0002249157 scopus 로고
    • Three-dimensional structure of a photosynthetic membrane
    • Miller K.R. Three-dimensional structure of a photosynthetic membrane. Nature 300 (1982) 53-55
    • (1982) Nature , vol.300 , pp. 53-55
    • Miller, K.R.1
  • 39
    • 0000132996 scopus 로고
    • The structure of the photoreceptor unit of Rhodopseudomonas viridis
    • Stark W., Kuhlbrandt W., Wildhaber I., Wehrli E., and Muhlethaler K. The structure of the photoreceptor unit of Rhodopseudomonas viridis. EMBO J. 3 (1984) 777-783
    • (1984) EMBO J. , vol.3 , pp. 777-783
    • Stark, W.1    Kuhlbrandt, W.2    Wildhaber, I.3    Wehrli, E.4    Muhlethaler, K.5
  • 40
    • 0001321802 scopus 로고
    • Stoichiometric model of the photosynthetic unit of Ectothiorhodospira halochloris
    • Engelhardt H., Engel A., and Baumeister W. Stoichiometric model of the photosynthetic unit of Ectothiorhodospira halochloris. Proc. Natl. Acad. Sci. U. S. A. 83 (1986) 8972-8976
    • (1986) Proc. Natl. Acad. Sci. U. S. A. , vol.83 , pp. 8972-8976
    • Engelhardt, H.1    Engel, A.2    Baumeister, W.3
  • 41
    • 0026757848 scopus 로고
    • The light-harvesting core-complex and the B820-subunit from Rhodopseudomonas marina. Part II. Electron microscopic characterisation
    • Meckenstock R.U., Krusche K., Brunisholz R.A., and Zuber H. The light-harvesting core-complex and the B820-subunit from Rhodopseudomonas marina. Part II. Electron microscopic characterisation. FEBS Letts. 311 (1992) 135-138
    • (1992) FEBS Letts. , vol.311 , pp. 135-138
    • Meckenstock, R.U.1    Krusche, K.2    Brunisholz, R.A.3    Zuber, H.4
  • 42
    • 0028346682 scopus 로고
    • Structure of the light harvesting antenna from Rhodospirillum molischianum studied by electron microscopy
    • Boonstra A.F., Germeroth L., and Boekema E.J. Structure of the light harvesting antenna from Rhodospirillum molischianum studied by electron microscopy. Biochim. Biophys. Acta 1184 (1994) 227-234
    • (1994) Biochim. Biophys. Acta , vol.1184 , pp. 227-234
    • Boonstra, A.F.1    Germeroth, L.2    Boekema, E.J.3
  • 43
    • 0028953308 scopus 로고
    • The 8.5 Å projection map of the light-harvesting complex I from Rhodospirillum rubrum reveals a ring composed of 16 subunits
    • Karrasch S., Bullough P.A., and Ghosh R. The 8.5 Å projection map of the light-harvesting complex I from Rhodospirillum rubrum reveals a ring composed of 16 subunits. EMBO J. 14 (1995) 631-638
    • (1995) EMBO J. , vol.14 , pp. 631-638
    • Karrasch, S.1    Bullough, P.A.2    Ghosh, R.3
  • 44
    • 0032475815 scopus 로고    scopus 로고
    • Projection structures of three photosynthetic complexes from Rhodobacter sphaeroides: LH2 at 6 Angstrom LH1 and RC-LH1 at 25 Angstrom
    • Walz T., Jamieson S.J., Bowers C.M., Bullough P.A., and Hunter C.N. Projection structures of three photosynthetic complexes from Rhodobacter sphaeroides: LH2 at 6 Angstrom LH1 and RC-LH1 at 25 Angstrom. J. Mol. Biol. 282 (1998) 833-845
    • (1998) J. Mol. Biol. , vol.282 , pp. 833-845
    • Walz, T.1    Jamieson, S.J.2    Bowers, C.M.3    Bullough, P.A.4    Hunter, C.N.5
  • 45
    • 0032475911 scopus 로고    scopus 로고
    • Are the light-harvesting I complexes from Rhodospirillum rubrum arranged around the reaction centre in a square geometry?
    • Stahlberg H., Dubochet J., Vogel H., and Ghosh R. Are the light-harvesting I complexes from Rhodospirillum rubrum arranged around the reaction centre in a square geometry?. J. Mol. Biol. 282 (1998) 819-831
    • (1998) J. Mol. Biol. , vol.282 , pp. 819-831
    • Stahlberg, H.1    Dubochet, J.2    Vogel, H.3    Ghosh, R.4
  • 46
    • 0036683068 scopus 로고    scopus 로고
    • Projection structure of the photosynthetic reaction centre-antenna complex of Rhodospirillum rubrum at 8.5 Angstrom resolution
    • Jamieson S.J., Wang P.Y., Qian P., Kirkland J.Y., Conroy M.J., Hunter C.N., and Bullough P.A. Projection structure of the photosynthetic reaction centre-antenna complex of Rhodospirillum rubrum at 8.5 Angstrom resolution. EMBO J. 21 (2002) 3927-3935
    • (2002) EMBO J. , vol.21 , pp. 3927-3935
    • Jamieson, S.J.1    Wang, P.Y.2    Qian, P.3    Kirkland, J.Y.4    Conroy, M.J.5    Hunter, C.N.6    Bullough, P.A.7
  • 47
    • 0032478682 scopus 로고    scopus 로고
    • Projection map of the reaction center-light harvesting 1 complex from Rhodopseudomonas viridis at 10 Angstrom resolution
    • Ikeda-Yamasaki I., Odahara T., Mitsuoka K., Fujiyoshi Y., and Murata K. Projection map of the reaction center-light harvesting 1 complex from Rhodopseudomonas viridis at 10 Angstrom resolution. FEBS Letts. 425 (1998) 505-508
    • (1998) FEBS Letts. , vol.425 , pp. 505-508
    • Ikeda-Yamasaki, I.1    Odahara, T.2    Mitsuoka, K.3    Fujiyoshi, Y.4    Murata, K.5
  • 48
    • 0037452675 scopus 로고    scopus 로고
    • Nanodissection and high-resolution imaging of the Rhodopseudomonas viridis photosynthetic core complex in native membranes by AFM
    • Scheuring S., Seguin J., Marco S., Levy D., Robert B., and Rigaud J.L. Nanodissection and high-resolution imaging of the Rhodopseudomonas viridis photosynthetic core complex in native membranes by AFM. Proc. Natl. Acad Sci U. S. A. 100 (2003) 1690-1693
    • (2003) Proc. Natl. Acad Sci U. S. A. , vol.100 , pp. 1690-1693
    • Scheuring, S.1    Seguin, J.2    Marco, S.3    Levy, D.4    Robert, B.5    Rigaud, J.L.6
  • 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
    • Fotiadis D., Qian P., Philippsen A., Bullough P.A., Engel A., and 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. 279 (2004) 2063-2068
    • (2004) J. Biol. Chem. , vol.279 , pp. 2063-2068
    • Fotiadis, D.1    Qian, P.2    Philippsen, A.3    Bullough, P.A.4    Engel, A.5    Hunter, C.N.6
  • 51
    • 28944431668 scopus 로고    scopus 로고
    • Architecture of the native photosynthetic apparatus of Phaeospirillum molischianum
    • Gonçalves R.P., Bernadac A., Sturgis J.N., and Scheuring S. Architecture of the native photosynthetic apparatus of Phaeospirillum molischianum. J. Struct. Biol. 152 (2005) 221-228
    • (2005) J. Struct. Biol. , vol.152 , pp. 221-228
    • Gonçalves, R.P.1    Bernadac, A.2    Sturgis, J.N.3    Scheuring, S.4
  • 53
    • 33645100807 scopus 로고    scopus 로고
    • The photosynthetic apparatus of Rhodopseudomonas palustris: structures and organization
    • Scheuring S., Gonçalves R.P., Prima V., and Sturgis J.N. The photosynthetic apparatus of Rhodopseudomonas palustris: structures and organization. J. Mol. Biol. 358 (2006) 83-96
    • (2006) J. Mol. Biol. , vol.358 , pp. 83-96
    • Scheuring, S.1    Gonçalves, R.P.2    Prima, V.3    Sturgis, J.N.4
  • 54
    • 0021455018 scopus 로고
    • Nucleotide and deduced polypeptide sequences of the photosynthetic reaction center, B870 antenna, and flanking polypeptides from R. capsulata
    • Youvan D.C., Bylina E.J., Alberti M., Begusch H., and Hearst J.E. Nucleotide and deduced polypeptide sequences of the photosynthetic reaction center, B870 antenna, and flanking polypeptides from R. capsulata. Cell 37 (1984) 949-957
    • (1984) Cell , vol.37 , pp. 949-957
    • Youvan, D.C.1    Bylina, E.J.2    Alberti, M.3    Begusch, H.4    Hearst, J.E.5
  • 55
    • 0021978242 scopus 로고
    • Differential expression of photosynthesis genes in R. capsulata results from segmental differences in stability within the polycistronic rxcA transcript
    • Belasco J.G., Beatty J.T., Adams C.W., Vongabain A., and Cohen S.N. Differential expression of photosynthesis genes in R. capsulata results from segmental differences in stability within the polycistronic rxcA transcript. Cell 40 (1985) 171-181
    • (1985) Cell , vol.40 , pp. 171-181
    • Belasco, J.G.1    Beatty, J.T.2    Adams, C.W.3    Vongabain, A.4    Cohen, S.N.5
  • 56
    • 0022973216 scopus 로고
    • Regulation of expression of genes for light-harvesting antenna proteins LH-I and LH-II - reaction center polypeptides RC-L, RC-M, and RC-H - and enzymes of bacteriochlorophyll and carotenoid biosynthesis in Rhodobacter capsulatus by light and oxygen
    • Zhu Y.S., and Hearst J.E. Regulation of expression of genes for light-harvesting antenna proteins LH-I and LH-II - reaction center polypeptides RC-L, RC-M, and RC-H - and enzymes of bacteriochlorophyll and carotenoid biosynthesis in Rhodobacter capsulatus by light and oxygen. Proc. Natl. Acad. Sci. U. S. A. 83 (1986) 7613-7617
    • (1986) Proc. Natl. Acad. Sci. U. S. A. , vol.83 , pp. 7613-7617
    • Zhu, Y.S.1    Hearst, J.E.2
  • 57
    • 0011209271 scopus 로고
    • The puf operon region of Rhodobacter sphaeroides
    • Donohue T.J., Kiley P.J., and Kaplan S. The puf operon region of Rhodobacter sphaeroides. Photosynth. Res. 19 (1988) 39-61
    • (1988) Photosynth. Res. , vol.19 , pp. 39-61
    • Donohue, T.J.1    Kiley, P.J.2    Kaplan, S.3
  • 58
    • 0024971623 scopus 로고
    • Transcriptional analysis of puf operon expression in Rhodobacter sphaeroides 2.4.1. and an intercistronic transcription terminator mutant
    • Lee J.K., DeHoff B.S., Donohue T.J., Gumport R.J., and Kaplan S. Transcriptional analysis of puf operon expression in Rhodobacter sphaeroides 2.4.1. and an intercistronic transcription terminator mutant. J. Biol. Chem. 264 (1989) 19354-19365
    • (1989) J. Biol. Chem. , vol.264 , pp. 19354-19365
    • Lee, J.K.1    DeHoff, B.S.2    Donohue, T.J.3    Gumport, R.J.4    Kaplan, S.5
  • 59
    • 0024197376 scopus 로고
    • Pleiotropic effects of localised Rhodobacter capsulatus puf operon deletions on production of light-absorbing pigment-protein complexes
    • Klug G., and Cohen S.N. Pleiotropic effects of localised Rhodobacter capsulatus puf operon deletions on production of light-absorbing pigment-protein complexes. J. Bact. 170 (1988) 5814-5821
    • (1988) J. Bact. , vol.170 , pp. 5814-5821
    • Klug, G.1    Cohen, S.N.2
  • 60
    • 0025139203 scopus 로고
    • Complementation of a reaction center deficient Rhodobacter sphaeroides pufLMX deletion strain in trans with pufBALM does not restore the photosynthesis-positive phenotype
    • Farchaus J.W., Gruenberg H., and Oesterhelt D. Complementation of a reaction center deficient Rhodobacter sphaeroides pufLMX deletion strain in trans with pufBALM does not restore the photosynthesis-positive phenotype. J. Bact. 172 (1990) 977-985
    • (1990) J. Bact. , vol.172 , pp. 977-985
    • Farchaus, J.W.1    Gruenberg, H.2    Oesterhelt, D.3
  • 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. Pleiotropic effects of pufX gene deletion on the structure and function of the photosynthetic apparatus of Rhodobacter capsulatus. Biochim. Biophys. Acta 1100 (1992) 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
    • 0026691439 scopus 로고
    • Studies on the expression of PufX polypeptide and its requirement for photoheterotrophic growth in Rhodobacter sphaeroides
    • Farchaus J.W., Barz W.P., Gruenberg H., and Oesterhelt D. Studies on the expression of PufX polypeptide and its requirement for photoheterotrophic growth in Rhodobacter sphaeroides. EMBO J. 11 (1992) 2779-2788
    • (1992) EMBO J. , vol.11 , pp. 2779-2788
    • Farchaus, J.W.1    Barz, W.P.2    Gruenberg, H.3    Oesterhelt, D.4
  • 63
    • 33751202658 scopus 로고    scopus 로고
    • Development of the bacterial photosynthetic apparatus
    • Tavano C.L., and Donohue T.J. Development of the bacterial photosynthetic apparatus. Curr. Op. Microbiol. 9 (2006) 625-631
    • (2006) Curr. Op. Microbiol. , vol.9 , pp. 625-631
    • Tavano, C.L.1    Donohue, T.J.2
  • 64
    • 0035873776 scopus 로고    scopus 로고
    • Role of the core region of the PufX protein in inhibition of reconstitution of the core light-harvesting complexes of Rhodobacter sphaeroides and Rhodobacter capsulatus
    • Parkes-Loach P.S., Law C.J., Recchia P.A., Kehoe J., Nehrlich S., Chen J., and Loach P.A. Role of the core region of the PufX protein in inhibition of reconstitution of the core light-harvesting complexes of Rhodobacter sphaeroides and Rhodobacter capsulatus. Biochemistry 40 (2001) 5593-5601
    • (2001) Biochemistry , vol.40 , pp. 5593-5601
    • Parkes-Loach, P.S.1    Law, C.J.2    Recchia, P.A.3    Kehoe, J.4    Nehrlich, S.5    Chen, J.6    Loach, P.A.7
  • 65
    • 0031936540 scopus 로고    scopus 로고
    • Demonstration of the key role played by the PufX protein in the functional and structural organization of native and hybrid bacterial photosynthetic core complexes
    • Fulcher T.K., Beatty J.T., and Jones M.R. Demonstration of the key role played by the PufX protein in the functional and structural organization of native and hybrid bacterial photosynthetic core complexes. J. Bact. 180 (1998) 642-646
    • (1998) J. Bact. , vol.180 , pp. 642-646
    • Fulcher, T.K.1    Beatty, J.T.2    Jones, M.R.3
  • 66
    • 0442298612 scopus 로고    scopus 로고
    • Phylogenetic distribution of unusual triheme to tetraheme cytochrome subunit in the reaction center complex of purple photosynthetic bacteria
    • Tsukatani Y., Matsuura K., Masuda S., Shimada K., Hiraishi A., and Nagashima K.V.P. Phylogenetic distribution of unusual triheme to tetraheme cytochrome subunit in the reaction center complex of purple photosynthetic bacteria. Photosynth. Res. 79 (2004) 83-91
    • (2004) Photosynth. Res. , vol.79 , pp. 83-91
    • Tsukatani, Y.1    Matsuura, K.2    Masuda, S.3    Shimada, K.4    Hiraishi, A.5    Nagashima, K.V.P.6
  • 67
    • 0032483080 scopus 로고    scopus 로고
    • 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
    • Recchia P.A., Davis C.M., Lilburn T.G., Beatty J.T., Parkes-Loach P.S., Hunter C.N., and 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 37 (1998) 11055-11063
    • (1998) Biochemistry , vol.37 , 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
  • 68
    • 0032494286 scopus 로고    scopus 로고
    • The LH1-RC core complex of Rhodobacter sphaeroides: interaction between components, time-dependent assembly, and topology of the PufX protein
    • Pugh R.J., McGlynn P., Jones M.R., and Hunter C.N. The LH1-RC core complex of Rhodobacter sphaeroides: interaction between components, time-dependent assembly, and topology of the PufX protein. Biochim. Biophys. Acta-Bioenerg. 1366 (1998) 301-316
    • (1998) Biochim. Biophys. Acta-Bioenerg. , vol.1366 , pp. 301-316
    • Pugh, R.J.1    McGlynn, P.2    Jones, M.R.3    Hunter, C.N.4
  • 69
    • 33748284893 scopus 로고    scopus 로고
    • Functional and structural analysis of the photosynthetic apparatus of Rhodobacter veldkampii
    • Gubellini F., Francia F., Busselez J., Venturoli G., and Lévy D. Functional and structural analysis of the photosynthetic apparatus of Rhodobacter veldkampii. Biochemistry 45 (2006) 10512-10520
    • (2006) Biochemistry , vol.45 , pp. 10512-10520
    • Gubellini, F.1    Francia, F.2    Busselez, J.3    Venturoli, G.4    Lévy, D.5
  • 70
    • 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. The reaction center-LH1 antenna complex of Rhodobacter sphaeroides contains one PufX molecule which is involved in dimerization of this complex. Biochemistry 38 (1999) 6834-6845
    • (1999) Biochemistry , vol.38 , pp. 6834-6845
    • Francia, F.1    Wang, J.2    Venturoli, G.3    Melandri, B.A.4    Barz, W.P.5    Oesterhelt, D.6
  • 71
    • 25444464841 scopus 로고    scopus 로고
    • Characterization of a highly purified, fully active, crystallizable RC-LH1-PufX core complex from Rhodobacter sphaeroides
    • Abresch E.C., Axelrod H.L.A., Beatty J.T., Johnson J.A., Nechushtai R., and Paddock M.L. Characterization of a highly purified, fully active, crystallizable RC-LH1-PufX core complex from Rhodobacter sphaeroides. Photosynth. Res. 86 (2005) 61-70
    • (2005) Photosynth. Res. , vol.86 , pp. 61-70
    • Abresch, E.C.1    Axelrod, H.L.A.2    Beatty, J.T.3    Johnson, J.A.4    Nechushtai, R.5    Paddock, M.L.6
  • 72
    • 27644567357 scopus 로고    scopus 로고
    • The PufX protein of Rhodobacter capsulatus affects the properties of bacteriochlorophyll a and carotenoid pigments of light-harvesting complex 1
    • Aklujkar M., and Beatty J.T. The PufX protein of Rhodobacter capsulatus affects the properties of bacteriochlorophyll a and carotenoid pigments of light-harvesting complex 1. Arch. Biochem. Biophys. 443 (2005) 21-32
    • (2005) Arch. Biochem. Biophys. , vol.443 , pp. 21-32
    • Aklujkar, M.1    Beatty, J.T.2
  • 74
    • 33745029738 scopus 로고    scopus 로고
    • Investigation of Rhodobacter capsulatus PufX interactions in the core complex of the photosynthetic apparatus
    • Aklujkar M., and Beatty J.T. Investigation of Rhodobacter capsulatus PufX interactions in the core complex of the photosynthetic apparatus. Photosynth. Res. 88 (2006) 159-171
    • (2006) Photosynth. Res. , vol.88 , pp. 159-171
    • Aklujkar, M.1    Beatty, J.T.2
  • 75
    • 0037705407 scopus 로고    scopus 로고
    • Interaction of bacteriochlorophyll with the LH1 and PufX polypeptides of photosynthetic bacteria: use of chemically synthesized analogs and covalently attached fluorescent probes
    • Law C.J., Chen J., Parkes-Loach P.S., and Loach P.A. Interaction of bacteriochlorophyll with the LH1 and PufX polypeptides of photosynthetic bacteria: use of chemically synthesized analogs and covalently attached fluorescent probes. Photosynth. Res. 75 (2003) 193-210
    • (2003) Photosynth. Res. , vol.75 , pp. 193-210
    • Law, C.J.1    Chen, J.2    Parkes-Loach, P.S.3    Loach, P.A.4
  • 76
    • 0033514311 scopus 로고    scopus 로고
    • TOXCAT: a measure of transmembrane helix association in a biological membrane
    • Russ W.P., and Engelman D.M. TOXCAT: a measure of transmembrane helix association in a biological membrane. Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 863-868
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 863-868
    • Russ, W.P.1    Engelman, D.M.2
  • 77
    • 0002405138 scopus 로고
    • Structure, molecular organization, and biosynthesis of membrane of purple bacteria
    • Blankenship R.E., Madigan M.T., and Bauer C.E. (Eds), Kluwer Academic Publishers, The Netherlands
    • Drews G., and Golecki J.R. Structure, molecular organization, and biosynthesis of membrane of purple bacteria. In: Blankenship R.E., Madigan M.T., and Bauer C.E. (Eds). Anoxygenic Photosynthetic Bacteria (1995), Kluwer Academic Publishers, The Netherlands 231-257
    • (1995) Anoxygenic Photosynthetic Bacteria , pp. 231-257
    • Drews, G.1    Golecki, J.R.2
  • 78
    • 0242603733 scopus 로고
    • Chromatophores of Rhodospirillum rubrum
    • Pardee A.B., Schachman H.K., and Stanier R.Y. Chromatophores of Rhodospirillum rubrum. Nature 169 (1952) 282-283
    • (1952) Nature , vol.169 , pp. 282-283
    • Pardee, A.B.1    Schachman, H.K.2    Stanier, R.Y.3
  • 79
    • 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. Oligomerization states and associations of light-harvesting pigment protein complexes of Rhodobacter sphaeroides as analyzed by lithium dodecyl-sulfate polyacrylamide-gel electrophoresis. Biochemistry 27 (1988) 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
  • 80
    • 0025734781 scopus 로고
    • Ultrastructural and electron spectroscopic analyses of cyanobacteria and bacteria
    • Golecki J.R., and Heinrich U.R. Ultrastructural and electron spectroscopic analyses of cyanobacteria and bacteria. J. Microsc. 162 (1991) 147-154
    • (1991) J. Microsc. , vol.162 , pp. 147-154
    • Golecki, J.R.1    Heinrich, U.R.2
  • 81
    • 0025967181 scopus 로고
    • The architecture of unusual membrane tubes in the B800-850 light-harvesting bacteriochlorophyll-deficient mutant 19 of Rhodobacter sphaeroides
    • Golecki J.R., Ventura S., and Oelze J. The architecture of unusual membrane tubes in the B800-850 light-harvesting bacteriochlorophyll-deficient mutant 19 of Rhodobacter sphaeroides. FEMS Micro. Letts. 77 (1991) 335-340
    • (1991) FEMS Micro. Letts. , vol.77 , pp. 335-340
    • Golecki, J.R.1    Ventura, S.2    Oelze, J.3
  • 82
    • 0026741627 scopus 로고
    • Construction and characterisation of a mutant of Rhodobacter sphaeroides with the reaction centre as the sole pigment-protein complex
    • Jones M.R., Visschers R.W., Van Grondelle R., and Hunter C.N. Construction and characterisation of a mutant of Rhodobacter sphaeroides with the reaction centre as the sole pigment-protein complex. Biochemistry 31 (1992) 4458-4465
    • (1992) Biochemistry , vol.31 , pp. 4458-4465
    • Jones, M.R.1    Visschers, R.W.2    Van Grondelle, R.3    Hunter, C.N.4
  • 83
    • 0027966016 scopus 로고
    • Organization of electron-transfer components in Rhodobacter sphaeroides forma sp. denitrificans whole cells
    • Sabaty M., Jappé J., Olive J., and Verméglio A. Organization of electron-transfer components in Rhodobacter sphaeroides forma sp. denitrificans whole cells. Biochim. Biophys. Acta 1187 (1994) 313-323
    • (1994) Biochim. Biophys. Acta , vol.1187 , pp. 313-323
    • Sabaty, M.1    Jappé, J.2    Olive, J.3    Verméglio, A.4
  • 84
    • 0033081638 scopus 로고    scopus 로고
    • Supramolecular organization of the photosynthetic apparatus of Rhodobacter sphaeroides
    • Jungas C., Ranck J.L., Rigaud J.L., Joliot P., and Verméglio A. Supramolecular organization of the photosynthetic apparatus of Rhodobacter sphaeroides. EMBO J. 18 (1999) 534-542
    • (1999) EMBO J. , vol.18 , pp. 534-542
    • Jungas, C.1    Ranck, J.L.2    Rigaud, J.L.3    Joliot, P.4    Verméglio, A.5
  • 85
    • 0037047004 scopus 로고    scopus 로고
    • Isolation, size estimates, and spectral heterogeneity of an oligomeric series of light-harvesting 1 complexes from Rhodobacter sphaeroides
    • Westerhuis W.H., Sturgis J.N., Ratcliffe E.C., Hunter C.N., and Niederman R.A. Isolation, size estimates, and spectral heterogeneity of an oligomeric series of light-harvesting 1 complexes from Rhodobacter sphaeroides. Biochemistry 41 (2002) 8698-8707
    • (2002) Biochemistry , vol.41 , pp. 8698-8707
    • Westerhuis, W.H.1    Sturgis, J.N.2    Ratcliffe, E.C.3    Hunter, C.N.4    Niederman, R.A.5
  • 86
    • 1842510034 scopus 로고    scopus 로고
    • Molecular architecture of photosynthetic membranes in Rhodobacter sphaeroides: the role of PufX
    • Siebert C.A., Qian P., Fotiadis D., Engel A., Hunter C.N., and Bullough P.A. Molecular architecture of photosynthetic membranes in Rhodobacter sphaeroides: the role of PufX. EMBO J. 23 (2004) 690-700
    • (2004) EMBO J. , vol.23 , pp. 690-700
    • Siebert, C.A.1    Qian, P.2    Fotiadis, D.3    Engel, A.4    Hunter, C.N.5    Bullough, P.A.6
  • 92
    • 84989685272 scopus 로고
    • Altered spectral properties of the B875 light-harvesting pigment-protein complex in a Rhodobacter-sphaeroides mutant lacking PufX
    • Westerhuis W.H.J., Farchaus J.W., and Niederman R.A. Altered spectral properties of the B875 light-harvesting pigment-protein complex in a Rhodobacter-sphaeroides mutant lacking PufX. Photochem. Photobiol. 58 (1993) 460-463
    • (1993) Photochem. Photobiol. , vol.58 , pp. 460-463
    • Westerhuis, W.H.J.1    Farchaus, J.W.2    Niederman, R.A.3
  • 93
    • 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
    • Joliot P., Joliot A., and Verméglio A. 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-Bioenerg. 1706 (2005) 204-214
    • (2005) Biochim. Biophys. Acta-Bioenerg. , vol.1706 , pp. 204-214
    • Joliot, P.1    Joliot, A.2    Verméglio, A.3
  • 94
    • 20344374627 scopus 로고    scopus 로고
    • The 8.5 angstrom projection structure of the core RC-LH1-PufX dimer of Rhodobacter sphaeroides
    • Qian P., Hunter C.N., and Bullough P.A. The 8.5 angstrom projection structure of the core RC-LH1-PufX dimer of Rhodobacter sphaeroides. J. Mol. Biol. 349 (2005) 948-960
    • (2005) J. Mol. Biol. , vol.349 , pp. 948-960
    • Qian, P.1    Hunter, C.N.2    Bullough, P.A.3
  • 95
    • 0942287196 scopus 로고    scopus 로고
    • Structural role of PufX in the dimerization of the photosynthetic core complex of Rhodobacter sphaeroides
    • Scheuring S., Francia F., Busselez J., Melandri B.A., Rigaud J.L., and Lévy D. Structural role of PufX in the dimerization of the photosynthetic core complex of Rhodobacter sphaeroides. J. Biol. Chem. 279 (2004) 3620-3626
    • (2004) J. Biol. Chem. , vol.279 , pp. 3620-3626
    • Scheuring, S.1    Francia, F.2    Busselez, J.3    Melandri, B.A.4    Rigaud, J.L.5    Lévy, D.6
  • 96
    • 37349003143 scopus 로고    scopus 로고
    • On the effects of PufX on the absorption properties of the light-harvesting complexes of Rhodobacter sphaeroides
    • Geyer T. On the effects of PufX on the absorption properties of the light-harvesting complexes of Rhodobacter sphaeroides. Biophys. J. 93 (2007) 4374-4381
    • (2007) Biophys. J. , vol.93 , pp. 4374-4381
    • Geyer, T.1
  • 98
    • 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. Structure of the dimeric PufX-containing core complex of Rhodobacter blasticus by in situ atomic force microscopy. J. Biol. Chem. 280 (2005) 1426-1431
    • (2005) J. Biol. Chem. , vol.280 , pp. 1426-1431
    • Scheuring, S.1    Busselez, J.2    Lévy, D.3
  • 99
    • 36749102634 scopus 로고    scopus 로고
    • Structural basis for the PufX-mediated dimerization of bacterial photosynthetic core complexes
    • Busselez J., Cottevieille M., Cuniasse P., Gubellini F., Boisset N., and Lévy D. Structural basis for the PufX-mediated dimerization of bacterial photosynthetic core complexes. Structure 15 (2007) 1674-1683
    • (2007) Structure , vol.15 , pp. 1674-1683
    • Busselez, J.1    Cottevieille, M.2    Cuniasse, P.3    Gubellini, F.4    Boisset, N.5    Lévy, D.6
  • 100
    • 0034711953 scopus 로고    scopus 로고
    • The GxxxG motif: a framework for transmembrane helix-helix association
    • Russ W.P., and Engelman D.M. The GxxxG motif: a framework for transmembrane helix-helix association. J. Mol. Biol. 296 (2000) 911-919
    • (2000) J. Mol. Biol. , vol.296 , pp. 911-919
    • Russ, W.P.1    Engelman, D.M.2
  • 102
    • 0022346923 scopus 로고
    • Isolation, characterization, and comparison of a ubiquitous pigment-protein complex consisting of a reaction center and light-harvesting bacteriochlorophyll proteins present in purple photosynthetic bacteria
    • Ueda T., Morimoto Y., Sato M., Kakuno T., Yamashita J., and Horio T. Isolation, characterization, and comparison of a ubiquitous pigment-protein complex consisting of a reaction center and light-harvesting bacteriochlorophyll proteins present in purple photosynthetic bacteria. J. Biochem. 98 (1985) 1487-1498
    • (1985) J. Biochem. , vol.98 , pp. 1487-1498
    • Ueda, T.1    Morimoto, Y.2    Sato, M.3    Kakuno, T.4    Yamashita, J.5    Horio, T.6
  • 103
    • 0000027407 scopus 로고
    • The size of the photosynthetic unit in purple bacteria
    • Francke C., and Amesz J. The size of the photosynthetic unit in purple bacteria. Photosynth. Res. 46 (1995) 347-352
    • (1995) Photosynth. Res. , vol.46 , pp. 347-352
    • Francke, C.1    Amesz, J.2
  • 104
    • 0028972070 scopus 로고
    • Role of PufX protein in photosynthetic growth of Rhodobacter sphaeroides. 1. PufX is required for efficient light driven electron-transfer and photophosphorylation under anaerobic conditions
    • Barz W.P., Francia F., Venturoli G., Melandri B.A., Verméglio A., and Oesterhelt D. Role of PufX protein in photosynthetic growth of Rhodobacter sphaeroides. 1. PufX is required for efficient light driven electron-transfer and photophosphorylation under anaerobic conditions. Biochemistry 34 (1995) 15235-15247
    • (1995) Biochemistry , vol.34 , pp. 15235-15247
    • Barz, W.P.1    Francia, F.2    Venturoli, G.3    Melandri, B.A.4    Verméglio, A.5    Oesterhelt, D.6
  • 106
    • 0028101094 scopus 로고
    • The Rhodobacter sphaeroides PufX protein is not required for photosynthetic competence in the absence of a light-harvesting system
    • McGlynn P., Hunter C.N., and Jones M.R. The Rhodobacter sphaeroides PufX protein is not required for photosynthetic competence in the absence of a light-harvesting system. FEBS Letts. 349 (1994) 349-353
    • (1994) FEBS Letts. , vol.349 , pp. 349-353
    • McGlynn, P.1    Hunter, C.N.2    Jones, M.R.3
  • 107
    • 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
    • Bahatyrova S., Frese R.N., van der Werf K.O., Otto C., Hunter C.N., and Olsen J.D. Flexibility and size heterogeneity of the LH1 light harvesting complex revealed by atomic force microscopy - functional significance for bacterial photosynthesis. J. Biol. Chem. 279 (2004) 21327-21333
    • (2004) J. Biol. Chem. , vol.279 , 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
  • 108
    • 0026679894 scopus 로고
    • Suppressor mutants of the photosynthetically incompetent PufX deletion mutant Rhodobacter capsulatus {up triangle, open}RC6(pTL2)
    • Lilburn T.G., and Beatty J.T. Suppressor mutants of the photosynthetically incompetent PufX deletion mutant Rhodobacter capsulatus {up triangle, open}RC6(pTL2). FEMS Micro. Letts. 100 (1992) 155-159
    • (1992) FEMS Micro. Letts. , vol.100 , pp. 155-159
    • Lilburn, T.G.1    Beatty, J.T.2
  • 109
    • 29144509559 scopus 로고    scopus 로고
    • The assembly and organisation of photosynthetic membranes in Rhodobacter sphaeroides
    • Hunter C.N., Tucker J.D., and Niederman R.A. The assembly and organisation of photosynthetic membranes in Rhodobacter sphaeroides. Photochem. Photobiol. Sci. 4 (2005) 1023-1027
    • (2005) Photochem. Photobiol. Sci. , vol.4 , pp. 1023-1027
    • Hunter, C.N.1    Tucker, J.D.2    Niederman, R.A.3
  • 111
    • 33746715610 scopus 로고    scopus 로고
    • Reconstruction of a kinetic model of the chromatophore vesicles from Rhodobacter sphaeroides
    • Geyer T., and Helms V. Reconstruction of a kinetic model of the chromatophore vesicles from Rhodobacter sphaeroides. Biophys. J. 91 (2006) 927-937
    • (2006) Biophys. J. , vol.91 , pp. 927-937
    • Geyer, T.1    Helms, V.2
  • 112
    • 35649018226 scopus 로고    scopus 로고
    • Atomic-level structural and functional model of a bacterial photosynthetic membrane vesicle
    • Sener M.K., Olsen J.D., Hunter C.N., and Schulten K. Atomic-level structural and functional model of a bacterial photosynthetic membrane vesicle. Proc. Natl. Acad. Sci. U. S. A. 104 (2007) 15723-15728
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 15723-15728
    • Sener, M.K.1    Olsen, J.D.2    Hunter, C.N.3    Schulten, K.4
  • 113
    • 0027933467 scopus 로고
    • Photosynthetic deficiency of a Pufx deletion mutant of Rhodobacter-sphaeroides is suppressed by point mutations in the light-harvesting complex genes pufb or pufa
    • Barz W.P., and Oesterhelt D. Photosynthetic deficiency of a Pufx deletion mutant of Rhodobacter-sphaeroides is suppressed by point mutations in the light-harvesting complex genes pufb or pufa. Biochemistry 33 (1994) 9741-9752
    • (1994) Biochemistry , vol.33 , pp. 9741-9752
    • Barz, W.P.1    Oesterhelt, D.2
  • 114
    • 0029091333 scopus 로고
    • Mutation of the Ser2 codon of the light-harvesting B870 alpha-polypeptide of Rhodobacter capsulatus partially suppresses the PufX phenotype
    • Lilburn T.G., Prince R.C., and Beatty J.T. Mutation of the Ser2 codon of the light-harvesting B870 alpha-polypeptide of Rhodobacter capsulatus partially suppresses the PufX phenotype. J. Bact. 177 (1995) 4593-4600
    • (1995) J. Bact. , vol.177 , pp. 4593-4600
    • Lilburn, T.G.1    Prince, R.C.2    Beatty, J.T.3
  • 115
    • 0030062095 scopus 로고    scopus 로고
    • Consequences for the organization of reaction center-light harvesting antenna 1 (LH1) core complexes of Rhodobacter sphaeroides arising from deletion of amino acid residues from the C terminus of the LH1 alpha polypeptide
    • McGlynn P., Westerhuis W.H.J., Jones M.R., and Hunter C.N. Consequences for the organization of reaction center-light harvesting antenna 1 (LH1) core complexes of Rhodobacter sphaeroides arising from deletion of amino acid residues from the C terminus of the LH1 alpha polypeptide. J Biol. Chem. 271 (1996) 3285-3292
    • (1996) J Biol. Chem. , vol.271 , pp. 3285-3292
    • McGlynn, P.1    Westerhuis, W.H.J.2    Jones, M.R.3    Hunter, C.N.4
  • 116
    • 0027486701 scopus 로고
    • Direct energy transfer from the peripheral LH2 antenna to the reaction centre in a mutant of Rhodobacter sphaeroides that lacks the core LH1 antenna
    • Hess S., Visscher K., Ulander J., Pullerits T., Jones M.R., Hunter C.N., and Sundstrom V. Direct energy transfer from the peripheral LH2 antenna to the reaction centre in a mutant of Rhodobacter sphaeroides that lacks the core LH1 antenna. Biochemistry 32 (1993) 10314-10322
    • (1993) Biochemistry , vol.32 , pp. 10314-10322
    • Hess, S.1    Visscher, K.2    Ulander, J.3    Pullerits, T.4    Jones, M.R.5    Hunter, C.N.6    Sundstrom, V.7
  • 118
    • 0037055974 scopus 로고    scopus 로고
    • Supramolecular organisation of the photosynthetic chain in anoxygenic bacteria
    • Verméglio A., and Joliot P. Supramolecular organisation of the photosynthetic chain in anoxygenic bacteria. Biochim. Biophys. Acta-Bioenerg. 1555 (2002) 60-64
    • (2002) Biochim. Biophys. Acta-Bioenerg. , vol.1555 , pp. 60-64
    • Verméglio, A.1    Joliot, P.2
  • 119
    • 34250095040 scopus 로고
    • The role of auxiliary oxidants in maintaining redox balance during phototrophic growth of Rhodobacter capsulatus on propionate or butyrate
    • Richardson D.J., King G.F., Kelly D.J., McEwan A.G., Ferguson S.J., and Jackson J.B. The role of auxiliary oxidants in maintaining redox balance during phototrophic growth of Rhodobacter capsulatus on propionate or butyrate. Arch. Micro. 150 (1988) 131-137
    • (1988) Arch. Micro. , vol.150 , pp. 131-137
    • Richardson, D.J.1    King, G.F.2    Kelly, D.J.3    McEwan, A.G.4    Ferguson, S.J.5    Jackson, J.B.6
  • 120
    • 0025283445 scopus 로고
    • In vivo redox poising of the cyclic electron transport system of Rhodobacter capsulatus and the effects of the auxiliary oxidants, nitrate, nitrous oxide and trimethylamine N-oxide, as revealed by multiple short flash excitation
    • Jones M.R., Richardson D.J., McEwan A.G., Ferguson S.J., and Jackson J.B. In vivo redox poising of the cyclic electron transport system of Rhodobacter capsulatus and the effects of the auxiliary oxidants, nitrate, nitrous oxide and trimethylamine N-oxide, as revealed by multiple short flash excitation. Biochim. Biophys. Acta 1017 (1990) 209-216
    • (1990) Biochim. Biophys. Acta , vol.1017 , pp. 209-216
    • Jones, M.R.1    Richardson, D.J.2    McEwan, A.G.3    Ferguson, S.J.4    Jackson, J.B.5
  • 121
    • 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
    • Francia F., Wang J., Zischka H., Venturoli G., and Oesterhelt D. 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 (2002) 1877-1885
    • (2002) Eur. J. Biochem. , vol.269 , pp. 1877-1885
    • Francia, F.1    Wang, J.2    Zischka, H.3    Venturoli, G.4    Oesterhelt, D.5
  • 122
    • 28644449137 scopus 로고    scopus 로고
    • Putative novel photosynthetic reaction centre organizations in marine aerobic anoxygenic photosynthetic bacteria: insights from metagenomics and environmental genomics
    • Yutin N., and Béjà O. Putative novel photosynthetic reaction centre organizations in marine aerobic anoxygenic photosynthetic bacteria: insights from metagenomics and environmental genomics. Environ. Microbiol. 7 (2005) 2027-2033
    • (2005) Environ. Microbiol. , vol.7 , pp. 2027-2033
    • Yutin, N.1    Béjà, O.2
  • 125
    • 28644435670 scopus 로고    scopus 로고
    • Aerobic anoxygenic photosynthesis genes and operons in uncultured bacteria in the Delaware River
    • Waidner L.A., and Kirchman D.L. Aerobic anoxygenic photosynthesis genes and operons in uncultured bacteria in the Delaware River. Environ. Microbiol. 7 (2005) 1896-1908
    • (2005) Environ. Microbiol. , vol.7 , pp. 1896-1908
    • Waidner, L.A.1    Kirchman, D.L.2
  • 126
    • 0037472747 scopus 로고    scopus 로고
    • Sequence analysis reveals new membrane anchor of reaction centre-bound cytochromes possibly related to PufX
    • Hucke O., Schiltz E., Drews G., and Labahn A. Sequence analysis reveals new membrane anchor of reaction centre-bound cytochromes possibly related to PufX. FEBS Letts. 535 (2003) 166-170
    • (2003) FEBS Letts. , vol.535 , pp. 166-170
    • Hucke, O.1    Schiltz, E.2    Drews, G.3    Labahn, A.4
  • 127
    • 0023220102 scopus 로고
    • The cytochrome subunit of the photosynthetic reaction center from Rhodopseudomonas viridis is a lipoprotein
    • Weyer K.A., Schafer W., Lottspeich F., and Michel H. The cytochrome subunit of the photosynthetic reaction center from Rhodopseudomonas viridis is a lipoprotein. Biochemistry 26 (1987) 2909-2914
    • (1987) Biochemistry , vol.26 , pp. 2909-2914
    • Weyer, K.A.1    Schafer, W.2    Lottspeich, F.3    Michel, H.4
  • 128
    • 0346414462 scopus 로고    scopus 로고
    • Structure of the puf operon of the obligately aerobic, bacteriochlorophyll a-containing bacterium Roseobacter denitrificans OCh114 and its expression in a Rhodobacter capsulatus puf puc deletion mutant
    • Kortlüke C., Breese K., Gad'on N., Labahn A., and Drews G. Structure of the puf operon of the obligately aerobic, bacteriochlorophyll a-containing bacterium Roseobacter denitrificans OCh114 and its expression in a Rhodobacter capsulatus puf puc deletion mutant. J. Bact. 179 (1997) 5247-5258
    • (1997) J. Bact. , vol.179 , pp. 5247-5258
    • Kortlüke, C.1    Breese, K.2    Gad'on, N.3    Labahn, A.4    Drews, G.5
  • 129
    • 0000057585 scopus 로고
    • Evolutionary relationships between reaction center complexes with and without cytochrome c subunits in purple bacteria
    • Baltscheffsky M. (Ed), Kluwer Academic Publishers, The Netherlands
    • Matsuura K., and Shimada K. Evolutionary relationships between reaction center complexes with and without cytochrome c subunits in purple bacteria. In: Baltscheffsky M. (Ed). Current Research in Photosynthesis vol. I (1990), Kluwer Academic Publishers, The Netherlands 193-196
    • (1990) Current Research in Photosynthesis , vol.I , pp. 193-196
    • Matsuura, K.1    Shimada, K.2
  • 131
    • 17844409565 scopus 로고    scopus 로고
    • The puhE gene of Rhodobacter capsulatus is needed for optimal transition from aerobic to photosynthetic growth and encodes a putative negative modulator of bacteriochlorophyll production
    • Aklujkar M., Prince R.C., and Beatty J.T. The puhE gene of Rhodobacter capsulatus is needed for optimal transition from aerobic to photosynthetic growth and encodes a putative negative modulator of bacteriochlorophyll production. Arch. Biochem. Biophys. 437 (2005) 186-198
    • (2005) Arch. Biochem. Biophys. , vol.437 , pp. 186-198
    • Aklujkar, M.1    Prince, R.C.2    Beatty, J.T.3
  • 132
    • 14544293950 scopus 로고    scopus 로고
    • The PuhB protein of Rhodobacter capsulatus functions in photosynthetic reaction center assembly with a secondary effect on light-harvesting complex 1
    • Aklujkar M., Prince R.C., and Beatty J.T. The PuhB protein of Rhodobacter capsulatus functions in photosynthetic reaction center assembly with a secondary effect on light-harvesting complex 1. J. Bact. 187 (2005) 1334-1343
    • (2005) J. Bact. , vol.187 , pp. 1334-1343
    • Aklujkar, M.1    Prince, R.C.2    Beatty, J.T.3
  • 133
    • 33748888356 scopus 로고    scopus 로고
    • The photosynthetic deficiency due to puhC gene deletion in Rhodobacter capsulatus suggests a PuhC protein-dependent process of RC/LH1/PufX complex reorganization
    • Aklujkar M., Prince R.C., and Beatty J.T. The photosynthetic deficiency due to puhC gene deletion in Rhodobacter capsulatus suggests a PuhC protein-dependent process of RC/LH1/PufX complex reorganization. Arch. Biochem. Biophys. 454 (2006) 59-71
    • (2006) Arch. Biochem. Biophys. , vol.454 , pp. 59-71
    • Aklujkar, M.1    Prince, R.C.2    Beatty, J.T.3
  • 134
    • 0000730725 scopus 로고
    • Genetic manipulation of the antenna complexes of purple bacteria
    • Blankenship R.E., Madigan M.T., and Bauer C.E. (Eds), Kluwer Academic Publishers, The Netherlands
    • Hunter C.N. Genetic manipulation of the antenna complexes of purple bacteria. In: Blankenship R.E., Madigan M.T., and Bauer C.E. (Eds). Anoxygenic Photosynthetic Bacteria (1995), Kluwer Academic Publishers, The Netherlands 473-501
    • (1995) Anoxygenic Photosynthetic Bacteria , pp. 473-501
    • Hunter, C.N.1
  • 135
    • 0022344842 scopus 로고
    • Chromosomal deletion and plasmid complementation of the photosynthetic reaction center and light-harvesting genes from Rhodopseudomonas capsulata
    • Youvan D.C., Ismail S., and Bylina E.J. Chromosomal deletion and plasmid complementation of the photosynthetic reaction center and light-harvesting genes from Rhodopseudomonas capsulata. Gene 38 (1985) 19-30
    • (1985) Gene , vol.38 , pp. 19-30
    • Youvan, D.C.1    Ismail, S.2    Bylina, E.J.3
  • 137
    • 0011805789 scopus 로고
    • Some mutational changes in the photosynthetic pigment system of Rhodopseudomonas spheroides
    • Griffiths M., and Stanier R.Y. Some mutational changes in the photosynthetic pigment system of Rhodopseudomonas spheroides. J. Gen. Micro. 14 (1956) 698-715
    • (1956) J. Gen. Micro. , vol.14 , pp. 698-715
    • Griffiths, M.1    Stanier, R.Y.2
  • 138
    • 0011175228 scopus 로고
    • Rhodopseudomonas-spheroides - high catalase and blue-green double mutants
    • Clayton R.K., and Smith C. Rhodopseudomonas-spheroides - high catalase and blue-green double mutants. Biochem. Biophys. Res. Commun. 3 (1960) 143-145
    • (1960) Biochem. Biophys. Res. Commun. , vol.3 , pp. 143-145
    • Clayton, R.K.1    Smith, C.2
  • 139
    • 0014411527 scopus 로고
    • Isolation of a reaction center fraction from Rhodopseudomonas spheroides
    • Reed D.W., and Clayton R.K. Isolation of a reaction center fraction from Rhodopseudomonas spheroides. Biochem. Biophys. Res. Commun. 30 (1968) 471-475
    • (1968) Biochem. Biophys. Res. Commun. , vol.30 , pp. 471-475
    • Reed, D.W.1    Clayton, R.K.2
  • 140
    • 0014690946 scopus 로고
    • Isolation and composition of a photosynthetic reaction center complex from Rhodopseudomonas spheroides
    • Reed D.W. Isolation and composition of a photosynthetic reaction center complex from Rhodopseudomonas spheroides. J. Biol. Chem. 244 (1969) 4936-4941
    • (1969) J. Biol. Chem. , vol.244 , pp. 4936-4941
    • Reed, D.W.1
  • 141
    • 0019842414 scopus 로고
    • The polypeptide composition of the B850 light-harvesting pigment-protein complex from Rhodopseudomonas sphaeroides, R26.1
    • Davidson E., and Cogdell R.J. The polypeptide composition of the B850 light-harvesting pigment-protein complex from Rhodopseudomonas sphaeroides, R26.1. FEBS Letts. 132 (1981) 81-84
    • (1981) FEBS Letts. , vol.132 , pp. 81-84
    • Davidson, E.1    Cogdell, R.J.2
  • 142
    • 0345129949 scopus 로고
    • Genetic analysis and regulation of carotenoid biosynthesis: structure and function of the crt genes and gene products
    • Blankenship R.E., Madigan M.T., and Bauer C.E. (Eds), Kluwer Academic Publishers, The Netherlands
    • Armstrong G.A. Genetic analysis and regulation of carotenoid biosynthesis: structure and function of the crt genes and gene products. In: Blankenship R.E., Madigan M.T., and Bauer C.E. (Eds). Anoxygenic Photosynthetic Bacteria (1995), Kluwer Academic Publishers, The Netherlands 1135-1157
    • (1995) Anoxygenic Photosynthetic Bacteria , pp. 1135-1157
    • Armstrong, G.A.1
  • 143
    • 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. The solution structure of the PufX polypeptide from Rhodobacter sphaeroides. FEBS Letts. 580 (2006) 6967-6971
    • (2006) FEBS Letts. , vol.580 , pp. 6967-6971
    • Tunnicliffe, R.B.1    Ratcliffe, E.C.2    Hunter, C.N.3    Williamson, M.P.4
  • 144
    • 33947634434 scopus 로고    scopus 로고
    • Overexpression and characterization of the Rhodobacter sphaeroides PufX membrane protein in Escherichia coli
    • Onodera S., Suzuki H., Shimada Y., Kobayashi M., Nozawa T., and Wang Z.Y. Overexpression and characterization of the Rhodobacter sphaeroides PufX membrane protein in Escherichia coli. Photochem. Photobiol. 83 (2007) 139-144
    • (2007) Photochem. Photobiol. , vol.83 , pp. 139-144
    • Onodera, S.1    Suzuki, H.2    Shimada, Y.3    Kobayashi, M.4    Nozawa, T.5    Wang, Z.Y.6
  • 145
    • 33947631898 scopus 로고    scopus 로고
    • Solution structure of the Rhodobacter sphaeroides PufX membrane protein: Implications for the quinone exchange and protein-protein interactions
    • Wang Z.Y., Suzuki H., Kobayashi M., and Nozawa T. Solution structure of the Rhodobacter sphaeroides PufX membrane protein: Implications for the quinone exchange and protein-protein interactions. Biochemistry 46 (2007) 3635-3642
    • (2007) Biochemistry , vol.46 , pp. 3635-3642
    • Wang, Z.Y.1    Suzuki, H.2    Kobayashi, M.3    Nozawa, T.4
  • 146
    • 0035825682 scopus 로고    scopus 로고
    • Crystal structure of photosystem-II from Synechococcus elongatus at 3.8 Å resolution
    • Zouni A., Witt H.T., Kern J., Fromme P., Krauss N., Saenger W., and Orth P. Crystal structure of photosystem-II from Synechococcus elongatus at 3.8 Å resolution. Nature 409 (2001) 739-743
    • (2001) Nature , vol.409 , pp. 739-743
    • Zouni, A.1    Witt, H.T.2    Kern, J.3    Fromme, P.4    Krauss, N.5    Saenger, W.6    Orth, P.7
  • 147
    • 0037422557 scopus 로고    scopus 로고
    • Crystal structure of oxygen-evolving photosystem II from Thermosynechococcus vulcanus at 3.7-Angstrom resolution
    • Kamiya N., and Shen J.-R. Crystal structure of oxygen-evolving photosystem II from Thermosynechococcus vulcanus at 3.7-Angstrom resolution. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 98-103
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 98-103
    • Kamiya, N.1    Shen, J.-R.2
  • 148
    • 8144227878 scopus 로고    scopus 로고
    • Crystal structure of cyanobacterial photosystem II at 3.2 Angstrom resolution: a closer look at the Mn-cluster
    • Biesiadka J., Loll B., Kern J., Irrgang K.D., and Zouni A. Crystal structure of cyanobacterial photosystem II at 3.2 Angstrom resolution: a closer look at the Mn-cluster. Phys. Chem. Chem. Phys. 6 (2004) 4733-4736
    • (2004) Phys. Chem. Chem. Phys. , vol.6 , pp. 4733-4736
    • Biesiadka, J.1    Loll, B.2    Kern, J.3    Irrgang, K.D.4    Zouni, A.5
  • 149
  • 150
    • 30744445692 scopus 로고    scopus 로고
    • Towards complete cofactor arrangement in the 3.0 angstrom resolution structure of photosystem II
    • Loll B., Kern J., Saenger W., Zouni A., and Biesiadka J. Towards complete cofactor arrangement in the 3.0 angstrom resolution structure of photosystem II. Nature 438 (2005) 1040-1044
    • (2005) Nature , vol.438 , pp. 1040-1044
    • Loll, B.1    Kern, J.2    Saenger, W.3    Zouni, A.4    Biesiadka, J.5
  • 151
    • 33751197485 scopus 로고    scopus 로고
    • Lipids in photosynthetic reaction centres: structural roles and functional holes
    • Jones M.R. Lipids in photosynthetic reaction centres: structural roles and functional holes. Prog. Lip. Res. 46 (2007) 56-87
    • (2007) Prog. Lip. Res. , vol.46 , pp. 56-87
    • Jones, M.R.1
  • 153
    • 22844437327 scopus 로고    scopus 로고
    • Strong effects of an individual water molecule on the rate of primary charge separation in the Rhodobacter sphaeroides reaction centre
    • Potter J.A., Fyfe P.K., Frolov D., Wakeham M.C., van Grondelle R., Robert B., and Jones M.R. Strong effects of an individual water molecule on the rate of primary charge separation in the Rhodobacter sphaeroides reaction centre. J. Biol. Chem. 280 (2005) 27155-27164
    • (2005) J. Biol. Chem. , vol.280 , pp. 27155-27164
    • Potter, J.A.1    Fyfe, P.K.2    Frolov, D.3    Wakeham, M.C.4    van Grondelle, R.5    Robert, B.6    Jones, M.R.7
  • 154
    • 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
    • Papiz M.Z., Prince S.M., Howard T., Cogdell R.J., and Isaacs N.W. 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. J. Mol. Biol. 326 (2003) 1523-1538
    • (2003) J. Mol. Biol. , vol.326 , pp. 1523-1538
    • Papiz, M.Z.1    Prince, S.M.2    Howard, T.3    Cogdell, R.J.4    Isaacs, N.W.5


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