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Volumn 63, Issue , 2009, Pages 51-82

Chapter 3 Harnessing Photosynthetic Bacteria for Membrane Protein Production

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EID: 66049130785     PISSN: 10635823     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1063-5823(09)63003-9     Document Type: Review
Times cited : (5)

References (71)
  • 1
    • 0034613080 scopus 로고    scopus 로고
    • Characterisation of new intracellular membranes in Escherichia coli accompanying large scale over-production of the b subunit of F(1)F(o) ATP synthase
    • Arechaga I., Miroux B., Karrasch S., Huijbregts R., de Kruijff B., Runswick M.J., et al. Characterisation of new intracellular membranes in Escherichia coli accompanying large scale over-production of the b subunit of F(1)F(o) ATP synthase. FEBS Letters 482 3 (2000) 215-219
    • (2000) FEBS Letters , vol.482 , Issue.3 , pp. 215-219
    • Arechaga, I.1    Miroux, B.2    Karrasch, S.3    Huijbregts, R.4    de Kruijff, B.5    Runswick, M.J.6
  • 3
    • 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. The Journal of Biological Chemistry 279 20 (2004) 21327-21333
    • (2004) The 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
  • 4
    • 0342586494 scopus 로고    scopus 로고
    • Membrane lipids in anoxygenic photosynthetic bacteria
    • Siegenthaler P.A., and Murata N. (Eds), Dordrecht, Kluwer
    • Benning C. Membrane lipids in anoxygenic photosynthetic bacteria. In: Siegenthaler P.A., and Murata N. (Eds). Lipids in photosynthesis: Structure, function, and genetics (1998), Dordrecht, Kluwer 83-101
    • (1998) Lipids in photosynthesis: Structure, function, and genetics , pp. 83-101
    • Benning, C.1
  • 5
    • 0037391107 scopus 로고    scopus 로고
    • Membrane protein crystallization
    • Caffrey M. Membrane protein crystallization. Journal of Structural Biology 142 (2003) 108-132
    • (2003) Journal of Structural Biology , vol.142 , pp. 108-132
    • Caffrey, M.1
  • 8
    • 33646147814 scopus 로고    scopus 로고
    • Expression, purification, and characterization of Thermotoga maritima membrane proteins for structure determination
    • Columbus L., Lipfert J., Klock H., Millett I., Doniach S., and Lesley S.A. Expression, purification, and characterization of Thermotoga maritima membrane proteins for structure determination. Protein Science 15 5 (2006) 961-975
    • (2006) Protein Science , vol.15 , Issue.5 , pp. 961-975
    • Columbus, L.1    Lipfert, J.2    Klock, H.3    Millett, I.4    Doniach, S.5    Lesley, S.A.6
  • 9
    • 0034917301 scopus 로고    scopus 로고
    • A novel system for heterologous expression of flavocytochrome c in phototrophic bacteria using the Allochromatium vinosum rbca promoter
    • De Smet L., Kostanjevecki V., Guisez Y., and Van Beeumen J. A novel system for heterologous expression of flavocytochrome c in phototrophic bacteria using the Allochromatium vinosum rbca promoter. Archives of Microbiology 176 1-2 (2001) 19-28
    • (2001) Archives of Microbiology , vol.176 , Issue.1-2 , pp. 19-28
    • De Smet, L.1    Kostanjevecki, V.2    Guisez, Y.3    Van Beeumen, J.4
  • 10
    • 0019514311 scopus 로고
    • On insertion of pigment-associated polypeptides during membrane biogenesis in Rhodopseudomonas capsulata
    • Dierstein R., Schumacher A., and Drews G. On insertion of pigment-associated polypeptides during membrane biogenesis in Rhodopseudomonas capsulata. Archives of Microbiology 128 (1981) 376-383
    • (1981) Archives of Microbiology , vol.128 , pp. 376-383
    • Dierstein, R.1    Schumacher, A.2    Drews, G.3
  • 11
    • 0022000283 scopus 로고
    • Plasmids related to the broad host range vector, prk290, useful for gene cloning and for monitoring gene expression
    • Ditta G., Schmidhauser T., Yakobsen E., Lu P., Liang X.W., Finlay D.R., et al. Plasmids related to the broad host range vector, prk290, useful for gene cloning and for monitoring gene expression. Plasmid 13 (1985) 149-153
    • (1985) Plasmid , vol.13 , pp. 149-153
    • Ditta, G.1    Schmidhauser, T.2    Yakobsen, E.3    Lu, P.4    Liang, X.W.5    Finlay, D.R.6
  • 12
    • 0021918898 scopus 로고
    • Structure and functional organization of light-harvesting complexes and photochemical reaction centers in membranes of phototrophic bacteria
    • Drews G. Structure and functional organization of light-harvesting complexes and photochemical reaction centers in membranes of phototrophic bacteria. Microbiological Review 49 1 (1985) 59-70
    • (1985) Microbiological Review , vol.49 , Issue.1 , pp. 59-70
    • Drews, G.1
  • 13
    • 0002405138 scopus 로고
    • Structure, molecular organization, and biosynthesis of membranes of purple bacteria
    • Blankenship R.E., Madigan M.T., and Bauer C.E. (Eds), Dordrecht, Kluwer
    • Drews G., and Golecki J.R. Structure, molecular organization, and biosynthesis of membranes of purple bacteria. In: Blankenship R.E., Madigan M.T., and Bauer C.E. (Eds). Anoxygenic photosynthetic bacteria (1995), Dordrecht, Kluwer 231-257
    • (1995) Anoxygenic photosynthetic bacteria , pp. 231-257
    • Drews, G.1    Golecki, J.R.2
  • 14
    • 0345356385 scopus 로고    scopus 로고
    • A strategy for identification and quantification of detergents frequently used in the purification of membrane proteins
    • Eriks L.R., Mayor J.A., and Kaplan R.S. A strategy for identification and quantification of detergents frequently used in the purification of membrane proteins. Analytical Biochemistry 323 2 (2003) 234-241
    • (2003) Analytical Biochemistry , vol.323 , Issue.2 , pp. 234-241
    • Eriks, L.R.1    Mayor, J.A.2    Kaplan, R.S.3
  • 15
    • 0036408584 scopus 로고    scopus 로고
    • Structural genomics of "non-standard" proteins: A chance for membrane proteins?
    • Essen L.O. Structural genomics of "non-standard" proteins: A chance for membrane proteins?. Gene Function and Disease 3 (2002) 39-48
    • (2002) Gene Function and Disease , vol.3 , pp. 39-48
    • Essen, L.O.1
  • 16
    • 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. 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 Journal 8 (1989) 47-54
    • (1989) EMBO Journal , vol.8 , pp. 47-54
    • Farchaus, J.W.1    Oesterhelt, D.2
  • 18
    • 0032914633 scopus 로고    scopus 로고
    • Surface display of a parasite antigen in the ciliate Tetrahymena thermophila
    • Gaertig J., Gao Y., Tishgarten T., Clark T.G., and Dickerson H.W. Surface display of a parasite antigen in the ciliate Tetrahymena thermophila. Nature Biotechnology 17 5 (1999) 462-465
    • (1999) Nature Biotechnology , vol.17 , Issue.5 , pp. 462-465
    • Gaertig, J.1    Gao, Y.2    Tishgarten, T.3    Clark, T.G.4    Dickerson, H.W.5
  • 19
    • 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. Journal of Microscopy 162 Pt. 1 (1991) 147-154
    • (1991) Journal of Microscopy , vol.162 , Issue.PART 1 , pp. 147-154
    • Golecki, J.R.1    Heinrich, U.R.2
  • 20
    • 0025967181 scopus 로고
    • The architecture of unusual membrane tubes in the B800-B850 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-B850 light-harvesting bacteriochlorophyll-deficient mutant 19 of Rhodobacter sphaeroides. FEMS Microbiology Letters 77 (1991) 335-340
    • (1991) FEMS Microbiology Letters , vol.77 , pp. 335-340
    • Golecki, J.R.1    Ventura, S.2    Oelze, J.3
  • 22
    • 0029142564 scopus 로고
    • Overexpression of integral membrane proteins for structural studies
    • Grisshammer R., and Tate C. Overexpression of integral membrane proteins for structural studies. Quarterly Reviews of Biophysics 28 3 (1995) 315-422
    • (1995) Quarterly Reviews of Biophysics , vol.28 , Issue.3 , pp. 315-422
    • Grisshammer, R.1    Tate, C.2
  • 23
    • 0032190666 scopus 로고    scopus 로고
    • Use of cell wall-less bacteria (L-forms) for efficient expression and secretion of heterologous gene products
    • Gumpert J., and Hoischen C. Use of cell wall-less bacteria (L-forms) for efficient expression and secretion of heterologous gene products. Current Opinion in Biotechnology 9 5 (1998) 506-509
    • (1998) Current Opinion in Biotechnology , vol.9 , Issue.5 , pp. 506-509
    • Gumpert, J.1    Hoischen, C.2
  • 24
    • 0036156641 scopus 로고    scopus 로고
    • Novel bacterial membrane surface display system using cell wall-less L-forms of Proteus mirabilis and Escherichia coli
    • Hoischen C., Fritsche C., Gumpert J., Westermann M., Gura K., and Fahnert B. Novel bacterial membrane surface display system using cell wall-less L-forms of Proteus mirabilis and Escherichia coli. Applied and Environmental Microbiology 68 2 (2002) 525-531
    • (2002) Applied and Environmental Microbiology , vol.68 , Issue.2 , pp. 525-531
    • Hoischen, C.1    Fritsche, C.2    Gumpert, J.3    Westermann, M.4    Gura, K.5    Fahnert, B.6
  • 25
    • 0001753915 scopus 로고
    • Oligomerization states and associations of light-harvesting pigment protein complexes of Rhodobacter sphaeroides as analyzed by lithium dodecylsulfate 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 dodecylsulfate 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
  • 26
    • 0002558837 scopus 로고
    • Taxonomy and physiology of phototrophic purple bacteria and green sulfur bacteria
    • Blankenship R.E., Madigan M.T., and Bauer C.E. (Eds), Dordrecht, Kluwer
    • Imhoff J.F. Taxonomy and physiology of phototrophic purple bacteria and green sulfur bacteria. In: Blankenship R.E., Madigan M.T., and Bauer C.E. (Eds). Anoxygenic photosynthetic bacteria (1995), Dordrecht, Kluwer
    • (1995) Anoxygenic photosynthetic bacteria
    • Imhoff, J.F.1
  • 27
    • 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., Qian P., Kirkland J.Y., Conroy M.J., Hunter C.N., et al. Projection structure of the photosynthetic reaction centre-antenna complex of Rhodospirillum rubrum at 8.5 Angstrom resolution. EMBO Journal 21 15 (2002) 3927-3935
    • (2002) EMBO Journal , vol.21 , Issue.15 , pp. 3927-3935
    • Jamieson, S.J.1    Wang, P.2    Qian, P.3    Kirkland, J.Y.4    Conroy, M.J.5    Hunter, C.N.6
  • 28
    • 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 Vermeglio A. Supramolecular organization of the photosynthetic apparatus of Rhodobacter sphaeroides. EMBO Journal 18 3 (1999) 534-542
    • (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
  • 29
    • 0037048677 scopus 로고    scopus 로고
    • A system for the heterologous expression of complex redox proteins in Rhodobacter capsulatus: Characterisation of recombinant sulphite:cytochrome c oxidoreductase from Starkeya novella
    • Kappler U., and McEwan A.G. A system for the heterologous expression of complex redox proteins in Rhodobacter capsulatus: Characterisation of recombinant sulphite:cytochrome c oxidoreductase from Starkeya novella. FEBS Letters 529 2-3 (2002) 208-214
    • (2002) FEBS Letters , vol.529 , Issue.2-3 , pp. 208-214
    • Kappler, U.1    McEwan, A.G.2
  • 30
    • 0028953308 scopus 로고
    • The 8.5 angstrom 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 angstrom projection map of the light-harvesting complex I from Rhodospirillum rubrum reveals a ring composed of 16 subunits. EMBO Journal 14 (1995) 631-638
    • (1995) EMBO Journal , vol.14 , pp. 631-638
    • Karrasch, S.1    Bullough, P.A.2    Ghosh, R.3
  • 31
    • 85012803379 scopus 로고
    • Techniques of lipidology: Isolation, analysis, and identification of lipids
    • Elsevier, New York, NY 2nd revised Ed., Vol. 3, Pt. 2
    • Kates M. Techniques of lipidology: Isolation, analysis, and identification of lipids. Laboratory techniques in biochemistry and molecular biology (1986), Elsevier, New York, NY 2nd revised Ed., Vol. 3, Pt. 2
    • (1986) Laboratory techniques in biochemistry and molecular biology
    • Kates, M.1
  • 32
    • 0033392364 scopus 로고    scopus 로고
    • Refolding of G-protein-coupled receptors from inclusion bodies produced in Escherichia coli
    • Kiefer H., Maier K., and Vogel R. Refolding of G-protein-coupled receptors from inclusion bodies produced in Escherichia coli. Biochemical Society Transactions 27 (1999) 908-912
    • (1999) Biochemical Society Transactions , vol.27 , pp. 908-912
    • Kiefer, H.1    Maier, K.2    Vogel, R.3
  • 33
    • 0023968065 scopus 로고
    • Molecular genetics of photosynthetic membrane biosynthesis in Rhodobacter sphaeroides
    • Kiley P.J., and Kaplan S. Molecular genetics of photosynthetic membrane biosynthesis in Rhodobacter sphaeroides. Microbiological Reviews 52 (1988) 50-69
    • (1988) Microbiological Reviews , vol.52 , pp. 50-69
    • Kiley, P.J.1    Kaplan, S.2
  • 34
    • 0023972876 scopus 로고
    • Physiological and structural analysis of light-harvesting mutants of Rhodobacter sphaeroides
    • Kiley P.J., Varga A., and Kaplan S. Physiological and structural analysis of light-harvesting mutants of Rhodobacter sphaeroides. Journal of Bacteriology 170 3 (1988) 1103-1115
    • (1988) Journal of Bacteriology , vol.170 , Issue.3 , pp. 1103-1115
    • Kiley, P.J.1    Varga, A.2    Kaplan, S.3
  • 36
    • 1642331383 scopus 로고    scopus 로고
    • Detergent effects on primary charge separation in wild-type and mutant Rhodobacter capsulatus reaction centers
    • Kirmaier C., Laible P.D., Hindin E., Hanson D.K., and Holten D. Detergent effects on primary charge separation in wild-type and mutant Rhodobacter capsulatus reaction centers. Chemical Physics 294 (2003) 305-318
    • (2003) Chemical Physics , vol.294 , pp. 305-318
    • Kirmaier, C.1    Laible, P.D.2    Hindin, E.3    Hanson, D.K.4    Holten, D.5
  • 37
    • 0002807629 scopus 로고
    • Post-transcriptional control of photosynthesis gene expression
    • Blankenship R.E., Madigan M.T., and Bauer C.E. (Eds), Dordrecht, Kluwer
    • Klug G. Post-transcriptional control of photosynthesis gene expression. In: Blankenship R.E., Madigan M.T., and Bauer C.E. (Eds). Anoxygenic photosynthetic bacteria (1995), Dordrecht, Kluwer 1235-1244
    • (1995) Anoxygenic photosynthetic bacteria , pp. 1235-1244
    • Klug, G.1
  • 38
    • 0030585121 scopus 로고    scopus 로고
    • The crystal structure of the light-harvesting complex II (B800-850) from Rhodospirillum molischianum
    • Koepke J., Hu X., 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.2    Muenke, C.3    Schulten, K.4    Michel, H.5
  • 39
    • 11144234979 scopus 로고    scopus 로고
    • Cloning and expression of multiple integral membrane proteins from Mycobacterium tuberculosis in Escherichia coli
    • Korepanova A., Gao F.P., Hua Y., Qin H., Nakamoto R.K., and Cross T.A. Cloning and expression of multiple integral membrane proteins from Mycobacterium tuberculosis in Escherichia coli. Protein Science 14 1 (2005) 148-158
    • (2005) Protein Science , vol.14 , Issue.1 , pp. 148-158
    • Korepanova, A.1    Gao, F.P.2    Hua, Y.3    Qin, H.4    Nakamoto, R.K.5    Cross, T.A.6
  • 41
    • 26444621348 scopus 로고    scopus 로고
    • Incorporation of selenomethionine into induced intracytoplasmic membrane proteins of Rhodobacter species
    • Laible P.D., Hata A.N., Crawford A.E., and Hanson D.K. Incorporation of selenomethionine into induced intracytoplasmic membrane proteins of Rhodobacter species. Journal of Structural and Functional Genomics 6 2-3 (2005) 95-102
    • (2005) Journal of Structural and Functional Genomics , vol.6 , Issue.2-3 , pp. 95-102
    • Laible, P.D.1    Hata, A.N.2    Crawford, A.E.3    Hanson, D.K.4
  • 43
    • 0024689101 scopus 로고
    • Post-transcriptional control of puc operon expression of B800-850 light-harvesting complex formation in Rhodobacter sphaeroides
    • Lee J.K., Kiley P.J., and Kaplan S. Post-transcriptional control of puc operon expression of B800-850 light-harvesting complex formation in Rhodobacter sphaeroides. Journal of Bacteriology 171 (1989) 3391-3405
    • (1989) Journal of Bacteriology , vol.171 , pp. 3391-3405
    • Lee, J.K.1    Kiley, P.J.2    Kaplan, S.3
  • 44
    • 0034707086 scopus 로고    scopus 로고
    • Interaction of membrane proteins and lipids with solubilizing detergents
    • le Maire M., Champeil P., and Moller J.V. Interaction of membrane proteins and lipids with solubilizing detergents. Biochimica et Biophysica Acta 1508 1-2 (2000) 86-111
    • (2000) Biochimica et Biophysica Acta , vol.1508 , Issue.1-2 , pp. 86-111
    • le Maire, M.1    Champeil, P.2    Moller, J.V.3
  • 45
    • 0018125862 scopus 로고
    • Comparison, by freeze-fracture electron microscopy, of chromatophores, spheroplast-derived membrane vesicles, and whole cells of Rhodopseudomonas sphaeroides
    • Lommen M.A., and Takemoto J. Comparison, by freeze-fracture electron microscopy, of chromatophores, spheroplast-derived membrane vesicles, and whole cells of Rhodopseudomonas sphaeroides. Journal of Bacteriology 136 2 (1978) 730-741
    • (1978) Journal of Bacteriology , vol.136 , Issue.2 , pp. 730-741
    • Lommen, M.A.1    Takemoto, J.2
  • 48
    • 0030593468 scopus 로고    scopus 로고
    • Over-production of proteins in Escherichia coli: Mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels
    • Miroux B., and Walker J.E. Over-production of proteins in Escherichia coli: Mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels. Journal of Molecular Biology 260 (1996) 289-298
    • (1996) Journal of Molecular Biology , vol.260 , pp. 289-298
    • Miroux, B.1    Walker, J.E.2
  • 49
    • 0020713543 scopus 로고
    • Monoclonal antibodies to rhodopsin: Characterization, cross-reactivity, and application as structural probes
    • Molday R.S., and MacKenzie D. Monoclonal antibodies to rhodopsin: Characterization, cross-reactivity, and application as structural probes. Biochemistry 22 3 (1983) 653-660
    • (1983) Biochemistry , vol.22 , Issue.3 , pp. 653-660
    • Molday, R.S.1    MacKenzie, D.2
  • 51
    • 0032478599 scopus 로고    scopus 로고
    • The particulate methane monooxygenase from Methylococcus capsulatus (Bath) is a novel copper-containing three-subunit enzyme. Isolation and characterization
    • Nguyen H.H., Elliott S.J., Yip J.H., and Chan S.I. The particulate methane monooxygenase from Methylococcus capsulatus (Bath) is a novel copper-containing three-subunit enzyme. Isolation and characterization. The Journal of Biological Chemistry 273 14 (1998) 7957-7966
    • (1998) The Journal of Biological Chemistry , vol.273 , Issue.14 , pp. 7957-7966
    • Nguyen, H.H.1    Elliott, S.J.2    Yip, J.H.3    Chan, S.I.4
  • 52
    • 11944264683 scopus 로고    scopus 로고
    • Membrane protein crystallization in amphiphile phases: Practical and theoretical considerations
    • Nollert P. Membrane protein crystallization in amphiphile phases: Practical and theoretical considerations. Progress in Biophysics and Molecular Biology 88 3 (2005) 339-357
    • (2005) Progress in Biophysics and Molecular Biology , vol.88 , Issue.3 , pp. 339-357
    • Nollert, P.1
  • 53
    • 0037076542 scopus 로고    scopus 로고
    • The structure of a mutant photosynthetic reaction center shows unexpected changes in main chain orientations and quinone position
    • Pokkuluri P.R., Laible P.D., Deng Y.L., Wong T.N., Hanson D.K., and Schiffer M. The structure of a mutant photosynthetic reaction center shows unexpected changes in main chain orientations and quinone position. Biochemistry 41 19 (2002) 5998-6007
    • (2002) Biochemistry , vol.41 , Issue.19 , pp. 5998-6007
    • Pokkuluri, P.R.1    Laible, P.D.2    Deng, Y.L.3    Wong, T.N.4    Hanson, D.K.5    Schiffer, M.6
  • 54
    • 33947172767 scopus 로고    scopus 로고
    • Detergents for the stabilization and crystallization of membrane proteins
    • Prive G.G. Detergents for the stabilization and crystallization of membrane proteins. Methods 41 4 (2007) 388-397
    • (2007) Methods , vol.41 , Issue.4 , pp. 388-397
    • Prive, G.G.1
  • 55
    • 0037593237 scopus 로고    scopus 로고
    • A reaction center-light-harvesting 1 complex (RC-LH1) from a Rhodospirillum rubrum mutant with altered esterifying pigments: Characterization by optical spectroscopy and cryo-electron microscopy
    • Qian P., Addlesee H.A., Ruban A.V., Wang P., Bullough P.A., and Hunter C.N. A reaction center-light-harvesting 1 complex (RC-LH1) from a Rhodospirillum rubrum mutant with altered esterifying pigments: Characterization by optical spectroscopy and cryo-electron microscopy. The Journal of Biological Chemistry 278 26 (2003) 23678-23685
    • (2003) The Journal of Biological Chemistry , vol.278 , Issue.26 , pp. 23678-23685
    • Qian, P.1    Addlesee, H.A.2    Ruban, A.V.3    Wang, P.4    Bullough, P.A.5    Hunter, C.N.6
  • 56
    • 20344374627 scopus 로고    scopus 로고
    • The 8.5A projection structure of the core RC-LH1-pufx dimer of Rhodobacter sphaeroides
    • Qian P., Hunter C.N., and Bullough P.A. The 8.5A projection structure of the core RC-LH1-pufx dimer of Rhodobacter sphaeroides. Journal of Molecular Biology 349 5 (2005) 948-960
    • (2005) Journal of Molecular Biology , vol.349 , Issue.5 , pp. 948-960
    • Qian, P.1    Hunter, C.N.2    Bullough, P.A.3
  • 57
    • 0022492620 scopus 로고
    • Role of apparent membrane growth initiation sites during photosynthetic membrane development in synchronously dividing Rhodopseudomonas sphaeroides
    • Reilly P.A., and Niederman R.A. Role of apparent membrane growth initiation sites during photosynthetic membrane development in synchronously dividing Rhodopseudomonas sphaeroides. Journal of Bacteriology 167 1 (1986) 153-159
    • (1986) Journal of Bacteriology , vol.167 , Issue.1 , pp. 153-159
    • Reilly, P.A.1    Niederman, R.A.2
  • 58
    • 0346874216 scopus 로고    scopus 로고
    • Crystal structure of the RC-LH1 core complex from Rhodopseudomonas palustris
    • Roszak A.W., Howard T.D., Southall J., Gardiner A.T., Law C.J., Isaacs N.W., et al. Crystal structure of the RC-LH1 core complex from Rhodopseudomonas palustris. Science 302 (2003) 1969-1972
    • (2003) Science , vol.302 , 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
  • 59
    • 7044272757 scopus 로고    scopus 로고
    • Membrane proteins, lipids and detergents: Not just a soap opera
    • Seddon A.M., Curnow P., and Booth P.J. Membrane proteins, lipids and detergents: Not just a soap opera. Biochimica et Biophysica Acta 1666 1-2 (2004) 105-117
    • (2004) Biochimica et Biophysica Acta , vol.1666 , Issue.1-2 , pp. 105-117
    • Seddon, A.M.1    Curnow, P.2    Booth, P.J.3
  • 60
    • 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 Journal 23 4 (2004) 690-700
    • (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
  • 61
    • 0021027842 scopus 로고
    • A broad host range mobilization system for in vivo genetic engineering: Transposon mutagenesis in gram negative bacteria
    • Simon R., Priefer U., and Puhler A. A broad host range mobilization system for in vivo genetic engineering: Transposon mutagenesis in gram negative bacteria. Bio/Technology 1 (1983) 37-45
    • (1983) Bio/Technology , vol.1 , pp. 37-45
    • Simon, R.1    Priefer, U.2    Puhler, A.3
  • 62
    • 0026467208 scopus 로고
    • Biochemical characterization and electron-transfer reactions of sym1, a Rhodobacter capsulatus symmetry mutant which affects the initial electron donor
    • Taguchi A.K.W., Stocker J.W., Alden R.G., Causgrove T.P., Peloquin J.M., Boxer S.G., et al. Biochemical characterization and electron-transfer reactions of sym1, a Rhodobacter capsulatus symmetry mutant which affects the initial electron donor. Biochemistry 31 (1992) 10345-10355
    • (1992) Biochemistry , vol.31 , pp. 10345-10355
    • Taguchi, A.K.W.1    Stocker, J.W.2    Alden, R.G.3    Causgrove, T.P.4    Peloquin, J.M.5    Boxer, S.G.6
  • 63
    • 0018356319 scopus 로고
    • Orientation of chromatophores and spheroplast-derived membrane vesicles of Rhodopseudomonas sphaeroides: Analysis by localization of enzyme activities
    • Takemoto J., and Bachmann R.C. Orientation of chromatophores and spheroplast-derived membrane vesicles of Rhodopseudomonas sphaeroides: Analysis by localization of enzyme activities. Archives of Biochemistry and Biophysics 195 2 (1979) 526-534
    • (1979) Archives of Biochemistry and Biophysics , vol.195 , Issue.2 , pp. 526-534
    • Takemoto, J.1    Bachmann, R.C.2
  • 64
    • 0026535478 scopus 로고
    • Cell-free synthesis and membrane integration of the reaction center subunit H from Rhodobacter capsulatus
    • Troschel D., Eckhardt S., Hoffschulte H.K., and Muller M. Cell-free synthesis and membrane integration of the reaction center subunit H from Rhodobacter capsulatus. FEMS Microbiology Letters 91 (1992) 129-133
    • (1992) FEMS Microbiology Letters , vol.91 , pp. 129-133
    • Troschel, D.1    Eckhardt, S.2    Hoffschulte, H.K.3    Muller, M.4
  • 67
    • 48749149466 scopus 로고
    • Size and structure of antenna complexes of photosynthetic bacteria as studied by singlet-singlet quenching of the bacteriochlrophyll fluorescence yield
    • van Grondelle R., Hunter C.N., Bakker J.G.C., and Kramer H.J.M. Size and structure of antenna complexes of photosynthetic bacteria as studied by singlet-singlet quenching of the bacteriochlrophyll fluorescence yield. Biochimica et Biophysica Acta 723 (1983) 30-36
    • (1983) Biochimica et Biophysica Acta , vol.723 , pp. 30-36
    • van Grondelle, R.1    Hunter, C.N.2    Bakker, J.G.C.3    Kramer, H.J.M.4
  • 68
    • 0000531750 scopus 로고
    • Organization of electron transfer components and supercomplexes
    • Blankenship R.E., Madigan M.T., and Bauer C.E. (Eds), Dordrecht, Kluwer
    • Verméglio A., Joliot P., and Joliot A. Organization of electron transfer components and supercomplexes. In: Blankenship R.E., Madigan M.T., and Bauer C.E. (Eds). Anoxygenic photosynthetic bacteria (1995), Dordrecht, Kluwer 279-295
    • (1995) Anoxygenic photosynthetic bacteria , pp. 279-295
    • Verméglio, A.1    Joliot, P.2    Joliot, A.3
  • 69
    • 0031877370 scopus 로고    scopus 로고
    • Electron crystallography of two dimensional crystals of membrane proteins
    • Walz T., and Grigorieff N. Electron crystallography of two dimensional crystals of membrane proteins. Journal of Structural Biology 121 (1998) 142-161
    • (1998) Journal of Structural Biology , vol.121 , pp. 142-161
    • Walz, T.1    Grigorieff, N.2
  • 70
    • 4344579363 scopus 로고    scopus 로고
    • A pedestrian guide to membrane protein crystallization
    • Wiener M.C. A pedestrian guide to membrane protein crystallization. Methods 34 3 (2004) 364-372
    • (2004) Methods , vol.34 , Issue.3 , pp. 364-372
    • Wiener, M.C.1
  • 71
    • 0029780351 scopus 로고    scopus 로고
    • The molecular structure of green fluorescent protein
    • Yang F., Moss L.G., and Phillips Jr. G.N. The molecular structure of green fluorescent protein. Nature Biotechnology 14 10 (1996) 1246-1251
    • (1996) Nature Biotechnology , vol.14 , Issue.10 , pp. 1246-1251
    • Yang, F.1    Moss, L.G.2    Phillips Jr., G.N.3


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