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Volumn 78, Issue 2, 2003, Pages 93-117

Chlorobium tepidum: Insights into the structure, physiology, and metabolism of a green sulfur bacterium derived from the complete genome sequence

Author keywords

Bacteriochlorophyll; Biosynthesis; Carotenoid; Chlorophyll; Chlorosome; Genomics; Green sulfur bacterium photosynthesis

Indexed keywords

BACTERIA (MICROORGANISMS); CHLOROBACULUM TEPIDUM; CHLOROBI; CHLOROBIUM; CYANOBACTERIA; PHOTOBACTERIA;

EID: 0347596598     PISSN: 01668595     EISSN: None     Source Type: Journal    
DOI: 10.1023/B:PRES.0000004310.96189.b4     Document Type: Review
Times cited : (145)

References (138)
  • 2
    • 0000972384 scopus 로고
    • Structure and sequence of the photosynthetic gene cluster
    • Blankenship RE, Madigan, MT and Bauer CE (eds) Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Alberti M, Burke DH and Hearst JE (1995) Structure and sequence of the photosynthetic gene cluster. In: Blankenship RE, Madigan, MT and Bauer CE (eds) Anoxygenic Photosynthetic Bacteria, pp 1083-1106. Kluwer Academic Publishers, Dordrecht, The Netherlands
    • (1995) Anoxygenic Photosynthetic Bacteria , pp. 1083-1106
    • Alberti, M.1    Burke, D.H.2    Hearst, J.E.3
  • 4
    • 0035425018 scopus 로고    scopus 로고
    • Protein export and drug efflux through bacterial channel-tunnels
    • Andersen C, Hughes C and Koronakis V (2001) Protein export and drug efflux through bacterial channel-tunnels. Curr Opin Cell Biol 13: 412-416
    • (2001) Curr Opin Cell Biol , vol.13 , pp. 412-416
    • Andersen, C.1    Hughes, C.2    Koronakis, V.3
  • 5
    • 0034082075 scopus 로고    scopus 로고
    • The bidirectional hydrogenase of Synechocystis sp PCC 6803 works as an electron valve during photosynthesis
    • Appel J, Phunpruch S, Steinmüller K and Schulz R (2000) The bidirectional hydrogenase of Synechocystis sp PCC 6803 works as an electron valve during photosynthesis. Arch Microbiol 173: 333-338
    • (2000) Arch Microbiol , vol.173 , pp. 333-338
    • Appel, J.1    Phunpruch, S.2    Steinmüller, K.3    Schulz, R.4
  • 6
    • 0000756743 scopus 로고    scopus 로고
    • Carotenoid genetics and biochemistry
    • Barton D, Nakanishi K and Meth-Cohn O (eds) Elsevier, Amsterdam
    • Armstrong G (1999) Carotenoid genetics and biochemistry. In: Barton D, Nakanishi K and Meth-Cohn O (eds) Comprehensive Natural Products Chemistry, Vol 2, pp 321-352. Elsevier, Amsterdam
    • (1999) Comprehensive Natural Products Chemistry , vol.2 , pp. 321-352
    • Armstrong, G.1
  • 7
    • 0036968064 scopus 로고    scopus 로고
    • Microbial enzymes involved in carbon dioxide fixation
    • Atomi H (2002) Microbial enzymes involved in carbon dioxide fixation. J Biosci Bioeng 94: 497-505
    • (2002) J Biosci Bioeng , vol.94 , pp. 497-505
    • Atomi, H.1
  • 8
    • 0027303801 scopus 로고
    • Enzymes of the reductive citric acid cycle in the autotrophic eubacterium Aquifex pyrophilus and in the archaebacterium Thermoproteus neutrophilus
    • Beh M, Strauss G, Huber R, Stetter K-O and Fuchs g (1993) Enzymes of the reductive citric acid cycle in the autotrophic eubacterium Aquifex pyrophilus and in the archaebacterium Thermoproteus neutrophilus. Arch Microbiol 160: 306-311
    • (1993) Arch Microbiol , vol.160 , pp. 306-311
    • Beh, M.1    Strauss, G.2    Huber, R.3    Stetter, K.-O.4    Fuchs, G.5
  • 10
    • 0842271127 scopus 로고    scopus 로고
    • Antenna complexes in green photosynthetic bacteria
    • Green BR and Parson WW (eds) Kluwer Academic Publishers, Dordrecht, The Netherlands (in press)
    • Blankenship RE and Matsuura K (2003) Antenna complexes in green photosynthetic bacteria. In: Green BR and Parson WW (eds) Light-Harvesting Antennas. Kluwer Academic Publishers, Dordrecht, The Netherlands (in press)
    • (2003) Light-Harvesting Antennas
    • Blankenship, R.E.1    Matsuura, K.2
  • 11
    • 0000400103 scopus 로고
    • Antenna complexes from green photosynthetic bacteria
    • Blankenship RE, Madigan, MT, and Bauer CE (eds) Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Blankenship RE, Olson J and Miller M (1995) Antenna complexes from green photosynthetic bacteria. In: Blankenship RE, Madigan, MT, and Bauer CE (eds) Anoxygenic Photosynthetic Bacteria, pp 399-435. Kluwer Academic Publishers, Dordrecht, The Netherlands
    • (1995) Anoxygenic Photosynthetic Bacteria , pp. 399-435
    • Blankenship, R.E.1    Olson, J.2    Miller, M.3
  • 12
    • 0025323481 scopus 로고
    • Red shift of absorption maxima in Chlorobiineae through enzymatic methylation of their antenna bacteriochlorophylls
    • Bobe FW, Pfennig N, Swanson KL and Smith km (1990) Red shift of absorption maxima in Chlorobiineae through enzymatic methylation of their antenna bacteriochlorophylls. Biochemistry 29: 4340-4348
    • (1990) Biochemistry , vol.29 , pp. 4340-4348
    • Bobe, F.W.1    Pfennig, N.2    Swanson, K.L.3    Smith, K.M.4
  • 13
    • 0031919675 scopus 로고    scopus 로고
    • Unusual gene arrangement of the bidirectional hydrogenase and functional analysis of its diaphorase subunit HoxU in respiration of the unicellular cyanobacterium Anacystis nidulans
    • Boison G, Schmitz O, Schmitz B and Bothe H (1998) Unusual gene arrangement of the bidirectional hydrogenase and functional analysis of its diaphorase subunit HoxU in respiration of the unicellular cyanobacterium Anacystis nidulans. Curr Microbiol 36: 253-258
    • (1998) Curr Microbiol , vol.36 , pp. 253-258
    • Boison, G.1    Schmitz, O.2    Schmitz, B.3    Bothe, H.4
  • 14
    • 0032795892 scopus 로고    scopus 로고
    • Light intensity effects on pigment composition and organisation in the green sulfur bacterium Chlorobium tepidum
    • Borrego CM, Gerola PD, Miller M and Cox RP (1999) Light intensity effects on pigment composition and organisation in the green sulfur bacterium Chlorobium tepidum. Photosynth Res 59: 159-166
    • (1999) Photosynth Res , vol.59 , pp. 159-166
    • Borrego, C.M.1    Gerola, P.D.2    Miller, M.3    Cox, R.P.4
  • 15
    • 0017864716 scopus 로고
    • Isolation of a BChl c mutant from Chlorobium with BChl d by cultivation at low light
    • Broch-Due M and Ormerod JG (1978) Isolation of a BChl c mutant from Chlorobium with BChl d by cultivation at low light. FEMS Microbiol Lett 3: 305-308
    • (1978) FEMS Microbiol Lett , vol.3 , pp. 305-308
    • Broch-Due, M.1    Ormerod, J.G.2
  • 16
    • 0001864314 scopus 로고
    • Sulfur compounds as photosynthetic electron donors
    • Blankenship RE, Madigan, MT and Bauer CE (eds) Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Brune DC (1995) Sulfur compounds as photosynthetic electron donors. In: Blankenship RE, Madigan, MT and Bauer CE (eds) Anoxygenic Photosynthetic Bacteria, pp 847-870. Kluwer Academic Publishers, Dordrecht, The Netherlands
    • (1995) Anoxygenic Photosynthetic Bacteria , pp. 847-870
    • Brune, D.C.1
  • 17
    • 0037015988 scopus 로고    scopus 로고
    • Selective protein extraction from Chlorobium tepidum chlorosomes using detergents. Evidence that CsmA forms multimers and binds bacteriochlorophyll a
    • Bryant DA, Vassilieva EV, Frigaard N-U and Li H (2002) Selective protein extraction from Chlorobium tepidum chlorosomes using detergents. Evidence that CsmA forms multimers and binds bacteriochlorophyll a. Biochemistry 41: 14403-14411
    • (2002) Biochemistry , vol.41 , pp. 14403-14411
    • Bryant, D.A.1    Vassilieva, E.V.2    Frigaard, N.-U.3    Li, H.4
  • 18
    • 0025697659 scopus 로고
    • A reverse Krebs cycle in photosynthesis: Consensus at last
    • Buchanan BB and Arnon DI (1990) A reverse Krebs cycle in photosynthesis: consensus at last. Photosynth Res 24: 47-53
    • (1990) Photosynth Res , vol.24 , pp. 47-53
    • Buchanan, B.B.1    Arnon, D.I.2
  • 19
    • 0026732787 scopus 로고
    • Photosynthetic reaction center genes in green sulfur bacteria and in Photosystem 1 are related
    • Büttner M, Lie D-L, Nelson H, Pinther W, Hauska G and Nelson N (1992a) Photosynthetic reaction center genes in green sulfur bacteria and in Photosystem 1 are related. Proc Natl Acad Sci USA 89: 8135-8139
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 8135-8139
    • Büttner, M.1    Lie, D.-L.2    Nelson, H.3    Pinther, W.4    Hauska, G.5    Nelson, N.6
  • 21
    • 0029806457 scopus 로고    scopus 로고
    • Characterization of csmB genes from Chlorobium vibrioforme 8327D and Chlorobium tepidum and overproduction of the Chlorobium tepidum CsmB protein in Escherichia coli
    • Chung S and Bryant DA (1996a) Characterization of csmB genes from Chlorobium vibrioforme 8327D and Chlorobium tepidum and overproduction of the Chlorobium tepidum CsmB protein in Escherichia coli. Arch Microbiol 166: 234-244
    • (1996) Arch Microbiol , vol.166 , pp. 234-244
    • Chung, S.1    Bryant, D.A.2
  • 22
    • 0030465889 scopus 로고    scopus 로고
    • Characterization of the csmD and csmE genes from Chlorobium tepidum. The CsmA, CsmC, CsmD, and CsmE proteins are components of the chlorosome envelope
    • Chung S and Bryant DA (1996b) Characterization of the csmD and csmE genes from Chlorobium tepidum. The CsmA, CsmC, CsmD, and CsmE proteins are components of the chlorosome envelope. Photosynth Res 50: 41-59
    • (1996) Photosynth Res , vol.50 , pp. 41-59
    • Chung, S.1    Bryant, D.A.2
  • 23
    • 0000360108 scopus 로고
    • Genes encoding two chlorosome proteins from the green sulfur bacteria Chlorobium vibrioforme strain 8327D and Chlorobium tepidum
    • Chung S, Frank G, Zuber H and Bryant DA (1994) Genes encoding two chlorosome proteins from the green sulfur bacteria Chlorobium vibrioforme strain 8327D and Chlorobium tepidum. Photosynth Res 41: 261-275
    • (1994) Photosynth Res , vol.41 , pp. 261-275
    • Chung, S.1    Frank, G.2    Zuber, H.3    Bryant, D.A.4
  • 24
    • 0032528062 scopus 로고    scopus 로고
    • Insertional inactivation studies of the csmA and csmC genes of the green sulfur bacterium Chlorobium vibrioforme 8327: The chlorosome protein CsmA is required for viability but CsmC is dispensable
    • Chung S, Shen G, Ormerod J and Bryant DA (1998) Insertional inactivation studies of the csmA and csmC genes of the green sulfur bacterium Chlorobium vibrioforme 8327: the chlorosome protein CsmA is required for viability but CsmC is dispensable. FEMS Microbiol Lett 164: 353-361
    • (1998) FEMS Microbiol Lett , vol.164 , pp. 353-361
    • Chung, S.1    Shen, G.2    Ormerod, J.3    Bryant, D.A.4
  • 26
    • 0036836471 scopus 로고    scopus 로고
    • Limiting steps of hydrogen production in Chlamydomonas reinhardtii and Synechocystis PCC 6803 as analysed by light-induced gas exchange transients
    • Cournac L, Mus F, Bernard L, Guedeney G, Vignais P and Peltier G (2002) Limiting steps of hydrogen production in Chlamydomonas reinhardtii and Synechocystis PCC 6803 as analysed by light-induced gas exchange transients. Intl J Hydrog Ener 27: 1229-1237
    • (2002) Intl J Hydrog Ener , vol.27 , pp. 1229-1237
    • Cournac, L.1    Mus, F.2    Bernard, L.3    Guedeney, G.4    Vignais, P.5    Peltier, G.6
  • 27
    • 0028485650 scopus 로고
    • Molecular structure and enzymatic function of lycopene cyclase from the cyanobacterium Synechococcus sp strain PCC7942
    • Cunningham FX Jr, Sun Z, Chamovitz D, Hirschberg J and Gantt E (1994) Molecular structure and enzymatic function of lycopene cyclase from the cyanobacterium Synechococcus sp strain PCC7942. Plant Cell 6: 1107-1121
    • (1994) Plant Cell , vol.6 , pp. 1107-1121
    • Cunningham Jr., F.X.1    Sun, Z.2    Chamovitz, D.3    Hirschberg, J.4    Gantt, E.5
  • 28
    • 0021875256 scopus 로고
    • Sulfide-repressed, membrane-bound hydrogenase in the thermophilic facultative phototroph Chloroflexus aurantiacus
    • Drutschmann M and Klemme J-H (1985) Sulfide-repressed, membrane-bound hydrogenase in the thermophilic facultative phototroph Chloroflexus aurantiacus. FEMS Microbiol Lett 28: 231
    • (1985) FEMS Microbiol Lett , vol.28 , pp. 231
    • Drutschmann, M.1    Klemme, J.-H.2
  • 30
    • 0030880018 scopus 로고    scopus 로고
    • Isolation and pigment composition of the antenna system of four species of green sulfur bacteria
    • Francke C and Amesz J (1997) Isolation and pigment composition of the antenna system of four species of green sulfur bacteria. Photosynth Res 52: 137-146
    • (1997) Photosynth Res , vol.52 , pp. 137-146
    • Francke, C.1    Amesz, J.2
  • 32
    • 0034782745 scopus 로고    scopus 로고
    • Complex I: A chimaera of a redox and conformation-driven proton pump?
    • Friedrich T (2001) Complex I: a chimaera of a redox and conformation-driven proton pump? J Bioenerg Biomembr 33: 169-177
    • (2001) J Bioenerg Biomembr , vol.33 , pp. 169-177
    • Friedrich, T.1
  • 33
    • 0034637432 scopus 로고    scopus 로고
    • The respiratory complex I of bacteria, archaea, and eukarya and its module common with membrane-bound multisubunit hydrogenases
    • Friedrich T and Scheide D (2000) The respiratory complex I of bacteria, archaea, and eukarya and its module common with membrane-bound multisubunit hydrogenases. FEBS Lett 479: 1-5
    • (2000) FEBS Lett , vol.479 , pp. 1-5
    • Friedrich, T.1    Scheide, D.2
  • 35
    • 0035377523 scopus 로고    scopus 로고
    • Chromosomal gene inactivation in the green sulfur bacterium Chlorobium tepidum by natural transformation
    • Frigaard N-U and Bryant DA (2001) Chromosomal gene inactivation in the green sulfur bacterium Chlorobium tepidum by natural transformation. Appl Environ Microbiol 67: 2538-2544
    • (2001) Appl Environ Microbiol , vol.67 , pp. 2538-2544
    • Frigaard, N.-U.1    Bryant, D.A.2
  • 36
    • 0032967969 scopus 로고    scopus 로고
    • Oxygen uncouples light absorption by the chlorosome antenna and photosynthetic electron transfer in the green sulfur bacterium Chlorobium tepidum
    • Frigaard N-U and Matsuura K (1999) Oxygen uncouples light absorption by the chlorosome antenna and photosynthetic electron transfer in the green sulfur bacterium Chlorobium tepidum. Biochim Biophys Acta 1412: 108-117
    • (1999) Biochim Biophys Acta , vol.1412 , pp. 108-117
    • Frigaard, N.-U.1    Matsuura, K.2
  • 37
    • 0030978942 scopus 로고    scopus 로고
    • Quinones in chlorosomes of green sulfur bacteria and their role in the redox-dependent fluorescence studied in chlorosome-like bacteriochlorophyll c aggregates
    • Frigaard N-U, Takaichi S, Hirota M, Shimada K and Matsuura K (1997) Quinones in chlorosomes of green sulfur bacteria and their role in the redox-dependent fluorescence studied in chlorosome-like bacteriochlorophyll c aggregates. Arch Microbiol 167: 343-349
    • (1997) Arch Microbiol , vol.167 , pp. 343-349
    • Frigaard, N.-U.1    Takaichi, S.2    Hirota, M.3    Shimada, K.4    Matsuura, K.5
  • 38
    • 0032444952 scopus 로고    scopus 로고
    • Studies of the location and function of isoprenoid quinones in chlorosomes from green sulfur bacteria
    • Frigaard N-U, Matsuura K, Hirota M, Miller M and Cox RP (1998) Studies of the location and function of isoprenoid quinones in chlorosomes from green sulfur bacteria. Photosynth Res 58: 81-90
    • (1998) Photosynth Res , vol.58 , pp. 81-90
    • Frigaard, N.-U.1    Matsuura, K.2    Hirota, M.3    Miller, M.4    Cox, R.P.5
  • 39
    • 0032706760 scopus 로고    scopus 로고
    • Exogenous quinones inhibit photosynthetic electron transfer in Chloroflexus aurantiacus by specific quenching of the excited bacteriochlorophyll c antenna
    • Frigaard N-U, Tokita S and Matsuura K (1999) Exogenous quinones inhibit photosynthetic electron transfer in Chloroflexus aurantiacus by specific quenching of the excited bacteriochlorophyll c antenna. Biochim Biophys Acta 1413: 108-116
    • (1999) Biochim Biophys Acta , vol.1413 , pp. 108-116
    • Frigaard, N.-U.1    Tokita, S.2    Matsuura, K.3
  • 41
    • 0036267394 scopus 로고    scopus 로고
    • Chlorobium tepidum mutant lacking bacteriochlorophyll c made by inactivation of the bchK gene, encoding bacteriochlorophyll c synthase
    • Frigaard N-U, Voigt GD and Bryant DA (2002) Chlorobium tepidum mutant lacking bacteriochlorophyll c made by inactivation of the bchK gene, encoding bacteriochlorophyll c synthase. J Bacteriol 184: 3368-3376
    • (2002) J Bacteriol , vol.184 , pp. 3368-3376
    • Frigaard, N.-U.1    Voigt, G.D.2    Bryant, D.A.3
  • 42
    • 0347939597 scopus 로고    scopus 로고
    • Bacteriochlorophyll biosynthesis in green bacteria
    • Grimm B, Porra R, Rüdiger W and Scheer H (eds) Kluwer Academic Press (in press)
    • Frigaard N-U, Gomez Maqueo Chew A and Bryant DA (2003a) Bacteriochlorophyll biosynthesis in green bacteria. In: Grimm B, Porra R, Rüdiger W and Scheer H (eds) Biochemistry and Biophysics of Chlorophyll. Kluwer Academic Press (in press)
    • (2003) Biochemistry and Biophysics of Chlorophyll
    • Frigaard, N.-U.1    Gomez Maqueo Chew, A.2    Bryant, D.A.3
  • 44
    • 0002974255 scopus 로고    scopus 로고
    • Phylum BVI. Chloroflexi phy. nov.
    • Boone DR and Castenholz RW (eds) Springer, New York
    • Garrity GM and Holt JG (2001a) Phylum BVI. Chloroflexi phy. nov. In: Boone DR and Castenholz RW (eds) Bergey's Manual of Systematic Bacteriology, 2nd ed, Vol I, pp 427-446. Springer, New York
    • (2001) Bergey's Manual of Systematic Bacteriology, 2nd Ed , vol.1 , pp. 427-446
    • Garrity, G.M.1    Holt, J.G.2
  • 45
    • 0346678801 scopus 로고    scopus 로고
    • Phylum BXI. Chlorobi phy. nov.
    • Boone DR and Castenholz RW (eds) Springer, New York
    • Garrity GM and Holt JG (2001b) Phylum BXI. Chlorobi phy. nov. In: Boone DR and Castenholz RW (eds) Bergey's Manual of Systematic Bacteriology, 2nd ed, Vol I, pp 601-623. Springer, New York
    • (2001) Bergey's Manual of Systematic Bacteriology, 2nd Ed , vol.1 , pp. 601-623
    • Garrity, G.M.1    Holt, J.G.2
  • 46
    • 0036778294 scopus 로고    scopus 로고
    • Carotenoid isomerase: A tale of light and isomers
    • Giuliano G, Giliberto L and Rosati C (2002) Carotenoid isomerase: a tale of light and isomers. Trends Plant Sci 7: 427-429
    • (2002) Trends Plant Sci , vol.7 , pp. 427-429
    • Giuliano, G.1    Giliberto, L.2    Rosati, C.3
  • 47
    • 0346678807 scopus 로고
    • Hydrogenases of green bacteria
    • Olson JM, Ormerod JG, Amesz J, Stackebrandt E and Trüper HG (eds) Plenum Press, New York
    • Gogotov IN (1988) Hydrogenases of green bacteria. In: Olson JM, Ormerod JG, Amesz J, Stackebrandt E and Trüper HG (eds) Green Photosynthetic Bacteria, pp 165-172. Plenum Press, New York
    • (1988) Green Photosynthetic Bacteria , pp. 165-172
    • Gogotov, I.N.1
  • 48
    • 0025757901 scopus 로고
    • Hydrogen-production by model systems including hydrogenases from phototrophic bacteria
    • Gogotov IN, Zorin NA and Serebriakova LT (1991) Hydrogen-production by model systems including hydrogenases from phototrophic bacteria. Intl J Hydrog Ener 16: 393-396
    • (1991) Intl J Hydrog Ener , vol.16 , pp. 393-396
    • Gogotov, I.N.1    Zorin, N.A.2    Serebriakova, L.T.3
  • 49
    • 0034612350 scopus 로고    scopus 로고
    • Anaerobic chlorophyll isocyclic ring formation in Rhodobacter capsulatus requires a cobalamin cofactor
    • Gough SP, Petersen BO and Duus JØ (2000) Anaerobic chlorophyll isocyclic ring formation in Rhodobacter capsulatus requires a cobalamin cofactor. Proc Natl Acad Sci USA 97: 6908-6913
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 6908-6913
    • Gough, S.P.1    Petersen, B.O.2    Duus, J.Ø.3
  • 50
    • 0029093467 scopus 로고
    • Stable photobleaching of P840 in Chlorobium reaction center preparations: Presence of the 42-kDa bacteriochlorophyll a protein and a 17-kDa polypeptide
    • Hager-Braun C, Xie D-L, Jarosch U, Herold E, Büttner M, Zimmermann R, Deutzmann R, Hauska G and Nelson N (1995) Stable photobleaching of P840 in Chlorobium reaction center preparations: presence of the 42-kDa bacteriochlorophyll a protein and a 17-kDa polypeptide. Biochemistry 34: 9617-9624
    • (1995) Biochemistry , vol.34 , pp. 9617-9624
    • Hager-Braun, C.1    Xie, D.-L.2    Jarosch, U.3    Herold, E.4    Büttner, M.5    Zimmermann, R.6    Deutzmann, R.7    Hauska, G.8    Nelson, N.9
  • 52
    • 0035836695 scopus 로고    scopus 로고
    • A ribulose-1,5-bisphosphate carboxylase/oxygenase (RubisCO)-like protein from Chlorobium tepidum that is involved with sulfur metabolism and the response to oxidative stress
    • Hanson TE and Tabita FR (2001) A ribulose-1,5-bisphosphate carboxylase/oxygenase (RubisCO)-like protein from Chlorobium tepidum that is involved with sulfur metabolism and the response to oxidative stress. Proc Natl Acad Sci USA 98: 4397-4402
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 4397-4402
    • Hanson, T.E.1    Tabita, F.R.2
  • 54
    • 0032774213 scopus 로고    scopus 로고
    • Chlorobium ferrooxidans sp. nov., a phototrophic green sulfur bacterium that oxidizes ferrous iron in coculture with a 'Geospirillum' sp. strain
    • Heising S, Richter L, Ludwig W and Schink B (1999) Chlorobium ferrooxidans sp. nov., a phototrophic green sulfur bacterium that oxidizes ferrous iron in coculture with a 'Geospirillum' sp. strain. Arch Microbiol 172: 116-124
    • (1999) Arch Microbiol , vol.172 , pp. 116-124
    • Heising, S.1    Richter, L.2    Ludwig, W.3    Schink, B.4
  • 56
    • 0035045707 scopus 로고    scopus 로고
    • Horizontal transfer of the photosynthesis gene cluster and operon rearrangement in purple bacteria
    • Igarashi N, Harada J, Nagashima S, Matsuura K, Shimada K and Nagashima KVP (2001) Horizontal transfer of the photosynthesis gene cluster and operon rearrangement in purple bacteria. J Mol Evol 52: 333-341
    • (2001) J Mol Evol , vol.52 , pp. 333-341
    • Igarashi, N.1    Harada, J.2    Nagashima, S.3    Matsuura, K.4    Shimada, K.5    Nagashima, K.V.P.6
  • 57
    • 0002558837 scopus 로고
    • Taxonomy and physiology of phototrophic purple bacteria and green sulfur bacteria
    • Blankenship RE, Madigan, MT and Bauer CE (eds) Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Imhoff JF (1995) Taxonomy and physiology of phototrophic purple bacteria and green sulfur bacteria. In: Blankenship RE, Madigan, MT and Bauer CE (eds) Anoxygenic Photosynthetic Bacteria, pp 1-15. Kluwer Academic Publishers, Dordrecht, The Netherlands
    • (1995) Anoxygenic Photosynthetic Bacteria , pp. 1-15
    • Imhoff, J.F.1
  • 58
    • 0036009770 scopus 로고    scopus 로고
    • Cloning of tangerine from tomato reveals a carotenoid isomerase essential for the production of β-carotene and xanthophylls in plants
    • Isaacson T, Ronen G, Zamir D and Hirschberg J (2002) Cloning of tangerine from tomato reveals a carotenoid isomerase essential for the production of β-carotene and xanthophylls in plants. Plant Cell 14: 333-342
    • (2002) Plant Cell , vol.14 , pp. 333-342
    • Isaacson, T.1    Ronen, G.2    Zamir, D.3    Hirschberg, J.4
  • 59
    • 0024651705 scopus 로고
    • Purification and characterization of ATP:citrate lyase from Hydrogenobacter thermophilus TK-6
    • Ishii M, Igarashi Y and Kodama T (1989) Purification and characterization of ATP:citrate lyase from Hydrogenobacter thermophilus TK-6. J Bacteriol 171: 1788-1792
    • (1989) J Bacteriol , vol.171 , pp. 1788-1792
    • Ishii, M.1    Igarashi, Y.2    Kodama, T.3
  • 60
    • 0036230811 scopus 로고    scopus 로고
    • Kinetics of electron transfer between soluble cytochrome c-554 and purified reaction center complex from the green sulfur bacterium Chlorobium tepidum
    • Itoh M, Seo D, Sakurai H and Sétif P (2002) Kinetics of electron transfer between soluble cytochrome c-554 and purified reaction center complex from the green sulfur bacterium Chlorobium tepidum. Photosynth Res 71: 125-135
    • (2002) Photosynth Res , vol.71 , pp. 125-135
    • Itoh, M.1    Seo, D.2    Sakurai, H.3    Sétif, P.4
  • 61
    • 0034931141 scopus 로고    scopus 로고
    • Isolation and characterization of anaerobic ethylbenzene dehydrogenase, a novel Mo-Fe-S enzyme
    • Johnson HA, Pelletier DA and Spormann AM (2001) Isolation and characterization of anaerobic ethylbenzene dehydrogenase, a novel Mo-Fe-S enzyme. J Bacteriol 183: 4536-4542
    • (2001) J Bacteriol , vol.183 , pp. 4536-4542
    • Johnson, H.A.1    Pelletier, D.A.2    Spormann, A.M.3
  • 62
    • 0034836201 scopus 로고    scopus 로고
    • ATP-citrate lyase from the green sulfur bacterium Chlorobium limicola is a heteromeric enzyme composed of two distinct gene products
    • Kanao T, Fukui T, Atomi H and Imanaka T (2001) ATP-citrate lyase from the green sulfur bacterium Chlorobium limicola is a heteromeric enzyme composed of two distinct gene products. Eur J Biochem 268: 1670-1678
    • (2001) Eur J Biochem , vol.268 , pp. 1670-1678
    • Kanao, T.1    Fukui, T.2    Atomi, H.3    Imanaka, T.4
  • 63
    • 0036375568 scopus 로고    scopus 로고
    • Kinetic and biochemical analyses on the reaction mechanism of a bacterial ATP-citrate lyase
    • Kanao T, Fukui T, Atomi H and Imanaka T (2002a) Kinetic and biochemical analyses on the reaction mechanism of a bacterial ATP-citrate lyase. Eur J Biochem 269: 3409-3416
    • (2002) Eur J Biochem , vol.269 , pp. 3409-3416
    • Kanao, T.1    Fukui, T.2    Atomi, H.3    Imanaka, T.4
  • 64
    • 0036230979 scopus 로고    scopus 로고
    • Characterization of isocitrate dehydrogenase from the green sulfur bacterium Chlorobium limicola - A carbon dioxide-fixing enzyme in the reductive tricarboxylic acid cycle
    • Kanao T, Kawamura M, Fukui T, Atomi H and Imanaka T (2002b) Characterization of isocitrate dehydrogenase from the green sulfur bacterium Chlorobium limicola - a carbon dioxide-fixing enzyme in the reductive tricarboxylic acid cycle. Eur J Biochem 269: 1926-1931
    • (2002) Eur J Biochem , vol.269 , pp. 1926-1931
    • Kanao, T.1    Kawamura, M.2    Fukui, T.3    Atomi, H.4    Imanaka, T.5
  • 65
    • 0035970116 scopus 로고    scopus 로고
    • An unusual isopentenyl diphosphate isomerase found in the mevalonate pathway gene cluster from Streptomyces sp strain CL190
    • Kaneda K, Kuzuyama T, Takagi M, Hayakawa Y and Seto H (2001) An unusual isopentenyl diphosphate isomerase found in the mevalonate pathway gene cluster from Streptomyces sp strain CL190. Proc Natl Acad Sci USA 98: 932-937
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 932-937
    • Kaneda, K.1    Kuzuyama, T.2    Takagi, M.3    Hayakawa, Y.4    Seto, H.5
  • 66
    • 33748245323 scopus 로고
    • Iron-sulfur centers in the photosynthetic reaction center complex from Chlorobium vibrioforme. Differences from and similarities to the iron-sulfur centers in Photosystem I
    • Kjær B, Jung Y-S, Yu L, Golbeck JH and Scheller HV (1994) Iron-sulfur centers in the photosynthetic reaction center complex from Chlorobium vibrioforme. Differences from and similarities to the iron-sulfur centers in Photosystem I. Photosynth Res 41: 105-114
    • (1994) Photosynth Res , vol.41 , pp. 105-114
    • Kjær, B.1    Jung, Y.-S.2    Yu, L.3    Golbeck, J.H.4    Scheller, H.V.5
  • 67
    • 0034471456 scopus 로고    scopus 로고
    • Molecular evolution of lycopene cyclases involved in the formation of carotenoids with ionone end groups
    • Krubasik P and Sandmann G (2000) Molecular evolution of lycopene cyclases involved in the formation of carotenoids with ionone end groups. Biochem Soc Trans 28: 806-810
    • (2000) Biochem Soc Trans , vol.28 , pp. 806-810
    • Krubasik, P.1    Sandmann, G.2
  • 68
    • 0345517285 scopus 로고    scopus 로고
    • Functional analysis of genes from Streptomyces griseus involved in the synthesis of isorenieratene, a carotenoid with aromatic end groups, revealed a novel type of carotenoid desaturase
    • Krügel H, Krubasik P, Weber K, Saluz HP and Sandmann G (1999) Functional analysis of genes from Streptomyces griseus involved in the synthesis of isorenieratene, a carotenoid with aromatic end groups, revealed a novel type of carotenoid desaturase. Biochim Biophys Acta 1439: 57-64
    • (1999) Biochim Biophys Acta , vol.1439 , pp. 57-64
    • Krügel, H.1    Krubasik, P.2    Weber, K.3    Saluz, H.P.4    Sandmann, G.5
  • 69
    • 0033807082 scopus 로고    scopus 로고
    • Site-specific mutational analysis of a novel cysteine motif proposed to ligate the 4Fe-4S cluster in the iron-sulfur flavoprotein of the thermophilic methanoarchaeon Methanosarcina thermophila
    • Leartsakulpanich U, Antonkine ML and Ferry JG (2000) Site-specific mutational analysis of a novel cysteine motif proposed to ligate the 4Fe-4S cluster in the iron-sulfur flavoprotein of the thermophilic methanoarchaeon Methanosarcina thermophila. J Bacteriol 182: 5309-5316
    • (2000) J Bacteriol , vol.182 , pp. 5309-5316
    • Leartsakulpanich, U.1    Antonkine, M.L.2    Ferry, J.G.3
  • 70
    • 0346678797 scopus 로고    scopus 로고
    • A comparative study of the isocitrate dehydrogenases of Chlorobium limicola forma thiosulfatophilum and Rhodopseudomonas palustris
    • Lebedeva NV, Malinina NV and Ivanovsky RN (2002) A comparative study of the isocitrate dehydrogenases of Chlorobium limicola forma thiosulfatophilum and Rhodopseudomonas palustris. Microbiology 71: 657-661
    • (2002) Microbiology , vol.71 , pp. 657-661
    • Lebedeva, N.V.1    Malinina, N.V.2    Ivanovsky, R.N.3
  • 71
    • 0028265991 scopus 로고
    • Structural differences in chlorosomes from Chloroflexus aurantiacus grown under different conditions support the BChl c-binding function of the 5.7 kDa polypeptide
    • Lehmann RP, Brunisholz RA and Zuber H (1994) Structural differences in chlorosomes from Chloroflexus aurantiacus grown under different conditions support the BChl c-binding function of the 5.7 kDa polypeptide. FEBS Lett 342: 319-324
    • (1994) FEBS Lett , vol.342 , pp. 319-324
    • Lehmann, R.P.1    Brunisholz, R.A.2    Zuber, H.3
  • 72
    • 0034699320 scopus 로고    scopus 로고
    • Translocases: A bacterial tunnel for drugs and proteins
    • Lewis K (2000) Translocases: a bacterial tunnel for drugs and proteins. Curr Biol 10: R678-R681
    • (2000) Curr Biol , vol.10
    • Lewis, K.1
  • 73
    • 0031583476 scopus 로고    scopus 로고
    • Crystal structure of the bacteriochlorophyll a protein from Chlorobium tepidum
    • Li YF, Zhou WL, Blankenship RE and Allen JP (1997) Crystal structure of the bacteriochlorophyll a protein from Chlorobium tepidum. J Mol Biol 271: 456-471
    • (1997) J Mol Biol , vol.271 , pp. 456-471
    • Li, Y.F.1    Zhou, W.L.2    Blankenship, R.E.3    Allen, J.P.4
  • 75
    • 0034065733 scopus 로고    scopus 로고
    • Characterization of hydrogenase II from the hyperthermophilic archaeon Pyrococcus furiosus and assessment of its role in sulfur reduction
    • Ma K, Weiss R and Adams MWW (2000) Characterization of hydrogenase II from the hyperthermophilic archaeon Pyrococcus furiosus and assessment of its role in sulfur reduction. J Bacteriol 182: 1864-1871
    • (2000) J Bacteriol , vol.182 , pp. 1864-1871
    • Ma, K.1    Weiss, R.2    Adams, M.W.W.3
  • 77
    • 0035544126 scopus 로고    scopus 로고
    • Identification of a gene required for cis-to-trans carotene isomerization in carotenogenesis of the cyanobacterium Synechocystis sp. PCC 6803
    • Masamoto K, Wada H, Kaneko T and Takaichi S (2001) Identification of a gene required for cis-to-trans carotene isomerization in carotenogenesis of the cyanobacterium Synechocystis sp. PCC 6803. Plant Cell Physiol 42: 1398-1402
    • (2001) Plant Cell Physiol , vol.42 , pp. 1398-1402
    • Masamoto, K.1    Wada, H.2    Kaneko, T.3    Takaichi, S.4
  • 78
    • 0035219809 scopus 로고    scopus 로고
    • 2) and ubiquinone (coenzyme Q): A perspective on enzymatic mechanisms
    • 2) and ubiquinone (coenzyme Q): a perspective on enzymatic mechanisms. Vitam Horm 6: 173-218
    • (2001) Vitam Horm , vol.6 , pp. 173-218
    • Meganathan, R.1
  • 79
    • 0028876029 scopus 로고
    • Genomic heterogeneity in Chlorobium limicola: Chromosomic and plasmidic differences among strains
    • Méndez-Alvarez S, Pavón V, Esteve I, Guerrero R and Gaju N (1995) Genomic heterogeneity in Chlorobium limicola: chromosomic and plasmidic differences among strains. FEMS Microbiol Lett 134: 279-285
    • (1995) FEMS Microbiol Lett , vol.134 , pp. 279-285
    • Méndez-Alvarez, S.1    Pavón, V.2    Esteve, I.3    Guerrero, R.4    Gaju, N.5
  • 80
    • 0028814979 scopus 로고
    • Thylakoid membrane-bound, NADPH-specific pyridine-nucleotide dehydrogenase complex mediates cyclic electron-transport in the cyanobacterium Synechocystis sp PCC-68038
    • Mi HL, Endo T, Ogawa T and Asada K (1995) Thylakoid membrane-bound, NADPH-specific pyridine-nucleotide dehydrogenase complex mediates cyclic electron-transport in the cyanobacterium Synechocystis sp PCC-68038. Plant Cell Physiol 36: 661-668
    • (1995) Plant Cell Physiol , vol.36 , pp. 661-668
    • Mi, H.L.1    Endo, T.2    Ogawa, T.3    Asada, K.4
  • 82
    • 0011815964 scopus 로고    scopus 로고
    • Isolation and characterization of the B795 baseplate light-harvesting complex from the chlorosomes of Chloroflexus aurantiacus
    • Montaño GA, Wu H-M, Lin S, Brune DC and Blankenship RE (2001b) Isolation and characterization of the B795 baseplate light-harvesting complex from the chlorosomes of Chloroflexus aurantiacus. Biophys J: 30A
    • (2001) Biophys J
    • Montaño, G.A.1    Wu, H.-M.2    Lin, S.3    Brune, D.C.4    Blankenship, R.E.5
  • 83
    • 0002036520 scopus 로고
    • Membranes and chlorosomes of green bacteria: Structure, composition and development
    • Blankenship RE, Madigan MT and Bauer CE (eds) Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Oelze J and Golecki JR (1995) Membranes and chlorosomes of green bacteria: structure, composition and development. In: Blankenship RE, Madigan MT and Bauer CE (eds) Anoxygenic Photosynthetic Bacteria, pp 259-278. Kluwer Academic Publishers, Dordrecht, The Netherlands
    • (1995) Anoxygenic Photosynthetic Bacteria , pp. 259-278
    • Oelze, J.1    Golecki, J.R.2
  • 85
    • 0029044508 scopus 로고
    • Two molecules of cytochrome c function as the electron donors to P840 in the reaction center complex isolated from a green sulfur bacterium, Chlorobium tepidum
    • Oh-oka H, Kamei S, Matsubara H and Itoh S (1995b) Two molecules of cytochrome c function as the electron donors to P840 in the reaction center complex isolated from a green sulfur bacterium, Chlorobium tepidum. FEBS Lett 365: 30-34
    • (1995) FEBS Lett , vol.365 , pp. 30-34
    • Oh-oka, H.1    Kamei, S.2    Matsubara, H.3    Itoh, S.4
  • 86
    • 0032169698 scopus 로고    scopus 로고
    • z couples quinol oxidoreductase to the P840 reaction center complex in isolated membranes of the green sulfur bacterium Chlorobium tepidum
    • z couples quinol oxidoreductase to the P840 reaction center complex in isolated membranes of the green sulfur bacterium Chlorobium tepidum. Biochemistry 37: 12293-12300
    • (1998) Biochemistry , vol.37 , pp. 12293-12300
    • Oh-oka, H.1    Iwaki, M.2    Itoh, S.3
  • 87
    • 0001315253 scopus 로고
    • Photo-oxidation of membrane-bound and soluble cytochrome c in the green sulfur bacterium Chlorobium tepidum
    • Okumura N, Shimada K and Matsuura K (1994) Photo-oxidation of membrane-bound and soluble cytochrome c in the green sulfur bacterium Chlorobium tepidum. Photosynth Res 41: 125-134
    • (1994) Photosynth Res , vol.41 , pp. 125-134
    • Okumura, N.1    Shimada, K.2    Matsuura, K.3
  • 88
    • 0002053155 scopus 로고    scopus 로고
    • Chlorophyll organization and function in green photosynthetic bacteria
    • Olson JM (1998) Chlorophyll organization and function in green photosynthetic bacteria. Photochem Photobiol 67: 61-75
    • (1998) Photochem Photobiol , vol.67 , pp. 61-75
    • Olson, J.M.1
  • 91
    • 0027088857 scopus 로고
    • An extremely low-light-adapted phototrophic sulfur bacterium from the Black Sea
    • Overmann J, Cypionka H and Pfennig N (1992) An extremely low-light-adapted phototrophic sulfur bacterium from the Black Sea. Limnol Oceanogr 37: 150-155
    • (1992) Limnol Oceanogr , vol.37 , pp. 150-155
    • Overmann, J.1    Cypionka, H.2    Pfennig, N.3
  • 92
    • 0036009771 scopus 로고    scopus 로고
    • Identification of the carotenoid isomerase provides insight into carotenoid biosynthesis, prolamellar body formation and photomorphogenesis
    • Park H, Kreunen SS, Cuttriss AJ, DellaPenna D and Pogson BJ (2002) Identification of the carotenoid isomerase provides insight into carotenoid biosynthesis, prolamellar body formation and photomorphogenesis. Plant Cell 14: 321-332
    • (2002) Plant Cell , vol.14 , pp. 321-332
    • Park, H.1    Kreunen, S.S.2    Cuttriss, A.J.3    DellaPenna, D.4    Pogson, B.J.5
  • 93
    • 0014667934 scopus 로고
    • Quinones of the Chlorobacteriaceae - Properties and possible function
    • Powls R and Redfearn ER (1969) Quinones of the Chlorobacteriaceae - properties and possible function. Biochim Biophys Acta 172: 429-437
    • (1969) Biochim Biophys Acta , vol.172 , pp. 429-437
    • Powls, R.1    Redfearn, E.R.2
  • 94
    • 0036428728 scopus 로고    scopus 로고
    • Genes involved in the anaerobic degradation of ethylbenzene in a denitrifying bacterium, strain EbN1
    • Rabus R, Kube M, Beck A, Widdel F and Reinhardt R (2002) Genes involved in the anaerobic degradation of ethylbenzene in a denitrifying bacterium, strain EbN1. Arch Microbiol 178: 506-516
    • (2002) Arch Microbiol , vol.178 , pp. 506-516
    • Rabus, R.1    Kube, M.2    Beck, A.3    Widdel, F.4    Reinhardt, R.5
  • 96
    • 0344327081 scopus 로고    scopus 로고
    • The reaction center complex from the green sulfur bacterium Chlorobium tepidum: A structural analysis by scanning transmission electron microscopy
    • Rémigy HW, Stahlberg H, Fotiadis D, Muller SA, Wolpensinger B, Engel A, Hauska G and Tsiotis G (1999) The reaction center complex from the green sulfur bacterium Chlorobium tepidum: A structural analysis by scanning transmission electron microscopy. J Mol Biol 290: 851-858
    • (1999) J Mol Biol , vol.290 , pp. 851-858
    • Rémigy, H.W.1    Stahlberg, H.2    Fotiadis, D.3    Muller, S.A.4    Wolpensinger, B.5    Engel, A.6    Hauska, G.7    Tsiotis, G.8
  • 97
    • 0036851226 scopus 로고    scopus 로고
    • Elucidation of the methylerythritol phosphate pathway for isoprenoid biosynthesis in bacteria and plastids. A metabolic milestone achieved through genomics
    • Rodríguez-Concepción M and Boronat A (2002) Elucidation of the methylerythritol phosphate pathway for isoprenoid biosynthesis in bacteria and plastids. A metabolic milestone achieved through genomics. Plant Physiol 130: 1079-1089
    • (2002) Plant Physiol , vol.130 , pp. 1079-1089
    • Rodríguez-Concepción, M.1    Boronat, A.2
  • 100
    • 0037194438 scopus 로고    scopus 로고
    • The cytochrome complex SoxXA of Paracoccus pantotrophus is produced in Escherichia coli and functional in the reconstituted sulfur-oxidizing enzyme system
    • Rother D and Friedrich CG (2002) The cytochrome complex SoxXA of Paracoccus pantotrophus is produced in Escherichia coli and functional in the reconstituted sulfur-oxidizing enzyme system. Biochim Biophys Acta 1598: 65-73
    • (2002) Biochim Biophys Acta , vol.1598 , pp. 65-73
    • Rother, D.1    Friedrich, C.G.2
  • 101
    • 0032732683 scopus 로고    scopus 로고
    • Association of bacteriochlorophyll a with the CsmA protein in chlorosomes of the photosynthetic green filamentous bacterium Chloroflexus aurantiacus
    • Sakuragi Y, Frigaard N-U, Shimada K and Matsuura K (1999) Association of bacteriochlorophyll a with the CsmA protein in chlorosomes of the photosynthetic green filamentous bacterium Chloroflexus aurantiacus. Biochim Biophys Acta 1413: 172-180
    • (1999) Biochim Biophys Acta , vol.1413 , pp. 172-180
    • Sakuragi, Y.1    Frigaard, N.-U.2    Shimada, K.3    Matsuura, K.4
  • 102
    • 0029824759 scopus 로고    scopus 로고
    • Function of the reaction center of green sulfur bacteria
    • Sakurai H, Kusumoto N and Inoue K (1996) Function of the reaction center of green sulfur bacteria. Photochem Photobiol 64: 5-13
    • (1996) Photochem Photobiol , vol.64 , pp. 5-13
    • Sakurai, H.1    Kusumoto, N.2    Inoue, K.3
  • 103
    • 0000657055 scopus 로고
    • Carbon assimilation pathways in sulfate-reducing bacteria. II. Enzymes of a reductive citric acid cycle in the autotrophic Desulfobacter hydrogenophilus
    • Schauder R, Widdel F and Fuchs G (1987) Carbon assimilation pathways in sulfate-reducing bacteria. II. Enzymes of a reductive citric acid cycle in the autotrophic Desulfobacter hydrogenophilus. Arch Microbiol 148: 218-225
    • (1987) Arch Microbiol , vol.148 , pp. 218-225
    • Schauder, R.1    Widdel, F.2    Fuchs, G.3
  • 104
    • 0037156874 scopus 로고    scopus 로고
    • HoxE - A subunit specific for the pentameric bidirectional hydrogenase complex (HoxEFUYH) of cyanobacteria
    • Schmitz O, Boison G, Salzmann H, Bothe H, Schütz K, Wang SH and Happe T (2002) HoxE - a subunit specific for the pentameric bidirectional hydrogenase complex (HoxEFUYH) of cyanobacteria. Biochim Biophys Acta 1554: 66-74
    • (2002) Biochim Biophys Acta , vol.1554 , pp. 66-74
    • Schmitz, O.1    Boison, G.2    Salzmann, H.3    Bothe, H.4    Schütz, K.5    Wang, S.H.6    Happe, T.7
  • 106
    • 0030609820 scopus 로고    scopus 로고
    • Redox titration of two [4Fe-4S] clusters in the photosynthetic reaction center from the anaerobic green sulfur bacterium Chlorobium vibrioforme
    • Scott MP, Kjær B, Scheller HV and Golbeck JH (1997) Redox titration of two [4Fe-4S] clusters in the photosynthetic reaction center from the anaerobic green sulfur bacterium Chlorobium vibrioforme. Eur J Biochem 244: 454-461
    • (1997) Eur J Biochem , vol.244 , pp. 454-461
    • Scott, M.P.1    Kjær, B.2    Scheller, H.V.3    Golbeck, J.H.4
  • 108
    • 0000392630 scopus 로고
    • Biosynthesis and structures of the bacteriochlorophylls
    • Blankenship RE, Madigan MT and Bauer CE (eds) Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Senge MO and Smith KM (1995) Biosynthesis and structures of the bacteriochlorophylls. In: Blankenship RE, Madigan MT and Bauer CE (eds) Anoxygenic Photosynthetic Bacteria, pp 137-151. Kluwer Academic Publishers, Dordrecht, The Netherlands
    • (1995) Anoxygenic Photosynthetic Bacteria , pp. 137-151
    • Senge, M.O.1    Smith, K.M.2
  • 109
    • 0037140926 scopus 로고    scopus 로고
    • + reductase from the green sulfur bacterium Chlorobium tepidum
    • + reductase from the green sulfur bacterium Chlorobium tepidum. Biochim Biophys Acta 1597: 123-132
    • (2002) Biochim Biophys Acta , vol.1597 , pp. 123-132
    • Seo, D.1    Sakurai, H.2
  • 110
    • 0035910655 scopus 로고    scopus 로고
    • Purification of ferredoxins and their reaction with purified reaction center complex from the green sulfur bacterium Chlorobium tepidum
    • Seo D, Tomioka A, Kusumoto N, Kamo M, Enami I and Sakurai H (2001) Purification of ferredoxins and their reaction with purified reaction center complex from the green sulfur bacterium Chlorobium tepidum. Biochim Biophys Acta 1503: 377-384
    • (2001) Biochim Biophys Acta , vol.1503 , pp. 377-384
    • Seo, D.1    Tomioka, A.2    Kusumoto, N.3    Kamo, M.4    Enami, I.5    Sakurai, H.6
  • 111
    • 0034801545 scopus 로고    scopus 로고
    • Analysis of the Desulfovibrio gigas transcriptional unit containing rubredoxin (rd) and rubredoxin-oxygen oxidoreductase (roo) genes and upstream ORFs
    • Silva G, Oliveira S, Le Gall J, Xavier AV and Rodrigues-Pousada C (2001) Analysis of the Desulfovibrio gigas transcriptional unit containing rubredoxin (rd) and rubredoxin-oxygen oxidoreductase (roo) genes and upstream ORFs. Biochem Biophys Res Commun 280: 491-502
    • (2001) Biochem Biophys Res Commun , vol.280 , pp. 491-502
    • Silva, G.1    Oliveira, S.2    Le Gall, J.3    Xavier, A.V.4    Rodrigues-Pousada, C.5
  • 112
    • 0038015923 scopus 로고
    • Carbon metabolism in green bacteria
    • Blankenship RE, Madigan MT and Bauer CE (eds) Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Sirevåg R (1995) Carbon metabolism in green bacteria. In: Blankenship RE, Madigan MT and Bauer CE (eds) Anoxygenic Photosynthetic Bacteria, pp 871-883. Kluwer Academic Publishers, Dordrecht, The Netherlands
    • (1995) Anoxygenic Photosynthetic Bacteria , pp. 871-883
    • Sirevåg, R.1
  • 113
    • 0000111789 scopus 로고
    • The biochemistry and molecular regulation of carbon dioxide metabolism in cyanobacteria
    • Bryant DA (ed) Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Tabita FR (1994) The biochemistry and molecular regulation of carbon dioxide metabolism in cyanobacteria. In: Bryant DA (ed) The Molecular Biology of Cyanobacteria, pp 437-467. Kluwer Academic Publishers, Dordrecht, The Netherlands
    • (1994) The Molecular Biology of Cyanobacteria , pp. 437-467
    • Tabita, F.R.1
  • 114
    • 0032807049 scopus 로고    scopus 로고
    • Pigment composition in the reaction center complex from the thermophilic green sulfur bacterium, Chlorobium tepidum: Carotenoid glucoside esters, menaquinone and chlorophylls
    • Takaichi S and Oh-oka H (1999) Pigment composition in the reaction center complex from the thermophilic green sulfur bacterium, Chlorobium tepidum: Carotenoid glucoside esters, menaquinone and chlorophylls. Plant Cell Physiol 40: 691-694
    • (1999) Plant Cell Physiol , vol.40 , pp. 691-694
    • Takaichi, S.1    Oh-oka, H.2
  • 115
    • 0008870125 scopus 로고
    • A novel carotenoid glucoside ester in green filamentous bacteria
    • Mathis P (ed) Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Takaichi S, Tsuji K, Hanada S, Matsuura K and Shimada K (1995) A novel carotenoid glucoside ester in green filamentous bacteria. In: Mathis P (ed) Photosynthesis: from Light to Biosphere, Vol IV, pp 127-130. Kluwer Academic Publishers, Dordrecht, The Netherlands
    • (1995) Photosynthesis: From Light to Biosphere , vol.4 , pp. 127-130
    • Takaichi, S.1    Tsuji, K.2    Hanada, S.3    Matsuura, K.4    Shimada, K.5
  • 116
    • 0030774641 scopus 로고    scopus 로고
    • New carotenoids from the thermophilic green sulfur bacterium Chlorobium tepidum: 1′,2′-dihydro-γ-carotene, 1′,2′- dihydrochlorobactene and OH-chlorobactene glucoside ester and the carotenoid composition of different strains
    • Takaichi S, Wang ZY, Umetsu M, Nozawa T, Shimada K and Madigan MT (1997) New carotenoids from the thermophilic green sulfur bacterium Chlorobium tepidum: 1′,2′-dihydro-γ-carotene, 1′,2′- dihydrochlorobactene and OH-chlorobactene glucoside ester and the carotenoid composition of different strains. Arch Microbiol 168: 270-276
    • (1997) Arch Microbiol , vol.168 , pp. 270-276
    • Takaichi, S.1    Wang, Z.Y.2    Umetsu, M.3    Nozawa, T.4    Shimada, K.5    Madigan, M.T.6
  • 118
    • 4244027594 scopus 로고
    • Metabolism of thiosulfate in Chlorobium
    • Olson JM, Ormerod JG, Amesz J, Stackebrandt E and Trüper HG (eds) Plenum Press, New York
    • Trüper HG, Lorenz C, Schedel M and Steinmetz (1988) Metabolism of thiosulfate in Chlorobium. In: Olson JM, Ormerod JG, Amesz J, Stackebrandt E and Trüper HG (eds) Green Photosynthetic Bacteria, pp 189-200. Plenum Press, New York
    • (1988) Green Photosynthetic Bacteria , pp. 189-200
    • Trüper, H.G.1    Lorenz, C.2    Schedel, M.3    Steinmetz4
  • 119
    • 0031030756 scopus 로고    scopus 로고
    • Redox effects on the excited-state lifetime in chlorosomes and bacteriochlorophyll c oligomers
    • van Noort PI, Zhu YW, LoBrutto R and Blankenship RE (1997) Redox effects on the excited-state lifetime in chlorosomes and bacteriochlorophyll c oligomers. Biophys J 72: 316-325
    • (1997) Biophys J , vol.72 , pp. 316-325
    • Van Noort, P.I.1    Zhu, Y.W.2    LoBrutto, R.3    Blankenship, R.E.4
  • 120
    • 0003026141 scopus 로고    scopus 로고
    • Chlorosomes: The light-harvesting complexes of the green bacteria
    • Vassilieva EV, Frigaard N-U and Bryant DA (2000) Chlorosomes: the light-harvesting complexes of the green bacteria. Spectrum 13: 7-13
    • (2000) Spectrum , vol.13 , pp. 7-13
    • Vassilieva, E.V.1    Frigaard, N.-U.2    Bryant, D.A.3
  • 121
    • 0035895361 scopus 로고    scopus 로고
    • Electron transfer may occur in the chlorosome envelope: The CsmI and CsmJ proteins of chlorosomes are 2Fe-2S ferredoxins
    • Vassilieva EV, Antonkine ML, Zybailov BL, Yang F, Jakobs C, Golbeck GH and Bryant DA (2001) Electron transfer may occur in the chlorosome envelope: the CsmI and CsmJ proteins of chlorosomes are 2Fe-2S ferredoxins. Biochemistry 40: 464-473
    • (2001) Biochemistry , vol.40 , pp. 464-473
    • Vassilieva, E.V.1    Antonkine, M.L.2    Zybailov, B.L.3    Yang, F.4    Jakobs, C.5    Golbeck, G.H.6    Bryant, D.A.7
  • 122
    • 0037006972 scopus 로고    scopus 로고
    • Subcellular localization of chlorosome proteins in Chlorobium tepidum and characterization of three new chlorosome proteins: CsmF, CsmH, and CsmX
    • Vassilieva EV, Stirewalt VL, Jakobs CU, Frigaard N-U, Inoue-Sakamoto K, Baker MA, Sotak A and Bryant DA (2002) Subcellular localization of chlorosome proteins in Chlorobium tepidum and characterization of three new chlorosome proteins: CsmF, CsmH, and CsmX. Biochemistry 41: 4358-4300
    • (2002) Biochemistry , vol.41 , pp. 4358-14300
    • Vassilieva, E.V.1    Stirewalt, V.L.2    Jakobs, C.U.3    Frigaard, N.-U.4    Inoue-Sakamoto, K.5    Baker, M.A.6    Sotak, A.7    Bryant, D.A.8
  • 123
    • 0037022824 scopus 로고    scopus 로고
    • Identification of a thiosulfate utilization gene cluster from the green phototrophic bacterium Chlorobium limicola
    • Verte F, Kostanjevecki V, De Smet L, Meyer TE, Cusanovich MA and Van Beeumen JJ (2002) Identification of a thiosulfate utilization gene cluster from the green phototrophic bacterium Chlorobium limicola. Biochemistry. 41: 2932-2945
    • (2002) Biochemistry , vol.41 , pp. 2932-2945
    • Verte, F.1    Kostanjevecki, V.2    De Smet, L.3    Meyer, T.E.4    Cusanovich, M.A.5    Van Beeumen, J.J.6
  • 124
  • 126
    • 0029057760 scopus 로고
    • Genetic transfer by conjugation in the thermophilic green sulfur bacterium Chlorobium tepidum
    • Wahlund TM and Madigan MT (1995) Genetic transfer by conjugation in the thermophilic green sulfur bacterium Chlorobium tepidum. J Bacteriol 177: 2583-2588
    • (1995) J Bacteriol , vol.177 , pp. 2583-2588
    • Wahlund, T.M.1    Madigan, M.T.2
  • 127
    • 0030802448 scopus 로고    scopus 로고
    • The reductive tricarboxylic acid cycle of carbon dioxide assimilation: Initial studies and purification of ATP-citrate lyase from the green sulfur bacterium Chlorobium tepidum
    • Wahlund TM and Tabita FR (1997) The reductive tricarboxylic acid cycle of carbon dioxide assimilation: initial studies and purification of ATP-citrate lyase from the green sulfur bacterium Chlorobium tepidum. J Bacteriol 179: 4859-4867
    • (1997) J Bacteriol , vol.179 , pp. 4859-4867
    • Wahlund, T.M.1    Tabita, F.R.2
  • 128
    • 0025813511 scopus 로고
    • A thermophilic green sulfur bacterium from New Zealand hot springs, Chlorobium tepidum sp. nov.
    • Wahlund TM, Woese CR, Castenholz RW and Madigan MT (1991) A thermophilic green sulfur bacterium from New Zealand hot springs, Chlorobium tepidum sp. nov. Arch Microbiol 156: 81-90
    • (1991) Arch Microbiol , vol.156 , pp. 81-90
    • Wahlund, T.M.1    Woese, C.R.2    Castenholz, R.W.3    Madigan, M.T.4
  • 129
    • 0026590069 scopus 로고
    • 2 from acetate by syntrophic cocultures of green sulfur bacteria and sulfur-reducing bacteria
    • 2 from acetate by syntrophic cocultures of green sulfur bacteria and sulfur-reducing bacteria. Arch Microbiol 157: 343-348
    • (1992) Arch Microbiol , vol.157 , pp. 343-348
    • Warthmann, R.1    Cypionka, H.2    Pfennig, N.3
  • 130
    • 0027519561 scopus 로고
    • The gene locus of the proton-translocating NADH:ubiquinone oxidoreductase of Escherichia coli. Organization of the 14 genes and relationship between the derived proteins and subunits of mitochondrial complex I
    • Weidner U, Geier S, Ptock A, Friedrich T, Leif H and Weiss H (1993) The gene locus of the proton-translocating NADH:ubiquinone oxidoreductase of Escherichia coli. Organization of the 14 genes and relationship between the derived proteins and subunits of mitochondrial complex I. J Mol Biol 233: 109-122
    • (1993) J Mol Biol , vol.233 , pp. 109-122
    • Weidner, U.1    Geier, S.2    Ptock, A.3    Friedrich, T.4    Leif, H.5    Weiss, H.6
  • 131
    • 0036414764 scopus 로고    scopus 로고
    • A cytochrome b origin of photosynthetic reaction centers: An evolutionary link between respiration and photosynthesis
    • Xiong J and Bauer CE (2002a) A cytochrome b origin of photosynthetic reaction centers: an evolutionary link between respiration and photosynthesis. J Mol Biol 322: 1025-1037
    • (2002) J Mol Biol , vol.322 , pp. 1025-1037
    • Xiong, J.1    Bauer, C.E.2
  • 132
    • 0037001963 scopus 로고    scopus 로고
    • Complex evolution of photosynthesis
    • Xiong J and Bauer CE (2002b) Complex evolution of photosynthesis. Annu Rev Plant Biol 53: 503-521
    • (2002) Annu Rev Plant Biol , vol.53 , pp. 503-521
    • Xiong, J.1    Bauer, C.E.2
  • 133
    • 0032424309 scopus 로고    scopus 로고
    • Tracking molecular evolution of photosynthesis by characterization of a major photosynthesis gene cluster from Heliobacillus mobilis
    • Xiong J, Inoue K and Bauer CE (1998) Tracking molecular evolution of photosynthesis by characterization of a major photosynthesis gene cluster from Heliobacillus mobilis. PNAS USA 95: 14851-14856
    • (1998) PNAS USA , vol.95 , pp. 14851-14856
    • Xiong, J.1    Inoue, K.2    Bauer, C.E.3
  • 134
    • 0034622999 scopus 로고    scopus 로고
    • Molecular evidence for the early evolution of photosynthesis
    • Xiong J, Fischer WM, Inoue K, Nakahara M and Bauer CE (2000) Molecular evidence for the early evolution of photosynthesis. Science 289: 1724-1730
    • (2000) Science , vol.289 , pp. 1724-1730
    • Xiong, J.1    Fischer, W.M.2    Inoue, K.3    Nakahara, M.4    Bauer, C.E.5
  • 135
    • 0033570050 scopus 로고    scopus 로고
    • Rubredoxin from the green sulfur bacterium Chlorobium tepidum functions as an electron acceptor for pyruvate ferredoxin oxidoreductase
    • Yoon KS, Hille R, Hemann C and Tabita FR (1999) Rubredoxin from the green sulfur bacterium Chlorobium tepidum functions as an electron acceptor for pyruvate ferredoxin oxidoreductase. J Biol Chem 274: 29772-29778
    • (1999) J Biol Chem , vol.274 , pp. 29772-29778
    • Yoon, K.S.1    Hille, R.2    Hemann, C.3    Tabita, F.R.4
  • 136
    • 0035941189 scopus 로고    scopus 로고
    • Spectroscopic and functional properties of novel 2[4Fe-4S] cluster-containing ferredoxins from the green sulfur bacterium Chlorobium tepidum
    • Yoon KS, Bobst C, Hemann CF, Hille R and Tabita FR (2001) Spectroscopic and functional properties of novel 2[4Fe-4S] cluster-containing ferredoxins from the green sulfur bacterium Chlorobium tepidum. J Biol Chem 276: 44027-44036
    • (2001) J Biol Chem , vol.276 , pp. 44027-44036
    • Yoon, K.S.1    Bobst, C.2    Hemann, C.F.3    Hille, R.4    Tabita, F.R.5
  • 137
    • 0035685613 scopus 로고    scopus 로고
    • Iron-sulfur flavoprotein (Isf) from Methanosarcina thermophila is the prototype of a widely distributed family
    • Zhao T, Cruz F and Ferry JG (2001) Iron-sulfur flavoprotein (Isf) from Methanosarcina thermophila is the prototype of a widely distributed family. J Bacteriol 183: 6225-6233
    • (2001) J Bacteriol , vol.183 , pp. 6225-6233
    • Zhao, T.1    Cruz, F.2    Ferry, J.G.3
  • 138
    • 0034282542 scopus 로고    scopus 로고
    • Structure of the ArsA ATPase: The catalytic subunit of a heavy metal resistance pump
    • Zhou TQ, Radaev S, Rosen BP and Gatti DL (2000) Structure of the ArsA ATPase: the catalytic subunit of a heavy metal resistance pump. EMBO J 19: 4838-4845
    • (2000) EMBO J , vol.19 , pp. 4838-4845
    • Zhou, T.Q.1    Radaev, S.2    Rosen, B.P.3    Gatti, D.L.4


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