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Volumn 8, Issue 1, 2013, Pages

Genomic Analysis of Melioribacter roseus, Facultatively Anaerobic Organotrophic Bacterium Representing a Novel Deep Lineage within Bacteriodetes/Chlorobi Group

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CARBOHYDRATE; CARBOHYDRATE ESTERASE; ESTERASE; GLYCOSIDASE; GLYCOSIDE TRANSFERASE; POLYSACCHARIDE LYASE; PROTEOME; TRANSFERASE; UNCLASSIFIED DRUG;

EID: 84871773633     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0053047     Document Type: Article
Times cited : (52)

References (69)
  • 1
    • 56649090649 scopus 로고    scopus 로고
    • The Family Chlorobiaceae
    • In: Dworkin M, Falkow S, Rosenberg E, Schleifer KH, Stackebrandt E, editors. Dordrecht: Springer
    • Overmann J (2006) The Family Chlorobiaceae. In: Dworkin M, Falkow S, Rosenberg E, Schleifer KH, Stackebrandt E, editors. The Prokaryotes. Vol. 7. Dordrecht: Springer. 359-380.
    • (2006) The Prokaryotes , vol.7 , pp. 359-380
    • Overmann, J.1
  • 2
    • 33749548848 scopus 로고    scopus 로고
    • Prokaryotic photosynthesis and phototrophy illuminated
    • Bryant DA, Frigaard NU, (2006) Prokaryotic photosynthesis and phototrophy illuminated. Trends Microbiol 14: 488-496.
    • (2006) Trends Microbiol , vol.14 , pp. 488-496
    • Bryant, D.A.1    Frigaard, N.U.2
  • 3
    • 0000400103 scopus 로고
    • Antenna complexes from green photosynthetic bacteria
    • In: Blankenship RE, Madigan MT, Bauer CE, editors. Kluwer, Dordrecht
    • Blankenship RE, Olson JM, Miller M (1995) Antenna complexes from green photosynthetic bacteria. In: Blankenship RE, Madigan MT, Bauer CE, editors. Anoxygenic photosynthetic bacteria. Kluwer, Dordrecht, 399-435.
    • (1995) Anoxygenic photosynthetic bacteria , pp. 399-435
    • Blankenship, R.E.1    Olson, J.M.2    Miller, M.3
  • 4
    • 0027509458 scopus 로고
    • Nitrogen fixation by the thermophilic green sulfur bacterium Chlorobium tepidum
    • Wahlund TM, Madigan MT, (1993) Nitrogen fixation by the thermophilic green sulfur bacterium Chlorobium tepidum. J Bacteriol 175: 474-478.
    • (1993) J Bacteriol , vol.175 , pp. 474-478
    • Wahlund, T.M.1    Madigan, M.T.2
  • 5
    • 0025697659 scopus 로고
    • A reverse KREBS cycle in photosynthesis: consensus at last
    • Buchanan BB, 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
  • 6
    • 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, 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
  • 7
    • 0346678801 scopus 로고    scopus 로고
    • Phylum BXI. Chlorobi phyl. nov
    • Boone DR, Castenholz RW, editors. 2nd edition, Springer
    • Garrity GM, Holt JG (2001) Phylum BXI. Chlorobi phyl. nov. In: Boone DR, Castenholz RW, editors. Bergey's Manual of Systematic Bacteriology, 2nd edition, Vol. 1. Springer. 601-623.
    • (2001) Bergey's Manual of Systematic Bacteriology , vol.1 , pp. 601-623
    • Garrity, G.M.1    Holt, J.G.2
  • 8
    • 0028055018 scopus 로고
    • The winds of (evolutionary) change: breathing new life into microbiology
    • Olsen GJ, Woese CR, Overbeek R, (1994) The winds of (evolutionary) change: breathing new life into microbiology. J Bacteriol 176: 1-6.
    • (1994) J Bacteriol , vol.176 , pp. 1-6
    • Olsen, G.J.1    Woese, C.R.2    Overbeek, R.3
  • 9
    • 0032080719 scopus 로고    scopus 로고
    • The phylogenetic relationships of Chlorobium tepidum and Chloroflexus auranticus based upon their RecA sequences
    • Gruber TM, Eisen JA, Gish K, Bryant DA, (1998) The phylogenetic relationships of Chlorobium tepidum and Chloroflexus auranticus based upon their RecA sequences. FEMS Microbiol Lett 162: 53-60.
    • (1998) FEMS Microbiol Lett , vol.162 , pp. 53-60
    • Gruber, T.M.1    Eisen, J.A.2    Gish, K.3    Bryant, D.A.4
  • 10
    • 2542465712 scopus 로고    scopus 로고
    • The phylogeny and signature sequences characteristics of Fibrobacters, Chlorobi and Bacteroidetes
    • Gupta RS, (2004) The phylogeny and signature sequences characteristics of Fibrobacters, Chlorobi and Bacteroidetes. Crit Rev Microbiol 30: 123-143.
    • (2004) Crit Rev Microbiol , vol.30 , pp. 123-143
    • Gupta, R.S.1
  • 11
    • 34249889555 scopus 로고    scopus 로고
    • Phylogeny and molecular signatures (conserved proteins and indels) that are specific for the Bacteroidetes and Chlorobi species
    • Gupta RS, Lorenzini E, (2007) Phylogeny and molecular signatures (conserved proteins and indels) that are specific for the Bacteroidetes and Chlorobi species. BMC Evol Biol 7: 71.
    • (2007) BMC Evol Biol , vol.7 , pp. 71
    • Gupta, R.S.1    Lorenzini, E.2
  • 12
    • 0028118435 scopus 로고
    • Phylogeny of Bacteroides, Prevotella, and Porphyromonas spp. and related bacteria
    • Paster BJ, Dewhirst FE, Olsen I, Fraser GJ, (1994) Phylogeny of Bacteroides, Prevotella, and Porphyromonas spp. and related bacteria. J Bacteriol 176: 725-732.
    • (1994) J Bacteriol , vol.176 , pp. 725-732
    • Paster, B.J.1    Dewhirst, F.E.2    Olsen, I.3    Fraser, G.J.4
  • 13
  • 14
    • 77953304160 scopus 로고    scopus 로고
    • Ignavibacterium album gen. nov., sp. nov., a moderately thermophilic anaerobic bacterium isolated from microbial mats at a terrestrial hot spring and proposal of Ignavibacteria classis nov., for a novel lineage at the periphery of green sulfur bacteria
    • Iino T, Mori K, Uchino Y, Nakagawa T, Harayama S, et al. (2010) Ignavibacterium album gen. nov., sp. nov., a moderately thermophilic anaerobic bacterium isolated from microbial mats at a terrestrial hot spring and proposal of Ignavibacteria classis nov., for a novel lineage at the periphery of green sulfur bacteria. Int J Syst Evol Microbiol 60: 1376-1382.
    • (2010) Int J Syst Evol Microbiol , vol.60 , pp. 1376-1382
    • Iino, T.1    Mori, K.2    Uchino, Y.3    Nakagawa, T.4    Harayama, S.5
  • 15
    • 84878658520 scopus 로고    scopus 로고
    • Characterization of Melioribacter roseus gen. nov., sp. nov. a novel facultatively anaerobic thermophilic cellulolytic bacterium from the class Ignavibacteria, and a proposal of a novel bacterial phylum Ignavibacteriae
    • (in press)
    • Podosokorskaya O, Kadnikov V, Gavrilov S, Mardanov A, Merkel A, et al. (2013) Characterization of Melioribacter roseus gen. nov., sp. nov., a novel facultatively anaerobic thermophilic cellulolytic bacterium from the class Ignavibacteria, and a proposal of a novel bacterial phylum Ignavibacteriae. Environ Microbiol (in press).
    • (2013) Environ Microbiol
    • Podosokorskaya, O.1    Kadnikov, V.2    Gavrilov, S.3    Mardanov, A.4    Merkel, A.5
  • 16
    • 84871764352 scopus 로고    scopus 로고
    • Complete genome of Ignavibacterium album, a metabolically versatile, flagellated, facultative anaerobe from the phylum Chlorobi
    • Liu Z, Frigaard N-U, Vogl K, Iino T, Ohkuma M, et al. (2012) Complete genome of Ignavibacterium album, a metabolically versatile, flagellated, facultative anaerobe from the phylum Chlorobi. Front Microbiol 3: 185.
    • (2012) Front Microbiol , vol.3 , pp. 185
    • Liu, Z.1    Frigaard, N.-U.2    Vogl, K.3    Iino, T.4    Ohkuma, M.5
  • 19
    • 0030854739 scopus 로고    scopus 로고
    • tRNAscan-SE: a program for improved detection of transfer RNA genes in genomic sequence
    • Lowe T, Eddy SR, (1997) tRNAscan-SE: a program for improved detection of transfer RNA genes in genomic sequence. Nucleic Acids Res 25: 955-964.
    • (1997) Nucleic Acids Res , vol.25 , pp. 955-964
    • Lowe, T.1    Eddy, S.R.2
  • 21
    • 25444458848 scopus 로고    scopus 로고
    • AutoFACT: an automatic functional annotation and classification tool
    • Koski LB, Gray MW, Langi BF, Burger G, (2005) AutoFACT: an automatic functional annotation and classification tool. BMC Bioinformatics 6: 151.
    • (2005) BMC Bioinformatics , vol.6 , pp. 151
    • Koski, L.B.1    Gray, M.W.2    Langi, B.F.3    Burger, G.4
  • 22
    • 34547579396 scopus 로고    scopus 로고
    • CRISPRFinder: a web tool to identify clustered regularly interspaced short palindromic repeats
    • Grissa I, Vergnaud G, Pourcel C (2007) CRISPRFinder: a web tool to identify clustered regularly interspaced short palindromic repeats. Nucleic Acids Res 35(Web Server issue): W52-57.
    • (2007) Nucleic Acids Res , vol.35 , Issue.Web Server issue , pp. 52-57
    • Grissa, I.1    Vergnaud, G.2    Pourcel, C.3
  • 24
    • 79957613599 scopus 로고    scopus 로고
    • MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods
    • Tamura K, Peterson D, Peterson N, Stecher G, Nei M, et al. (2011) MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods. Molec Biol Evol 28: 2731-2739.
    • (2011) Molec Biol Evol , vol.28 , pp. 2731-2739
    • Tamura, K.1    Peterson, D.2    Peterson, N.3    Stecher, G.4    Nei, M.5
  • 25
    • 34547489084 scopus 로고    scopus 로고
    • Improvement of phylogenies after removing divergent and ambiguously aligned blocks from protein sequence alignments
    • Talavera G, Castresana J, (2007) Improvement of phylogenies after removing divergent and ambiguously aligned blocks from protein sequence alignments. Syst Biol 56: 564-577.
    • (2007) Syst Biol , vol.56 , pp. 564-577
    • Talavera, G.1    Castresana, J.2
  • 26
    • 33750403801 scopus 로고    scopus 로고
    • RAxML-VI-HPC: maximum likelihood-based phylogenetic analyses with thousands of taxa and mixed models
    • Stamatakis A, (2006) RAxML-VI-HPC: maximum likelihood-based phylogenetic analyses with thousands of taxa and mixed models. Bioinformatics 22(21): 2688-2690.
    • (2006) Bioinformatics , vol.22 , Issue.21 , pp. 2688-2690
    • Stamatakis, A.1
  • 28
    • 16444385662 scopus 로고    scopus 로고
    • Intervening sequences of regularly spaced prokaryotic repeats derive from foreign genetic elements
    • Mojica FJ, Diez-Villasenor C, Garcia-Martinez J, Soria E, (2005) Intervening sequences of regularly spaced prokaryotic repeats derive from foreign genetic elements. J Mol Evol 60: 174-182.
    • (2005) J Mol Evol , vol.60 , pp. 174-182
    • Mojica, F.J.1    Diez-Villasenor, C.2    Garcia-Martinez, J.3    Soria, E.4
  • 29
    • 57149085868 scopus 로고    scopus 로고
    • Genomics of bacteria and archaea: the emerging dynamic view of the prokaryotic world
    • Koonin EV, Wolf YI, (2008) Genomics of bacteria and archaea: the emerging dynamic view of the prokaryotic world. Nucleic Acids Res 36: 6688-6719.
    • (2008) Nucleic Acids Res , vol.36 , pp. 6688-6719
    • Koonin, E.V.1    Wolf, Y.I.2
  • 30
    • 0037214767 scopus 로고    scopus 로고
    • Caldithrix abyssi gen. nov., sp. nov., a Nitrate-Reducing, Thermophilic, Anaerobic Bacterium Isolated from a Mid-Atlantic Ridge Hydrothermal Vent, Represents a Novel Bacterial Lineage
    • Miroshnichenko ML, Kostrikina NA, Chernyh NA, Pimenov NV, Tourova TP, et al. (2003) Caldithrix abyssi gen. nov., sp. nov., a nitrate-reducing, thermophilic, anaerobic bacterium isolated from a Mid-Atlantic Ridge hydrothermal vent, represents a novel bacterial lineage Int J Syst Evol Microbiol 53: 323-329.
    • (2003) Int J Syst Evol Microbiol , vol.53 , pp. 323-329
    • Miroshnichenko, M.L.1    Kostrikina, N.A.2    Chernyh, N.A.3    Pimenov, N.V.4    Tourova, T.P.5
  • 31
    • 0036315809 scopus 로고    scopus 로고
    • Phylogeny of green sulfur bacteria on the basis of gene sequences of 16S rRNA and of the Fenna-Matthews-Olson protein
    • Alexander B, Andersen JH, Cox RP, Imhoff JF, (2002) Phylogeny of green sulfur bacteria on the basis of gene sequences of 16S rRNA and of the Fenna-Matthews-Olson protein. Arch Microbiol 178: 131-140.
    • (2002) Arch Microbiol , vol.178 , pp. 131-140
    • Alexander, B.1    Andersen, J.H.2    Cox, R.P.3    Imhoff, J.F.4
  • 32
    • 84867747979 scopus 로고    scopus 로고
    • Candidatus Thermochlorobacter aerophilum:' an aerobic chlorophotoheterotrophic member of the phylum Chlorobi defined by metagenomics and metatranscriptomics
    • (in press)
    • Liu Z, Klatt CG, Ludwig M, Rusch DB, Jensen SI, et al. (2012) 'Candidatus Thermochlorobacter aerophilum:' an aerobic chlorophotoheterotrophic member of the phylum Chlorobi defined by metagenomics and metatranscriptomics. ISME J (in press).
    • (2012) ISME J
    • Liu, Z.1    Klatt, C.G.2    Ludwig, M.3    Rusch, D.B.4    Jensen, S.I.5
  • 35
    • 2442681858 scopus 로고    scopus 로고
    • The family 6 carbohydrate binding module CmCBM6-2 contains two ligand-binding sites with distinct specificities
    • Henshaw JL, Bolam DN, Pires VM, Czjzek M, Henrissat B, et al. (2004) The family 6 carbohydrate binding module CmCBM6-2 contains two ligand-binding sites with distinct specificities. J Biol Chem 279(20): 21552-21559.
    • (2004) J Biol Chem , vol.279 , Issue.20 , pp. 21552-21559
    • Henshaw, J.L.1    Bolam, D.N.2    Pires, V.M.3    Czjzek, M.4    Henrissat, B.5
  • 36
    • 34249901672 scopus 로고    scopus 로고
    • Recent insights into the activities of cellobiohydrolases from Cellulomonas fimi and other cellulolytic microorganisms
    • In Ohmiya K, Hayashi K, Sakka K, Kobayashi Y, Karita S, Kimura T, editors, Uni Publishers Co., Tokyo, Japan
    • Gilkes NR, Kilburn D, Kwan E, Mansfield S, Saddler J, et al. (1999) Recent insights into the activities of cellobiohydrolases from Cellulomonas fimi and other cellulolytic microorganisms. In Ohmiya K, Hayashi K, Sakka K, Kobayashi Y, Karita S, Kimura T, editors. Genetics, biochemistry and ecology of cellulose degradation. Uni Publishers Co., Tokyo, Japan, 24-34.
    • (1999) Genetics, biochemistry and ecology of cellulose degradation , pp. 24-34
    • Gilkes, N.R.1    Kilburn, D.2    Kwan, E.3    Mansfield, S.4    Saddler, J.5
  • 37
    • 0026477467 scopus 로고
    • Biochemistry and genetics of actinomycete cellulases
    • Wilson DB, (1992) Biochemistry and genetics of actinomycete cellulases. Crit Rev Biotechnol 12: 45-63.
    • (1992) Crit Rev Biotechnol , vol.12 , pp. 45-63
    • Wilson, D.B.1
  • 39
    • 68149099020 scopus 로고    scopus 로고
    • Evidence for a novel mechanism of microbial cellulose degradation
    • Wilson DB, (2009) Evidence for a novel mechanism of microbial cellulose degradation. Cellulose 16: 723-727.
    • (2009) Cellulose , vol.16 , pp. 723-727
    • Wilson, D.B.1
  • 40
    • 0033802036 scopus 로고    scopus 로고
    • Characterization of four outer membrane proteins involved in binding starch to the cell surface of Bacteroides thetaiotaomicron
    • Shipman JA, Berleman JE, Salyers AA, (2000) Characterization of four outer membrane proteins involved in binding starch to the cell surface of Bacteroides thetaiotaomicron. J Bacteriol 182: 5365-72.
    • (2000) J Bacteriol , vol.182 , pp. 5365-5372
    • Shipman, J.A.1    Berleman, J.E.2    Salyers, A.A.3
  • 41
    • 79955446915 scopus 로고    scopus 로고
    • The complete genome sequence of Fibrobacter succinogenes S85 reveals a cellulolytic and metabolic specialist
    • Suen G, Weimer PJ, Stevenson DM, Aylward FO, Boyum J, et al. (2011) The complete genome sequence of Fibrobacter succinogenes S85 reveals a cellulolytic and metabolic specialist. PLoS One 6(4): e18814.
    • (2011) PLoS One , vol.6 , Issue.4
    • Suen, G.1    Weimer, P.J.2    Stevenson, D.M.3    Aylward, F.O.4    Boyum, J.5
  • 42
    • 0034646192 scopus 로고    scopus 로고
    • Structure and binding specificity of the second N-terminal cellulose-binding domain from Cellulomonas fimi endoglucanase C
    • Brun E, Johnson PE, Creagh AL, Tomme P, Webster P, et al. (2000) Structure and binding specificity of the second N-terminal cellulose-binding domain from Cellulomonas fimi endoglucanase C. Biochemistry. 39(10): 2445-2258.
    • (2000) Biochemistry , vol.39 , Issue.10 , pp. 2258-2445
    • Brun, E.1    Johnson, P.E.2    Creagh, A.L.3    Tomme, P.4    Webster, P.5
  • 43
    • 0028901697 scopus 로고
    • Identification of a novel cellulose-binding domain within the multidomain 120 kDa xylanase XynA of the hyperthermophilic bacterium Thermotoga maritima
    • Winterhalter C, Heinrich P, Candussio A, Wich G, Liebl W, (1995) Identification of a novel cellulose-binding domain within the multidomain 120 kDa xylanase XynA of the hyperthermophilic bacterium Thermotoga maritima. Mol Microbiol 15: 431-444.
    • (1995) Mol Microbiol , vol.15 , pp. 431-444
    • Winterhalter, C.1    Heinrich, P.2    Candussio, A.3    Wich, G.4    Liebl, W.5
  • 45
    • 0031878285 scopus 로고    scopus 로고
    • Regulation of pectic enzymes from the exo-1 mutant strain of Neurospora crassa: effects of glucose, galactose, and galacturonic acid
    • Crotti LB, Terenzi HF, Jorge JA, de Lourdes M, Polizeli ML, (1998) Regulation of pectic enzymes from the exo-1 mutant strain of Neurospora crassa: effects of glucose, galactose, and galacturonic acid. J Basic Microbiol 38(3): 181-188.
    • (1998) J Basic Microbiol , vol.38 , Issue.3 , pp. 181-188
    • Crotti, L.B.1    Terenzi, H.F.2    Jorge, J.A.3    de Lourdes, M.4    Polizeli, M.L.5
  • 47
    • 33744778762 scopus 로고    scopus 로고
    • Bundle-forming pili and EspA are involved in biofilm formation by enteropathogenic Escherichia coli
    • Moreira CG, Palmer K, Whiteley M, Sircili MP, Trabulsi LR, et al. (2006) Bundle-forming pili and EspA are involved in biofilm formation by enteropathogenic Escherichia coli. J Bacteriol 188: 3952-3961.
    • (2006) J Bacteriol , vol.188 , pp. 3952-3961
    • Moreira, C.G.1    Palmer, K.2    Whiteley, M.3    Sircili, M.P.4    Trabulsi, L.R.5
  • 48
    • 27844506497 scopus 로고    scopus 로고
    • Type II secretion: a protein secretion system for all seasons
    • Cianciotto NP, (2005) Type II secretion: a protein secretion system for all seasons. Trends in Microbiol 13: 581-588.
    • (2005) Trends in Microbiol , vol.13 , pp. 581-588
    • Cianciotto, N.P.1
  • 49
    • 0029908371 scopus 로고    scopus 로고
    • Photosynthate partitioning and fermentation in hot spring microbial mat communities
    • Nold SC, Ward DM, (1996) Photosynthate partitioning and fermentation in hot spring microbial mat communities. Appl Environ Microbiol 62: 4598-4607.
    • (1996) Appl Environ Microbiol , vol.62 , pp. 4598-4607
    • Nold, S.C.1    Ward, D.M.2
  • 50
    • 0025000128 scopus 로고
    • The structure and mechanism of iron-hydrogenases
    • Adams MWW, (1990) The structure and mechanism of iron-hydrogenases. Biochim Biophys Acta 1020: 115-145.
    • (1990) Biochim Biophys Acta , vol.1020 , pp. 115-145
    • Adams, M.W.W.1
  • 51
    • 35748974830 scopus 로고    scopus 로고
    • Occurrence, classification, and biological function of hydrogenases: an overview
    • Vignais PM, Billoud B, (2007) Occurrence, classification, and biological function of hydrogenases: an overview. Chem Rev 107: 4206-4272.
    • (2007) Chem Rev , vol.107 , pp. 4206-4272
    • Vignais, P.M.1    Billoud, B.2
  • 52
    • 67649413347 scopus 로고    scopus 로고
    • The iron-hydrogenase of Thermotoga maritima utilizes ferredoxin and NADH synergistically: a new perspective on anaerobic hydrogen production
    • Schut GJ, Adams MW, (2009) The iron-hydrogenase of Thermotoga maritima utilizes ferredoxin and NADH synergistically: a new perspective on anaerobic hydrogen production. J Bacteriol 191: 4451-1457.
    • (2009) J Bacteriol , vol.191 , pp. 1457-4451
    • Schut, G.J.1    Adams, M.W.2
  • 53
    • 33847687662 scopus 로고    scopus 로고
    • Respiratory complex I: mechanistic and structural insights provided by the crystal structure of the hydrophilic domain
    • Sazanov LA, (2007) Respiratory complex I: mechanistic and structural insights provided by the crystal structure of the hydrophilic domain. Biochemistry 46: 2275-2288.
    • (2007) Biochemistry , vol.46 , pp. 2275-2288
    • Sazanov, L.A.1
  • 54
    • 78249274619 scopus 로고    scopus 로고
    • The specificity of proton-translocating transhydrogenase for nicotinamide nucleotides
    • Huxley L, Quirk PG, Cotton NP, White SA, Jackson JB, (2011) The specificity of proton-translocating transhydrogenase for nicotinamide nucleotides. Biochem Biophys Acta 1807: 85-94.
    • (2011) Biochem Biophys Acta , vol.1807 , pp. 85-94
    • Huxley, L.1    Quirk, P.G.2    Cotton, N.P.3    White, S.A.4    Jackson, J.B.5
  • 55
    • 34948894523 scopus 로고    scopus 로고
    • The alternative complex III from Rhodothermus marinus - a prototype of a new family of quinol:electron acceptor oxidoreductases, FEBS Lett
    • Pereira MM, Refojo PN, Hreggvidsson GO, Hjorleifsdottir S, Teixeira M, (2007) The alternative complex III from Rhodothermus marinus- a prototype of a new family of quinol:electron acceptor oxidoreductases, FEBS Lett. 581: 4831-4835.
    • (2007) , vol.581 , pp. 4831-4835
    • Pereira, M.M.1    Refojo, P.N.2    Hreggvidsson, G.O.3    Hjorleifsdottir, S.4    Teixeira, M.5
  • 57
    • 78149471622 scopus 로고    scopus 로고
    • The alternative complex III: a different architecture using known building modules
    • Refojo PN, Sousa FL, Teixeira M, Pereira MM, (2010) The alternative complex III: a different architecture using known building modules. Biochim Biophys Acta 1797: 1869-1876.
    • (2010) Biochim Biophys Acta , vol.1797 , pp. 1869-1876
    • Refojo, P.N.1    Sousa, F.L.2    Teixeira, M.3    Pereira, M.M.4
  • 58
    • 56249143434 scopus 로고    scopus 로고
    • A novel type of monoheme cytochrome c: biochemical and structural characterization at 1.23 A resolution of Rhodothermus marinus cytochrome c
    • Stelter M, Melo AM, Pereira MM, Gomes CM, Hreggvidsson GO, et al. (2008) A novel type of monoheme cytochrome c: biochemical and structural characterization at 1.23 A resolution of Rhodothermus marinus cytochrome c. Biochemistry 47: 11953-11963.
    • (2008) Biochemistry , vol.47 , pp. 11953-11963
    • Stelter, M.1    Melo, A.M.2    Pereira, M.M.3    Gomes, C.M.4    Hreggvidsson, G.O.5
  • 59
    • 0027131592 scopus 로고
    • Identification of a new class of nitrogen fixation genes in Rhodobacter capsulatus: a putative membrane complex involved in electron transport to nitrogenase
    • Schmehl M, Jahn A, Meyer zu Vilsendorf A, Hennecke S, Masepohl B, et al. (1993) Identification of a new class of nitrogen fixation genes in Rhodobacter capsulatus: a putative membrane complex involved in electron transport to nitrogenase. Mol Gen Genet 241: 602-615.
    • (1993) Mol Gen Genet , vol.241 , pp. 602-615
    • Schmehl, M.1    Jahn, A.2    Meyer zu Vilsendorf, A.3    Hennecke, S.4    Masepohl, B.5
  • 60
    • 0033962472 scopus 로고    scopus 로고
    • Enhanced nitrogenase activity in strains of Rhodobacter capsulatus that overexpress the rnf genes
    • Jeong HS, Jouanneau Y, (2000) Enhanced nitrogenase activity in strains of Rhodobacter capsulatus that overexpress the rnf genes. J Bacteriol 182: 1208-1214.
    • (2000) J Bacteriol , vol.182 , pp. 1208-1214
    • Jeong, H.S.1    Jouanneau, Y.2
  • 61
    • 78149247216 scopus 로고    scopus 로고
    • Bacterial Na+-translocating ferredoxin:NAD+oxidoreductase
    • Biegel E, Müller V, (2010) Bacterial Na+-translocating ferredoxin:NAD+oxidoreductase. Proc Natl Acad Sci USA 107: 18138-18142.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 18138-18142
    • Biegel, E.1    Müller, V.2
  • 62
    • 79951579402 scopus 로고    scopus 로고
    • Biochemistry, evolution and physiological function of the Rnf complex, a novel ion-motive electron transport complex in prokaryotes
    • Biegel E, Schmidt S, González JM, Müller V, (2011) Biochemistry, evolution and physiological function of the Rnf complex, a novel ion-motive electron transport complex in prokaryotes. Cell Mol Life Sci 68: 613-634.
    • (2011) Cell Mol Life Sci , vol.68 , pp. 613-634
    • Biegel, E.1    Schmidt, S.2    González, J.M.3    Müller, V.4
  • 63
    • 44649152990 scopus 로고    scopus 로고
    • The cbb3 oxidases are an ancient innovation of the domain bacteria
    • Ducluzeau AL, Ouchane S, Nitschke W, (2008) The cbb3 oxidases are an ancient innovation of the domain bacteria. Mol Biol Evol 25(6): 1158-1166.
    • (2008) Mol Biol Evol , vol.25 , Issue.6 , pp. 1158-1166
    • Ducluzeau, A.L.1    Ouchane, S.2    Nitschke, W.3
  • 64
    • 0036669911 scopus 로고    scopus 로고
    • Cytochrome cbb(3) oxidase and bacterial microaerobic metabolism
    • Pitcher RS, Brittain T, Watmough NJ, (2002) Cytochrome cbb(3) oxidase and bacterial microaerobic metabolism. Biochem Soc Trans 30: 653-658.
    • (2002) Biochem Soc Trans , vol.30 , pp. 653-658
    • Pitcher, R.S.1    Brittain, T.2    Watmough, N.J.3
  • 65
    • 84860681836 scopus 로고    scopus 로고
    • Biogenesis of cbb(3)-type cytochrome c oxidase in Rhodobacter capsulatus
    • Ekici S, Pawlik G, Lohmeyer E, Koch HG, Daldal F, (2012) Biogenesis of cbb(3)-type cytochrome c oxidase in Rhodobacter capsulatus. Biochim Biophys Acta 1817: 898-910.
    • (2012) Biochim Biophys Acta , vol.1817 , pp. 898-910
    • Ekici, S.1    Pawlik, G.2    Lohmeyer, E.3    Koch, H.G.4    Daldal, F.5
  • 66
    • 0035946912 scopus 로고    scopus 로고
    • The RegB/RegA two-component regulatory system controls synthesis of photosynthesis and respiratory electron transfer components in Rhodobacter capsulatus
    • Swem LR, Elsen S, Bird TH, Swem DL, Koch HG, et al. (2001) The RegB/RegA two-component regulatory system controls synthesis of photosynthesis and respiratory electron transfer components in Rhodobacter capsulatus. J Mol Biol 309: 121-138.
    • (2001) J Mol Biol , vol.309 , pp. 121-138
    • Swem, L.R.1    Elsen, S.2    Bird, T.H.3    Swem, D.L.4    Koch, H.G.5
  • 67
    • 50049103112 scopus 로고    scopus 로고
    • The prokaryotic complex iron-sulfur molybdoenzyme family
    • Rothery RA, Workun GJ, Weiner JH, (2008) The prokaryotic complex iron-sulfur molybdoenzyme family. Biochim Biophys Acta 1778: 1897-1929.
    • (2008) Biochim Biophys Acta , vol.1778 , pp. 1897-1929
    • Rothery, R.A.1    Workun, G.J.2    Weiner, J.H.3
  • 68
    • 0023258583 scopus 로고
    • Tetrathionate reduction and production of hydrogen sulfide from thiosulfate
    • Barrett EL, Clark MA, (1987) Tetrathionate reduction and production of hydrogen sulfide from thiosulfate. Microbiol Rev 51: 192-205.
    • (1987) Microbiol Rev , vol.51 , pp. 192-205
    • Barrett, E.L.1    Clark, M.A.2
  • 69
    • 76749118614 scopus 로고    scopus 로고
    • Microbial arsenic metabolism: new twists on an old poison
    • Stolz JF, Partha B, Oremland RS, (2010) Microbial arsenic metabolism: new twists on an old poison. Microbe 5(2): 53-59.
    • (2010) Microbe , vol.5 , Issue.2 , pp. 53-59
    • Stolz, J.F.1    Partha, B.2    Oremland, R.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.