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Volumn 16, Issue 11, 2014, Pages 3562-3580

Insights into organohalide respiration and the versatile catabolism of Sulfurospirillum multivorans gained from comparative genomics and physiological studies

Author keywords

[No Author keywords available]

Indexed keywords

SULFUROSPIRILLUM MULTIVORANS;

EID: 84911930262     PISSN: 14622912     EISSN: 14622920     Source Type: Journal    
DOI: 10.1111/1462-2920.12589     Document Type: Article
Times cited : (75)

References (128)
  • 1
    • 0034965129 scopus 로고    scopus 로고
    • Pyruvate oxidase contributes to the aerobic growth efficiency of Escherichia coli
    • Abdel-Hamid, A.M., Attwood, M.M., and Guest, J.R. (2001) Pyruvate oxidase contributes to the aerobic growth efficiency of Escherichia coli. Microbiology 147: 1483-1498.
    • (2001) Microbiology , vol.147 , pp. 1483-1498
    • Abdel-Hamid, A.M.1    Attwood, M.M.2    Guest, J.R.3
  • 2
    • 23144463910 scopus 로고    scopus 로고
    • RibEx: a web server for locating riboswitches and other conserved bacterial regulatory elements
    • Abreu-Goodger, C., and Merino, E. (2005) RibEx: a web server for locating riboswitches and other conserved bacterial regulatory elements. Nucleic Acids Res 33: W690-W692.
    • (2005) Nucleic Acids Res , vol.33 , pp. W690-W692
    • Abreu-Goodger, C.1    Merino, E.2
  • 3
    • 84868099390 scopus 로고    scopus 로고
    • PhiSpy: a novel algorithm for finding prophages in bacterial genomes that combines similarity- and composition-based strategies
    • Akhter, S., Aziz, R., and Edwards, R. (2012) PhiSpy: a novel algorithm for finding prophages in bacterial genomes that combines similarity- and composition-based strategies. Nucleic Acids Res 40: e126. doi:10.1093/nar/gks406.
    • (2012) Nucleic Acids Res , vol.40 , pp. e126
    • Akhter, S.1    Aziz, R.2    Edwards, R.3
  • 4
    • 79961109150 scopus 로고    scopus 로고
    • BLAST Ring Image Generator (BRIG): simple prokaryote genome comparisons
    • Alikhan, N.F., Petty, N.K., Ben Zakour, N.L., and Beatson, S.A. (2011) BLAST Ring Image Generator (BRIG): simple prokaryote genome comparisons. BMC Genomics 12: 402. doi:10.1186/1471-2164-12-402.
    • (2011) BMC Genomics , vol.12 , pp. 402
    • Alikhan, N.F.1    Petty, N.K.2    Ben Zakour, N.L.3    Beatson, S.A.4
  • 5
    • 0032880364 scopus 로고    scopus 로고
    • Comparison of proteins involved in pilus synthesis and mating pair stabilization from the related plasmids F and R100-1: insights into the mechanism of conjugation
    • Anthony, K., Klimke, W., Manchak, J., and Frost, L. (1999) Comparison of proteins involved in pilus synthesis and mating pair stabilization from the related plasmids F and R100-1: insights into the mechanism of conjugation. J Bacteriol 181: 5149-5159.
    • (1999) J Bacteriol , vol.181 , pp. 5149-5159
    • Anthony, K.1    Klimke, W.2    Manchak, J.3    Frost, L.4
  • 6
    • 0035166973 scopus 로고    scopus 로고
    • The InterPro database, an integrated documentation resource for protein families, domains and functional sites
    • Apweiler, R., Attwood, T., Bairoch, A., Bateman, A., Birney, E., Biswas, M., etal. (2001) The InterPro database, an integrated documentation resource for protein families, domains and functional sites. Nucleic Acids Res 29: 37-40.
    • (2001) Nucleic Acids Res , vol.29 , pp. 37-40
    • Apweiler, R.1    Attwood, T.2    Bairoch, A.3    Bateman, A.4    Birney, E.5    Biswas, M.6
  • 7
    • 40549120596 scopus 로고    scopus 로고
    • The RAST Server: rapid annotations using subsystems technology
    • Aziz, R.K., Bartels, D., Best, A.A., DeJongh, M., Disz, T., Edwards, R.A., etal. (2008) The RAST Server: rapid annotations using subsystems technology. BMC Genomics 9: 75. doi:10.1186/1471-2164-9-75.
    • (2008) BMC Genomics , vol.9 , pp. 75
    • Aziz, R.K.1    Bartels, D.2    Best, A.A.3    DeJongh, M.4    Disz, T.5    Edwards, R.A.6
  • 9
    • 0742286265 scopus 로고    scopus 로고
    • Structural and functional features of formate hydrogen lyase, an enzyme of mixed-acid fermentation from Escherichia coli
    • Bagramyan, K., and Trchounian, A. (2003) Structural and functional features of formate hydrogen lyase, an enzyme of mixed-acid fermentation from Escherichia coli. Biochemistry (Mosc) 68: 1159-1170.
    • (2003) Biochemistry (Mosc) , vol.68 , pp. 1159-1170
    • Bagramyan, K.1    Trchounian, A.2
  • 10
    • 0011865764 scopus 로고
    • Biosynthesis of delta-aminolevulinic acid from intact carbon skeleton of glutamic acid in greening barley
    • Beale, S., Gough, S., and Granick, S. (1975) Biosynthesis of delta-aminolevulinic acid from intact carbon skeleton of glutamic acid in greening barley. Proc Natl Acad Sci USA 72: 2719-2723.
    • (1975) Proc Natl Acad Sci USA , vol.72 , pp. 2719-2723
    • Beale, S.1    Gough, S.2    Granick, S.3
  • 11
    • 85047700415 scopus 로고    scopus 로고
    • Reconstitution of coupled fumarate respiration in liposomes by incorporating the electron transport enzymes isolated from Wolinella succinogenes
    • Biel, S., Simon, J., Gross, R., Ruiz, T., Ruitenberg, M., and Kröger, A. (2002) Reconstitution of coupled fumarate respiration in liposomes by incorporating the electron transport enzymes isolated from Wolinella succinogenes. Eur J Biochem 269: 1974-1983.
    • (2002) Eur J Biochem , vol.269 , pp. 1974-1983
    • Biel, S.1    Simon, J.2    Gross, R.3    Ruiz, T.4    Ruitenberg, M.5    Kröger, A.6
  • 12
    • 0025811139 scopus 로고
    • A simple method for the isolation of chromosomal DNA from gram positive or acid-fast bacteria
    • Bollet, C., Gevaudan, M.J., de Lamballerie, X., Zandotti, C., and de Micco, P. (1991) A simple method for the isolation of chromosomal DNA from gram positive or acid-fast bacteria. Nucleic Acids Res 19: 1955.
    • (1991) Nucleic Acids Res , vol.19 , pp. 1955
    • Bollet, C.1    Gevaudan, M.J.2    de Lamballerie, X.3    Zandotti, C.4    de Micco, P.5
  • 14
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 15
    • 0346816638 scopus 로고    scopus 로고
    • Primary sources of selected POPs: regional and global scale emission inventories
    • Breivik, K., Alcock, R., Li, Y., Bailey, R., Fiedler, H., and Pacyna, J. (2004) Primary sources of selected POPs: regional and global scale emission inventories. Environ Pollut 128: 3-16.
    • (2004) Environ Pollut , vol.128 , pp. 3-16
    • Breivik, K.1    Alcock, R.2    Li, Y.3    Bailey, R.4    Fiedler, H.5    Pacyna, J.6
  • 16
    • 1842833398 scopus 로고    scopus 로고
    • NapGH components of the periplasmic nitrate reductase of Escherichia coli K-12: location, topology and physiological roles in quinol oxidation and redox balancing
    • Brondijk, T., Nilavongse, A., Filenko, N., Richardson, D., and Cole, J. (2004) NapGH components of the periplasmic nitrate reductase of Escherichia coli K-12: location, topology and physiological roles in quinol oxidation and redox balancing. Biochem J 379: 47-55.
    • (2004) Biochem J , vol.379 , pp. 47-55
    • Brondijk, T.1    Nilavongse, A.2    Filenko, N.3    Richardson, D.4    Cole, J.5
  • 17
    • 0346319020 scopus 로고    scopus 로고
    • Reductive dehalogenation of chlorinated dioxins by an anaerobic bacterium
    • Bunge, M., Adrian, L., Kraus, A., Opel, M., Lorenz, W., Andreesen, J., etal. (2003) Reductive dehalogenation of chlorinated dioxins by an anaerobic bacterium. Nature 421: 357-360.
    • (2003) Nature , vol.421 , pp. 357-360
    • Bunge, M.1    Adrian, L.2    Kraus, A.3    Opel, M.4    Lorenz, W.5    Andreesen, J.6
  • 18
    • 84886647181 scopus 로고    scopus 로고
    • Functional genotyping of Sulfurospirillum spp. in mixed cultures allowed the identification of a new tetrachloroethene reductive dehalogenase
    • Buttet, G., Holliger, C., and Maillard, J. (2013) Functional genotyping of Sulfurospirillum spp. in mixed cultures allowed the identification of a new tetrachloroethene reductive dehalogenase. Appl Environ Microbiol 79: 6941-6947.
    • (2013) Appl Environ Microbiol , vol.79 , pp. 6941-6947
    • Buttet, G.1    Holliger, C.2    Maillard, J.3
  • 20
    • 0035489758 scopus 로고    scopus 로고
    • Growth and phylogenetic properties of novel bacteria belonging to the epsilon subdivision of the Proteobacteria enriched from Alvinella pompejana and deep-sea hydrothermal vents
    • Campbell, B., Jeanthon, C., Kostka, J., Luther, G., and Cary, S. (2001) Growth and phylogenetic properties of novel bacteria belonging to the epsilon subdivision of the Proteobacteria enriched from Alvinella pompejana and deep-sea hydrothermal vents. Appl Environ Microbiol 67: 4566-4572.
    • (2001) Appl Environ Microbiol , vol.67 , pp. 4566-4572
    • Campbell, B.1    Jeanthon, C.2    Kostka, J.3    Luther, G.4    Cary, S.5
  • 21
    • 84879586425 scopus 로고    scopus 로고
    • Physiological and genetic description of dissimilatory perchlorate reduction by the novel marine bacterium Arcobacter sp. strain CAB
    • Carlstrom, C., Wang, O., Melnyk, R., Bauer, S., Lee, J., Engelbrektson, A., and Coates, J. (2013) Physiological and genetic description of dissimilatory perchlorate reduction by the novel marine bacterium Arcobacter sp. strain CAB. Mbio 4 (3): e00217-13.
    • (2013) Mbio , vol.4 , Issue.3 , pp. e00217-e00313
    • Carlstrom, C.1    Wang, O.2    Melnyk, R.3    Bauer, S.4    Lee, J.5    Engelbrektson, A.6    Coates, J.7
  • 22
    • 77950650668 scopus 로고    scopus 로고
    • Tetrachloroethene conversion to ethene by a Dehalococcoides-containing enrichment culture from Bitterfeld
    • Cichocka, D., Nikolausz, M., Haest, P.J., and Nijenhuis, I. (2010) Tetrachloroethene conversion to ethene by a Dehalococcoides-containing enrichment culture from Bitterfeld. FEMS Microbiol Ecol 72: 297-310.
    • (2010) FEMS Microbiol Ecol , vol.72 , pp. 297-310
    • Cichocka, D.1    Nikolausz, M.2    Haest, P.J.3    Nijenhuis, I.4
  • 23
    • 0029311220 scopus 로고
    • Tetrachloroethene and 3-chlorobenzoate dechlorination activities are co-induced in Desulfomonile tiedjei DCB-1
    • Cole, J.R., Fathepure, B.Z., and Tiedje, J.M. (1995) Tetrachloroethene and 3-chlorobenzoate dechlorination activities are co-induced in Desulfomonile tiedjei DCB-1. Biodegradation 6: 167-172.
    • (1995) Biodegradation , vol.6 , pp. 167-172
    • Cole, J.R.1    Fathepure, B.Z.2    Tiedje, J.M.3
  • 24
    • 0032493294 scopus 로고    scopus 로고
    • The SbcCD nuclease of Escherichia coli is a structural maintenance of chromosomes (SMC) family protein that cleaves hairpin DNA
    • Connelly, J.C., Kirkham, L.A., and Leach, D.R. (1998) The SbcCD nuclease of Escherichia coli is a structural maintenance of chromosomes (SMC) family protein that cleaves hairpin DNA. Proc Natl Acad Sci USA 95: 7969-7974.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 7969-7974
    • Connelly, J.C.1    Kirkham, L.A.2    Leach, D.R.3
  • 25
    • 77956193448 scopus 로고    scopus 로고
    • progressiveMauve: multiple genome alignment with gene gain, loss and rearrangement
    • Darling, A.E., Mau, B., and Perna, N.T. (2010) progressiveMauve: multiple genome alignment with gene gain, loss and rearrangement. PLoS ONE 5: e11147.
    • (2010) PLoS ONE , vol.5 , pp. e11147
    • Darling, A.E.1    Mau, B.2    Perna, N.T.3
  • 27
    • 84866156154 scopus 로고    scopus 로고
    • The physiological opportunism of Desulfitobacterium hafniense strain TCE1 towards organohalide respiration with tetrachloroethene
    • Duret, A., Holliger, C., and Maillard, J. (2012) The physiological opportunism of Desulfitobacterium hafniense strain TCE1 towards organohalide respiration with tetrachloroethene. Appl Environ Microbiol 78: 6121-6127.
    • (2012) Appl Environ Microbiol , vol.78 , pp. 6121-6127
    • Duret, A.1    Holliger, C.2    Maillard, J.3
  • 28
    • 0034671914 scopus 로고    scopus 로고
    • Cytochrome c nitrite reductase from Wolinella succinogenes - structure at 1.6 angstrom resolution, inhibitor binding, and heme-packing motifs
    • Einsle, O., Stach, P., Messerschmidt, A., Simon, J., Kroger, A., Huber, R., and Kroneck, P. (2000) Cytochrome c nitrite reductase from Wolinella succinogenes - structure at 1.6 angstrom resolution, inhibitor binding, and heme-packing motifs. J Biol Chem 275: 39608-39616.
    • (2000) J Biol Chem , vol.275 , pp. 39608-39616
    • Einsle, O.1    Stach, P.2    Messerschmidt, A.3    Simon, J.4    Kroger, A.5    Huber, R.6    Kroneck, P.7
  • 29
    • 0035095129 scopus 로고    scopus 로고
    • Crystal structure of the 100kDa arsenite oxidase from Alcaligenes faecalis in two crystal forms at 1.64 A and 2.03 A
    • Ellis, P.J., Conrads, T., Hille, R., and Kuhn, P. (2001) Crystal structure of the 100kDa arsenite oxidase from Alcaligenes faecalis in two crystal forms at 1.64 A and 2.03 A. Structure 9: 125-132.
    • (2001) Structure , vol.9 , pp. 125-132
    • Ellis, P.J.1    Conrads, T.2    Hille, R.3    Kuhn, P.4
  • 30
    • 0032414781 scopus 로고    scopus 로고
    • Bacterial dehalogenation
    • Fetzner, S. (1998) Bacterial dehalogenation. Appl Microbiol Biotechnol 50: 633-657.
    • (1998) Appl Microbiol Biotechnol , vol.50 , pp. 633-657
    • Fetzner, S.1
  • 31
    • 0030853122 scopus 로고    scopus 로고
    • Sulfurospirillum arcachonense sp. nov., a new-microaerophilic sulfur-reducing bacterium
    • Finster, K., Liesack, W., and Tindall, B. (1997) Sulfurospirillum arcachonense sp. nov., a new-microaerophilic sulfur-reducing bacterium. Int J Syst Bacteriol 47: 1212-1217.
    • (1997) Int J Syst Bacteriol , vol.47 , pp. 1212-1217
    • Finster, K.1    Liesack, W.2    Tindall, B.3
  • 32
    • 41349112730 scopus 로고    scopus 로고
    • Ori-Finder: a web-based system for finding oriCs in unannotated bacterial genomes
    • Gao, F., and Zhang, C.T. (2008) Ori-Finder: a web-based system for finding oriCs in unannotated bacterial genomes. BMC Bioinformatics 9: 79. doi:10.1186/1471-2105-9-79.
    • (2008) BMC Bioinformatics , vol.9 , pp. 79
    • Gao, F.1    Zhang, C.T.2
  • 33
    • 0023046885 scopus 로고
    • Nucleotide sequence and deduced amino acid sequence of Escherichia coli pyruvate oxidase, a lipid-activated flavoprotein
    • Grabau, C., and Cronan, J. (1986) Nucleotide sequence and deduced amino acid sequence of Escherichia coli pyruvate oxidase, a lipid-activated flavoprotein. Nucleic Acids Res 14: 5449-5460.
    • (1986) Nucleic Acids Res , vol.14 , pp. 5449-5460
    • Grabau, C.1    Cronan, J.2
  • 34
    • 0038324086 scopus 로고    scopus 로고
    • The diversity of naturally produced organohalogens
    • Gribble, G. (2003) The diversity of naturally produced organohalogens. Chemosphere 52: 289-297.
    • (2003) Chemosphere , vol.52 , pp. 289-297
    • Gribble, G.1
  • 35
    • 34547579396 scopus 로고    scopus 로고
    • CRISPRFinder: a web tool to identify clustered regularly interspaced short palindromic repeats
    • Grissa, I., Vergnaud, G., and Pourcel, C. (2007) CRISPRFinder: a web tool to identify clustered regularly interspaced short palindromic repeats. Nucleic Acids Res 35: W52-W57.
    • (2007) Nucleic Acids Res , vol.35 , pp. W52-W57
    • Grissa, I.1    Vergnaud, G.2    Pourcel, C.3
  • 36
    • 14644443590 scopus 로고    scopus 로고
    • Hydrogen metabolism in the hyperthermophilic bacterium Aquifex aeolicus
    • Guiral, M., Aubert, C., and Giudici-Orticoni, M.T. (2005) Hydrogen metabolism in the hyperthermophilic bacterium Aquifex aeolicus. Biochem Soc Trans 33: 22-24.
    • (2005) Biochem Soc Trans , vol.33 , pp. 22-24
    • Guiral, M.1    Aubert, C.2    Giudici-Orticoni, M.T.3
  • 37
    • 16544383694 scopus 로고    scopus 로고
    • Halogenated organic compounds - a global perspective
    • Häggblom, M.M., and Bossert, I.D. (eds). Boston, MA, USA: Kluwer Academic Publishers
    • Häggblom, M.M., and Bossert, I.D. (2003) Halogenated organic compounds - a global perspective. In Dehalogenation: Microbial Processes and Environmental Applications. Häggblom, M.M., and Bossert, I.D. (eds). Boston, MA, USA: Kluwer Academic Publishers, pp. 3-29.
    • (2003) Dehalogenation: Microbial Processes and Environmental Applications , pp. 3-29
    • Häggblom, M.M.1    Bossert, I.D.2
  • 39
    • 33748236238 scopus 로고
    • Toxicity of chlorinated organic compounds - effects of the introduction of chlorine in organic molecules
    • Henschler, D. (1994) Toxicity of chlorinated organic compounds - effects of the introduction of chlorine in organic molecules. Angew Chem Int Ed Engl 33: 1920-1935.
    • (1994) Angew Chem Int Ed Engl , vol.33 , pp. 1920-1935
    • Henschler, D.1
  • 40
    • 52249100797 scopus 로고    scopus 로고
    • An alternative menaquinone biosynthetic pathway operating in microorganisms
    • Hiratsuka, T., Furihata, K., Ishikawa, J., Yamashita, H., Itoh, N., Seto, H., and Dairi, T. (2008) An alternative menaquinone biosynthetic pathway operating in microorganisms. Science 321: 1670-1673.
    • (2008) Science , vol.321 , pp. 1670-1673
    • Hiratsuka, T.1    Furihata, K.2    Ishikawa, J.3    Yamashita, H.4    Itoh, N.5    Seto, H.6    Dairi, T.7
  • 41
    • 0032450045 scopus 로고    scopus 로고
    • Reductive dechlorination in the energy metabolism of anaerobic bacteria
    • Holliger, C., Wohlfarth, G., and Diekert, G. (1998) Reductive dechlorination in the energy metabolism of anaerobic bacteria. FEMS Microbiol Rev 22: 383-398.
    • (1998) FEMS Microbiol Rev , vol.22 , pp. 383-398
    • Holliger, C.1    Wohlfarth, G.2    Diekert, G.3
  • 42
    • 34247586220 scopus 로고    scopus 로고
    • Oil field souring control by nitrate-reducing Sulfurospirillum spp. that outcompete sulfate-reducing bacteria for organic electron donors
    • Hubert, C., and Voordouw, G. (2007) Oil field souring control by nitrate-reducing Sulfurospirillum spp. that outcompete sulfate-reducing bacteria for organic electron donors. Appl Environ Microbiol 73: 2644-2652.
    • (2007) Appl Environ Microbiol , vol.73 , pp. 2644-2652
    • Hubert, C.1    Voordouw, G.2
  • 43
  • 44
    • 33947366478 scopus 로고    scopus 로고
    • Oxygen reactivity of both respiratory oxidases in Campylobacter jejuni: the cydAB genes encode a cyanide-resistant, low-affinity oxidase that is not of the cytochrome bd type
    • Jackson, R., Elvers, K., Lee, L., Gidley, M., Wainwright, L., Lightfoot, J., etal. (2007) Oxygen reactivity of both respiratory oxidases in Campylobacter jejuni: the cydAB genes encode a cyanide-resistant, low-affinity oxidase that is not of the cytochrome bd type. J Bacteriol 189: 1604-1615.
    • (2007) J Bacteriol , vol.189 , pp. 1604-1615
    • Jackson, R.1    Elvers, K.2    Lee, L.3    Gidley, M.4    Wainwright, L.5    Lightfoot, J.6
  • 45
    • 25144525184 scopus 로고    scopus 로고
    • Isolation and characterization of Sulfurospirillum carboxydovorans sp. nov., a new microaerophilic carbon monoxide oxidizing epsilon Proteobacterium
    • Jensen, A., and Finster, K. (2005) Isolation and characterization of Sulfurospirillum carboxydovorans sp. nov., a new microaerophilic carbon monoxide oxidizing epsilon Proteobacterium. Antonie Van Leeuwenhoek 87: 339-353.
    • (2005) Antonie Van Leeuwenhoek , vol.87 , pp. 339-353
    • Jensen, A.1    Finster, K.2
  • 46
    • 33746426583 scopus 로고    scopus 로고
    • Growth substrate dependent localization of tetrachloroethene reductive dehalogenase in Sulfurospirillum multivorans
    • John, M., Schmitz, R., Westermann, M., Richter, W., and Diekert, G. (2006) Growth substrate dependent localization of tetrachloroethene reductive dehalogenase in Sulfurospirillum multivorans. Arch Microbiol 186: 99-106.
    • (2006) Arch Microbiol , vol.186 , pp. 99-106
    • John, M.1    Schmitz, R.2    Westermann, M.3    Richter, W.4    Diekert, G.5
  • 47
    • 62649099789 scopus 로고    scopus 로고
    • Retentive memory of bacteria: long-term regulation of dehalorespiration in Sulfurospirillum multivorans
    • John, M., Rubick, R., Schmitz, R.P., Rakoczy, J., Schubert, T., and Diekert, G. (2009) Retentive memory of bacteria: long-term regulation of dehalorespiration in Sulfurospirillum multivorans. J Bacteriol 191: 1650-1655.
    • (2009) J Bacteriol , vol.191 , pp. 1650-1655
    • John, M.1    Rubick, R.2    Schmitz, R.P.3    Rakoczy, J.4    Schubert, T.5    Diekert, G.6
  • 48
    • 33947152438 scopus 로고    scopus 로고
    • Nitrogen fixation by reductively dechlorinating bacteria
    • Ju, X., Zhao, L., and Sun, B. (2007) Nitrogen fixation by reductively dechlorinating bacteria. Environ Microbiol 9: 1078-1083.
    • (2007) Environ Microbiol , vol.9 , pp. 1078-1083
    • Ju, X.1    Zhao, L.2    Sun, B.3
  • 49
    • 0033951106 scopus 로고    scopus 로고
    • Genetic and biochemical evidence of a Campylobacter jejuni capsular polysaccharide that accounts for Penner serotype specificity
    • Karlyshev, A.V., Linton, D., Gregson, N.A., Lastovica, A.J., and Wren, B.W. (2000) Genetic and biochemical evidence of a Campylobacter jejuni capsular polysaccharide that accounts for Penner serotype specificity. Mol Microbiol 35: 529-541.
    • (2000) Mol Microbiol , vol.35 , pp. 529-541
    • Karlyshev, A.V.1    Linton, D.2    Gregson, N.A.3    Lastovica, A.J.4    Wren, B.W.5
  • 50
    • 0034109116 scopus 로고    scopus 로고
    • Another unusual type of citric acid cycle enzyme in Helicobacter pylori: the malate:quinone oxidoreductase
    • Kather, B., Stingl, K., van der Rest, M.E., Altendorf, K., and Molenaar, D. (2000) Another unusual type of citric acid cycle enzyme in Helicobacter pylori: the malate:quinone oxidoreductase. J Bacteriol 182: 3204-3209.
    • (2000) J Bacteriol , vol.182 , pp. 3204-3209
    • Kather, B.1    Stingl, K.2    van der Rest, M.E.3    Altendorf, K.4    Molenaar, D.5
  • 51
    • 2142657817 scopus 로고    scopus 로고
    • A combined transmembrane topology and signal peptide prediction method
    • Käll, L., Krogh, A., and Sonnhammer, E.L. (2004) A combined transmembrane topology and signal peptide prediction method. J Mol Biol 338: 1027-1036.
    • (2004) J Mol Biol , vol.338 , pp. 1027-1036
    • Käll, L.1    Krogh, A.2    Sonnhammer, E.L.3
  • 52
    • 84912044237 scopus 로고    scopus 로고
    • Exogenous 5,6-dimethylbenzimidazole caused production of a non-functional tetrachloroethene reductive dehalogenase in Sulfurospirillum multivorans
    • Keller, S., Ruetz, M., Kunze, C., Kräutler, B., Diekert, G., and Schubert, T. (2013) Exogenous 5, 6-dimethylbenzimidazole caused production of a non-functional tetrachloroethene reductive dehalogenase in Sulfurospirillum multivorans. Environ Microbiol doi:10.1111/1462-2920.12268.
    • (2013) Environ Microbiol
    • Keller, S.1    Ruetz, M.2    Kunze, C.3    Kräutler, B.4    Diekert, G.5    Schubert, T.6
  • 53
    • 49249105797 scopus 로고    scopus 로고
    • Characterization of the NapGH quinol dehydrogenase complex involved in Wolinella succinogenes nitrate respiration
    • Kern, M., and Simon, J. (2008) Characterization of the NapGH quinol dehydrogenase complex involved in Wolinella succinogenes nitrate respiration. Mol Microbiol 69: 1137-1152.
    • (2008) Mol Microbiol , vol.69 , pp. 1137-1152
    • Kern, M.1    Simon, J.2
  • 54
    • 66349117533 scopus 로고    scopus 로고
    • Electron transport chains and bioenergetics of respiratory nitrogen metabolism in Wolinella succinogenes and other Epsilonproteobacteria
    • Kern, M., and Simon, J. (2009) Electron transport chains and bioenergetics of respiratory nitrogen metabolism in Wolinella succinogenes and other Epsilonproteobacteria. Biochim Biophys Acta 1787: 646-656.
    • (2009) Biochim Biophys Acta , vol.1787 , pp. 646-656
    • Kern, M.1    Simon, J.2
  • 55
    • 80052636384 scopus 로고    scopus 로고
    • The oxidative and nitrosative stress defence network of Wolinella succinogenes: cytochrome c nitrite reductase mediates the stress response to nitrite, nitric oxide, hydroxylamine and hydrogen peroxide
    • Kern, M., Volz, J., and Simon, J. (2011a) The oxidative and nitrosative stress defence network of Wolinella succinogenes: cytochrome c nitrite reductase mediates the stress response to nitrite, nitric oxide, hydroxylamine and hydrogen peroxide. Environ Microbiol 13: 2478-2494.
    • (2011) Environ Microbiol , vol.13 , pp. 2478-2494
    • Kern, M.1    Volz, J.2    Simon, J.3
  • 56
    • 83355166271 scopus 로고    scopus 로고
    • The Wolinella succinogenes mcc gene cluster encodes an unconventional respiratory sulphite reduction system
    • Kern, M., Klotz, M., and Simon, J. (2011b) The Wolinella succinogenes mcc gene cluster encodes an unconventional respiratory sulphite reduction system. Mol Microbiol 82: 1515-1530.
    • (2011) Mol Microbiol , vol.82 , pp. 1515-1530
    • Kern, M.1    Klotz, M.2    Simon, J.3
  • 57
    • 0001219297 scopus 로고
    • Pyruvate: ferredoxin oxidoreductase - new findings on an ancient enzyme
    • Kerscher, L., and Oesterhelt, D. (1982) Pyruvate: ferredoxin oxidoreductase - new findings on an ancient enzyme. Trends Biochem Sci 7: 371-374.
    • (1982) Trends Biochem Sci , vol.7 , pp. 371-374
    • Kerscher, L.1    Oesterhelt, D.2
  • 58
    • 84856588903 scopus 로고    scopus 로고
    • Genome sequence of Desulfitobacterium hafniense DCB-2, a gram-positive anaerobe capable of dehalogenation and metal reduction
    • Kim, S.H., Harzman, C., Davis, J.K., Hutcheson, R., Broderick, J.B., Marsh, T.L., and Tiedje, J.M. (2012) Genome sequence of Desulfitobacterium hafniense DCB-2, a gram-positive anaerobe capable of dehalogenation and metal reduction. BMC Microbiol 12: 21. doi:10.1186/1471-2180-12-21
    • (2012) BMC Microbiol , vol.12 , pp. 21
    • Kim, S.H.1    Harzman, C.2    Davis, J.K.3    Hutcheson, R.4    Broderick, J.B.5    Marsh, T.L.6    Tiedje, J.M.7
  • 59
    • 0025063286 scopus 로고
    • A radical-chemical route to acetyl-CoA - the anaerobically induced pyruvate formate-lyase system of Escherichia coli
    • Knappe, J., and Sawers, G. (1990) A radical-chemical route to acetyl-CoA - the anaerobically induced pyruvate formate-lyase system of Escherichia coli. FEMS Microbiol Lett 75: 383-398.
    • (1990) FEMS Microbiol Lett , vol.75 , pp. 383-398
    • Knappe, J.1    Sawers, G.2
  • 60
    • 34248206215 scopus 로고    scopus 로고
    • Sulfurospirillum cavolei sp. nov., a facultatively anaerobic sulfur-reducing bacterium isolated from an underground crude oil storage cavity
    • Kodama, Y., Ha, L., and Watanabe, K. (2007) Sulfurospirillum cavolei sp. nov., a facultatively anaerobic sulfur-reducing bacterium isolated from an underground crude oil storage cavity. Int J Syst Evol Microbiol 57: 827-831.
    • (2007) Int J Syst Evol Microbiol , vol.57 , pp. 827-831
    • Kodama, Y.1    Ha, L.2    Watanabe, K.3
  • 61
    • 0043032814 scopus 로고    scopus 로고
    • The mechanism of Mycobacterium tuberculosis alkylhydroperoxidase AhpD as defined by mutagenesis, crystallography, and kinetics
    • Koshkin, A., Nunn, C., Djordjevic, S., and de Montellano, P. (2003) The mechanism of Mycobacterium tuberculosis alkylhydroperoxidase AhpD as defined by mutagenesis, crystallography, and kinetics. J Biol Chem 278: 29502-29508.
    • (2003) J Biol Chem , vol.278 , pp. 29502-29508
    • Koshkin, A.1    Nunn, C.2    Djordjevic, S.3    de Montellano, P.4
  • 62
    • 0029016693 scopus 로고
    • The function of Wolinella succinogenes psr genes in electron transport with polysulphide as the terminal electron acceptor
    • Krafft, T., Gross, R., and Kröger, A. (1995) The function of Wolinella succinogenes psr genes in electron transport with polysulphide as the terminal electron acceptor. Eur J Biochem 230: 601-606.
    • (1995) Eur J Biochem , vol.230 , pp. 601-606
    • Krafft, T.1    Gross, R.2    Kröger, A.3
  • 64
    • 27144500225 scopus 로고    scopus 로고
    • Genome sequence of the chlorinated compound-respiring bacterium Dehalococcoides species strain CBDB1
    • Kube, M., Beck, A., Zinder, S.H., Kuhl, H., Reinhardt, R., and Adrian, L. (2005) Genome sequence of the chlorinated compound-respiring bacterium Dehalococcoides species strain CBDB1. Nat Biotechnol 23: 1269-1273.
    • (2005) Nat Biotechnol , vol.23 , pp. 1269-1273
    • Kube, M.1    Beck, A.2    Zinder, S.H.3    Kuhl, H.4    Reinhardt, R.5    Adrian, L.6
  • 66
    • 0037122940 scopus 로고    scopus 로고
    • Succinate:quinone oxidoreductases from epsilon-proteobacteria
    • Lancaster, C.R., and Simon, J. (2002) Succinate:quinone oxidoreductases from epsilon-proteobacteria. Biochim Biophys Acta 1553: 84-101.
    • (2002) Biochim Biophys Acta , vol.1553 , pp. 84-101
    • Lancaster, C.R.1    Simon, J.2
  • 67
    • 0010049951 scopus 로고    scopus 로고
    • Structure of fumarate reductase from Wolinella succinogenes at 2.2 A resolution
    • Lancaster, C.R., Kröger, A., Auer, M., and Michel, H. (1999) Structure of fumarate reductase from Wolinella succinogenes at 2.2 A resolution. Nature 402: 377-385.
    • (1999) Nature , vol.402 , pp. 377-385
    • Lancaster, C.R.1    Kröger, A.2    Auer, M.3    Michel, H.4
  • 68
    • 2942691821 scopus 로고    scopus 로고
    • Anaerobic reduction and oxidation of quinone moieties and the reduction of oxidized metals by halorespiring and related organisms
    • Luijten, M., Weelink, S., Godschalk, B., Langenhoff, A., van Eekert, M., Schraa, G., and Stams, A. (2004) Anaerobic reduction and oxidation of quinone moieties and the reduction of oxidized metals by halorespiring and related organisms. FEMS Microbiol Ecol 49: 145-150.
    • (2004) FEMS Microbiol Ecol , vol.49 , pp. 145-150
    • Luijten, M.1    Weelink, S.2    Godschalk, B.3    Langenhoff, A.4    van Eekert, M.5    Schraa, G.6    Stams, A.7
  • 69
    • 0037640029 scopus 로고    scopus 로고
    • Description of Sulfurospirillum halorespirans sp. nov., an anaerobic, tetrachloroethene-respiring bacterium, and transfer of Dehalospirillum multivorans to the genus Sulfurospirillum as Sulfurospirillum multivorans comb. nov
    • Luijten, M.L., de Weert, J., Smidt, H., Boschker, H.T., de Vos, W.M., Schraa, G., and Stams, A.J. (2003) Description of Sulfurospirillum halorespirans sp. nov., an anaerobic, tetrachloroethene-respiring bacterium, and transfer of Dehalospirillum multivorans to the genus Sulfurospirillum as Sulfurospirillum multivorans comb. nov. Int J Syst Evol Microbiol 53: 787-793.
    • (2003) Int J Syst Evol Microbiol , vol.53 , pp. 787-793
    • Luijten, M.L.1    de Weert, J.2    Smidt, H.3    Boschker, H.T.4    de Vos, W.M.5    Schraa, G.6    Stams, A.J.7
  • 70
    • 79957817494 scopus 로고    scopus 로고
    • Site-specific mobilization of vinyl chloride respiration islands by a mechanism common in Dehalococcoides
    • McMurdie, P.J., Hug, L.A., Edwards, E.A., Holmes, S., and Spormann, A.M. (2011) Site-specific mobilization of vinyl chloride respiration islands by a mechanism common in Dehalococcoides. BMC Genomics 12: 287. doi:10.1186/1471-2164-12-287.
    • (2011) BMC Genomics , vol.12 , pp. 287
    • McMurdie, P.J.1    Hug, L.A.2    Edwards, E.A.3    Holmes, S.4    Spormann, A.M.5
  • 73
    • 77953121577 scopus 로고    scopus 로고
    • Exploiting the ecogenomics toolbox for environmental diagnostics of organohalide-respiring bacteria
    • Maphosa, F., de Vos, W., and Smidt, H. (2010) Exploiting the ecogenomics toolbox for environmental diagnostics of organohalide-respiring bacteria. Trends Biotechnol 28: 308-316.
    • (2010) Trends Biotechnol , vol.28 , pp. 308-316
    • Maphosa, F.1    de Vos, W.2    Smidt, H.3
  • 75
    • 24044455869 scopus 로고    scopus 로고
    • Genome sequencing in microfabricated high-density picolitre reactors
    • Margulies, M., Egholm, M., Altman, W.E., Attiya, S., Bader, J.S., Bemben, L.A., etal. (2005) Genome sequencing in microfabricated high-density picolitre reactors. Nature 437: 376-380.
    • (2005) Nature , vol.437 , pp. 376-380
    • Margulies, M.1    Egholm, M.2    Altman, W.E.3    Attiya, S.4    Bader, J.S.5    Bemben, L.A.6
  • 76
    • 0344622120 scopus 로고    scopus 로고
    • Isolation of a bacterium that reductively dechlorinates tetrachloroethene to ethene
    • Maymó-Gatell, X., Chien, Y., Gossett, J.M., and Zinder, S.H. (1997) Isolation of a bacterium that reductively dechlorinates tetrachloroethene to ethene. Science 276: 1568-1571.
    • (1997) Science , vol.276 , pp. 1568-1571
    • Maymó-Gatell, X.1    Chien, Y.2    Gossett, J.M.3    Zinder, S.H.4
  • 77
    • 0030461965 scopus 로고    scopus 로고
    • Studies on tetrachloroethene respiration in Dehalospirillum multivorans
    • Miller, E., Wohlfarth, G., and Diekert, G. (1996) Studies on tetrachloroethene respiration in Dehalospirillum multivorans. Arch Microbiol 166: 379-387.
    • (1996) Arch Microbiol , vol.166 , pp. 379-387
    • Miller, E.1    Wohlfarth, G.2    Diekert, G.3
  • 78
    • 78651320818 scopus 로고    scopus 로고
    • WebGeSTer DB - a transcription terminator database
    • Mitra, A., Kesarwani, A.K., Pal, D., and Nagaraja, V. (2011) WebGeSTer DB - a transcription terminator database. Nucleic Acids Res 39: D129-D135.
    • (2011) Nucleic Acids Res , vol.39 , pp. D129-D135
    • Mitra, A.1    Kesarwani, A.K.2    Pal, D.3    Nagaraja, V.4
  • 79
    • 85011936070 scopus 로고    scopus 로고
    • ARNold: a web tool for the prediction of Rho-independent transcription terminators
    • Naville, M., Ghuillot-Gaudeffroy, A., Marchais, A., and Gautheret, D. (2011) ARNold: a web tool for the prediction of Rho-independent transcription terminators. RNA Biol 8: 11-13.
    • (2011) RNA Biol , vol.8 , pp. 11-13
    • Naville, M.1    Ghuillot-Gaudeffroy, A.2    Marchais, A.3    Gautheret, D.4
  • 80
    • 0028073774 scopus 로고
    • Tetrachloroethene metabolism of Dehalospirillum multivorans
    • Neumann, A., Scholz-Muramatsu, H., and Diekert, G. (1994) Tetrachloroethene metabolism of Dehalospirillum multivorans. Arch Microbiol 162: 295-301.
    • (1994) Arch Microbiol , vol.162 , pp. 295-301
    • Neumann, A.1    Scholz-Muramatsu, H.2    Diekert, G.3
  • 81
    • 0029895362 scopus 로고    scopus 로고
    • Purification and characterization of tetrachloroethene reductive dehalogenase from Dehalospirillum multivorans
    • Neumann, A., Wohlfarth, G., and Diekert, G. (1996) Purification and characterization of tetrachloroethene reductive dehalogenase from Dehalospirillum multivorans. J Biol Chem 271: 16515-16519.
    • (1996) J Biol Chem , vol.271 , pp. 16515-16519
    • Neumann, A.1    Wohlfarth, G.2    Diekert, G.3
  • 82
    • 0031859044 scopus 로고    scopus 로고
    • Tetrachloroethene dehalogenase from Dehalospirillum multivorans: cloning, sequencing of the encoding genes, and expression of the pceA gene in Escherichia coli
    • Neumann, A., Wohlfarth, G., and Diekert, G. (1998) Tetrachloroethene dehalogenase from Dehalospirillum multivorans: cloning, sequencing of the encoding genes, and expression of the pceA gene in Escherichia coli. J Bacteriol 180: 4140-4145.
    • (1998) J Bacteriol , vol.180 , pp. 4140-4145
    • Neumann, A.1    Wohlfarth, G.2    Diekert, G.3
  • 83
    • 33644854231 scopus 로고    scopus 로고
    • Complete genome sequence of the dehalorespiring bacterium Desulfitobacterium hafniense Y51 and comparison with Dehalococcoides ethenogenes 195
    • Nonaka, H., Keresztes, G., Shinoda, Y., Ikenaga, Y., Abe, M., Naito, K., etal. (2006) Complete genome sequence of the dehalorespiring bacterium Desulfitobacterium hafniense Y51 and comparison with Dehalococcoides ethenogenes 195. J Bacteriol 188: 2262-2274.
    • (2006) J Bacteriol , vol.188 , pp. 2262-2274
    • Nonaka, H.1    Keresztes, G.2    Shinoda, Y.3    Ikenaga, Y.4    Abe, M.5    Naito, K.6
  • 84
    • 84859165788 scopus 로고    scopus 로고
    • The Genomes OnLine Database (GOLD) v.4: status of genomic and metagenomic projects and their associated metadata
    • Pagani, I., Liolios, K., Jansson, J., Chen, I., Smirnova, T., Nosrat, B., etal. (2012) The Genomes OnLine Database (GOLD) v.4: status of genomic and metagenomic projects and their associated metadata. Nucleic Acids Res 40: D571-D579.
    • (2012) Nucleic Acids Res , vol.40 , pp. D571-D579
    • Pagani, I.1    Liolios, K.2    Jansson, J.3    Chen, I.4    Smirnova, T.5    Nosrat, B.6
  • 85
    • 0034628526 scopus 로고    scopus 로고
    • The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences
    • Parkhill, J., Wren, B., Mungall, K., Ketley, J., Churcher, C., Basham, D., etal. (2000) The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences. Nature 403: 665-668.
    • (2000) Nature , vol.403 , pp. 665-668
    • Parkhill, J.1    Wren, B.2    Mungall, K.3    Ketley, J.4    Churcher, C.5    Basham, D.6
  • 87
    • 84878383709 scopus 로고    scopus 로고
    • Genome sequences of two dehalogenation specialists - Dehalococcoides mccartyi strains BTF08 and DCMB5 enriched from the highly polluted Bitterfeld region
    • Pöritz, M., Goris, T., Wubet, T., Tarkka, M.T., Buscot, F., Nijenhuis, I., etal. (2013) Genome sequences of two dehalogenation specialists - Dehalococcoides mccartyi strains BTF08 and DCMB5 enriched from the highly polluted Bitterfeld region. FEMS Microbiol Lett 343: 101-104.
    • (2013) FEMS Microbiol Lett , vol.343 , pp. 101-104
    • Pöritz, M.1    Goris, T.2    Wubet, T.3    Tarkka, M.T.4    Buscot, F.5    Nijenhuis, I.6
  • 88
    • 0023823389 scopus 로고
    • Reductive dechlorination of polychlorinated biphenyls by anerobic microorganisms from sediments
    • Quensen, J., Tiedje, J., and Boyd, S. (1988) Reductive dechlorination of polychlorinated biphenyls by anerobic microorganisms from sediments. Science 242: 752-754.
    • (1988) Science , vol.242 , pp. 752-754
    • Quensen, J.1    Tiedje, J.2    Boyd, S.3
  • 90
    • 84888869356 scopus 로고    scopus 로고
    • Membrane-bound oxygen reductases of the anaerobic sulfate-reducing Desulfovibrio vulgaris Hildenborough: roles in oxygen defence and electron link with periplasmic hydrogen oxidation
    • Ramel, F., Amrani, A., Pieulle, L., Lamrabet, O., Voordouw, G., Seddiki, N., etal. (2013) Membrane-bound oxygen reductases of the anaerobic sulfate-reducing Desulfovibrio vulgaris Hildenborough: roles in oxygen defence and electron link with periplasmic hydrogen oxidation. Microbiology 159: 2663-2673.
    • (2013) Microbiology , vol.159 , pp. 2663-2673
    • Ramel, F.1    Amrani, A.2    Pieulle, L.3    Lamrabet, O.4    Voordouw, G.5    Seddiki, N.6
  • 91
    • 0024967060 scopus 로고
    • Transfer RNA genes frequently serve as integration sites for prokaryotic genetic elements
    • Reiter, W., Palm, P., and Yeats, S. (1989) Transfer RNA genes frequently serve as integration sites for prokaryotic genetic elements. Nucleic Acids Res 17: 1907-1914.
    • (1989) Nucleic Acids Res , vol.17 , pp. 1907-1914
    • Reiter, W.1    Palm, P.2    Yeats, S.3
  • 92
    • 50049103112 scopus 로고    scopus 로고
    • The prokaryotic complex iron-sulfur molybdoenzyme family
    • Rothery, R.A., Workun, G.J., and Weiner, J.H. (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
  • 95
    • 34347386473 scopus 로고    scopus 로고
    • Flavodoxin:quinone reductase (FqrB): a redox partner of pyruvate:ferredoxin oxidoreductase that reversibly couples pyruvate oxidation to NADPH production in Helicobacter pylori and Campylobacter jejuni
    • St Maurice, M., Cremades, N., Croxen, M.A., Sisson, G., Sancho, J., and Hoffman, P.S. (2007) Flavodoxin:quinone reductase (FqrB): a redox partner of pyruvate:ferredoxin oxidoreductase that reversibly couples pyruvate oxidation to NADPH production in Helicobacter pylori and Campylobacter jejuni. J Bacteriol 189: 4764-4773.
    • (2007) J Bacteriol , vol.189 , pp. 4764-4773
    • St Maurice, M.1    Cremades, N.2    Croxen, M.A.3    Sisson, G.4    Sancho, J.5    Hoffman, P.S.6
  • 96
    • 0028566978 scopus 로고
    • The hydrogenases and formate dehydrogenases of Escherichia coli
    • Sawers, G. (1994) The hydrogenases and formate dehydrogenases of Escherichia coli. Antonie Van Leeuwenhoek 66: 57-88.
    • (1994) Antonie Van Leeuwenhoek , vol.66 , pp. 57-88
    • Sawers, G.1
  • 97
    • 0347625653 scopus 로고    scopus 로고
    • Purification and properties of the formate dehydrogenase and characterization of the fdhA gene of Sulfurospirillum multivorans
    • Schmitz, R.P., and Diekert, G. (2003) Purification and properties of the formate dehydrogenase and characterization of the fdhA gene of Sulfurospirillum multivorans. Arch Microbiol 180: 394-401.
    • (2003) Arch Microbiol , vol.180 , pp. 394-401
    • Schmitz, R.P.1    Diekert, G.2
  • 98
    • 35948970560 scopus 로고    scopus 로고
    • Evidence for a radical mechanism of the dechlorination of chlorinated propenes mediated by the tetrachloroethene reductive dehalogenase of Sulfurospirillum muftivorans
    • Schmitz, R.P., Wolf, J., Habel, A., Neumann, A., Ploss, K., Svatos, A., etal. (2007) Evidence for a radical mechanism of the dechlorination of chlorinated propenes mediated by the tetrachloroethene reductive dehalogenase of Sulfurospirillum muftivorans. Environ Sci Technol 41: 7370-7375.
    • (2007) Environ Sci Technol , vol.41 , pp. 7370-7375
    • Schmitz, R.P.1    Wolf, J.2    Habel, A.3    Neumann, A.4    Ploss, K.5    Svatos, A.6
  • 99
    • 0028831324 scopus 로고
    • Isolation and characterization of Dehalospirillum multivorans gen. nov., sp. nov., a tetrachloroethene-utilizing, strictly anaerobic bacterium
    • Scholz-Muramatsu, H., Neumann, A., Messmer, M., Moore, E., and Diekert, G. (1995) Isolation and characterization of Dehalospirillum multivorans gen. nov., sp. nov., a tetrachloroethene-utilizing, strictly anaerobic bacterium. Arch Microbiol 163: 48-56.
    • (1995) Arch Microbiol , vol.163 , pp. 48-56
    • Scholz-Muramatsu, H.1    Neumann, A.2    Messmer, M.3    Moore, E.4    Diekert, G.5
  • 100
    • 0242696464 scopus 로고    scopus 로고
    • Purification and characterization of the selenate reductase from Thauera selenatis
    • Schröder, I., Rech, S., Krafft, T., and Macy, J. (1997) Purification and characterization of the selenate reductase from Thauera selenatis. J Biol Chem 272: 23765-23768.
    • (1997) J Biol Chem , vol.272 , pp. 23765-23768
    • Schröder, I.1    Rech, S.2    Krafft, T.3    Macy, J.4
  • 101
    • 0026646868 scopus 로고
    • Comparative systematic study on 'Spirillum' 5175, Campylobacter and Wolinella species
    • Schumacher, W., Kroneck, P., and Pfennig, N. (1992) Comparative systematic study on 'Spirillum' 5175, Campylobacter and Wolinella species. Arch Microbiol 158: 287-293.
    • (1992) Arch Microbiol , vol.158 , pp. 287-293
    • Schumacher, W.1    Kroneck, P.2    Pfennig, N.3
  • 102
    • 19944426081 scopus 로고    scopus 로고
    • Genome sequence of the PCE-dechlorinating bacterium Dehalococcoides ethenogenes
    • Seshadri, R., Adrian, L., Fouts, D.E., Eisen, J.A., Phillipy, A.M., and Methe, B.A. (2005) Genome sequence of the PCE-dechlorinating bacterium Dehalococcoides ethenogenes. Science 307: 105-108.
    • (2005) Science , vol.307 , pp. 105-108
    • Seshadri, R.1    Adrian, L.2    Fouts, D.E.3    Eisen, J.A.4    Phillipy, A.M.5    Methe, B.A.6
  • 103
    • 0036428776 scopus 로고    scopus 로고
    • A non-dechlorinating strain of Dehalospirillum multivorans: evidence for a key role of the corrinoid cofactor in the synthesis of an active tetrachloroethene dehalogenase
    • Siebert, A., Neumann, A., Schubert, T., and Diekert, G. (2002) A non-dechlorinating strain of Dehalospirillum multivorans: evidence for a key role of the corrinoid cofactor in the synthesis of an active tetrachloroethene dehalogenase. Arch Microbiol 178: 443-449.
    • (2002) Arch Microbiol , vol.178 , pp. 443-449
    • Siebert, A.1    Neumann, A.2    Schubert, T.3    Diekert, G.4
  • 106
    • 0036024581 scopus 로고    scopus 로고
    • Enzymology and bioenergetics of respiratory nitrite ammonification
    • Simon, J. (2002) Enzymology and bioenergetics of respiratory nitrite ammonification. FEMS Microbiol Rev 26: 285-309.
    • (2002) FEMS Microbiol Rev , vol.26 , pp. 285-309
    • Simon, J.1
  • 107
    • 84871720360 scopus 로고    scopus 로고
    • Diversity and evolution of bioenergetic systems involved in microbial nitrogen compound transformations
    • Simon, J., and Klotz, M.G. (2013) Diversity and evolution of bioenergetic systems involved in microbial nitrogen compound transformations. Biochim Biophys Acta 1827: 114-135.
    • (2013) Biochim Biophys Acta , vol.1827 , pp. 114-135
    • Simon, J.1    Klotz, M.G.2
  • 108
    • 3042689049 scopus 로고    scopus 로고
    • The unprecedented nos gene cluster of Wolinella succinogenes encodes a novel respiratory electron transfer pathway to cytochrome c nitrous oxide reductase
    • Simon, J., Einsle, O., Kroneck, P.M., and Zumft, W.G. (2004) The unprecedented nos gene cluster of Wolinella succinogenes encodes a novel respiratory electron transfer pathway to cytochrome c nitrous oxide reductase. FEBS Lett 569: 7-12.
    • (2004) FEBS Lett , vol.569 , pp. 7-12
    • Simon, J.1    Einsle, O.2    Kroneck, P.M.3    Zumft, W.G.4
  • 109
    • 9244251590 scopus 로고    scopus 로고
    • Anaerobic microbial dehalogenation
    • Smidt, H., and de Vos, W. (2004) Anaerobic microbial dehalogenation. Annu Rev Microbiol 58: 43-73.
    • (2004) Annu Rev Microbiol , vol.58 , pp. 43-73
    • Smidt, H.1    de Vos, W.2
  • 110
    • 0033872083 scopus 로고    scopus 로고
    • Characteristics of the aerobic respiratory chains of the microaerophiles Campylobacter jejuni and Helicobacter pylori
    • Smith, M.A., Finel, M., Korolik, V., and Mendz, G.L. (2000) Characteristics of the aerobic respiratory chains of the microaerophiles Campylobacter jejuni and Helicobacter pylori. Arch Microbiol 174: 1-10.
    • (2000) Arch Microbiol , vol.174 , pp. 1-10
    • Smith, M.A.1    Finel, M.2    Korolik, V.3    Mendz, G.L.4
  • 111
    • 0036436922 scopus 로고    scopus 로고
    • 2-evolving enzyme complex from Carboxydothermus hydrogenoformans
    • 2-evolving enzyme complex from Carboxydothermus hydrogenoformans. Eur J Biochem 269: 5712-5721.
    • (2002) Eur J Biochem , vol.269 , pp. 5712-5721
    • Soboh, B.1    Linder, D.2    Hedderich, R.3
  • 112
    • 0021717996 scopus 로고
    • A new 3-hydroxybutyrate fermenting anaerobe, Ilyobacter polytropus, gen. nov. sp. nov., possessing various fermentation pathways
    • Stieb, M., and Schink, B. (1984) A new 3-hydroxybutyrate fermenting anaerobe, Ilyobacter polytropus, gen. nov. sp. nov., possessing various fermentation pathways. Arch Microbiol 140: 139-146.
    • (1984) Arch Microbiol , vol.140 , pp. 139-146
    • Stieb, M.1    Schink, B.2
  • 113
    • 0033064952 scopus 로고    scopus 로고
    • Sulfurospirillum barnesii sp. nov. and Sulfurospirillum arsenophilum sp. nov., new members of the Sulfurospirillum clade of the epsilon Proteobacteria
    • Stolz, J., Ellis, D., Blum, J., Ahmann, D., Lovley, D., and Oremland, R. (1999) Sulfurospirillum barnesii sp. nov. and Sulfurospirillum arsenophilum sp. nov., new members of the Sulfurospirillum clade of the epsilon Proteobacteria. Int J Syst Bacteriol 49: 1177-1180.
    • (1999) Int J Syst Bacteriol , vol.49 , pp. 1177-1180
    • Stolz, J.1    Ellis, D.2    Blum, J.3    Ahmann, D.4    Lovley, D.5    Oremland, R.6
  • 115
    • 84864552445 scopus 로고    scopus 로고
    • Abiotic degradation of chlorinated ethanes and ethenes in water
    • Tobiszewski, M., and Namiesnik, J. (2012) Abiotic degradation of chlorinated ethanes and ethenes in water. Environ Sci Pollut Res Int 19: 1994-2006.
    • (2012) Environ Sci Pollut Res Int , vol.19 , pp. 1994-2006
    • Tobiszewski, M.1    Namiesnik, J.2
  • 116
    • 0030835739 scopus 로고    scopus 로고
    • The complete genome sequence of the gastric pathogen Helicobacter pylori
    • Tomb, J., White, O., Kerlavage, A., Clayton, R., Sutton, G., Fleischmann, R., etal. (1997) The complete genome sequence of the gastric pathogen Helicobacter pylori. Nature 388: 539-547.
    • (1997) Nature , vol.388 , pp. 539-547
    • Tomb, J.1    White, O.2    Kerlavage, A.3    Clayton, R.4    Sutton, G.5    Fleischmann, R.6
  • 117
    • 0029772305 scopus 로고    scopus 로고
    • Characterization of chloroethylene dehalogenation by cell extracts of Desulfomonile tiedjei and its relationship to chlorobenzoate dehalogenation
    • Townsend, G., and Suflita, J. (1996) Characterization of chloroethylene dehalogenation by cell extracts of Desulfomonile tiedjei and its relationship to chlorobenzoate dehalogenation. Appl Environ Microbiol 62: 2850-2853.
    • (1996) Appl Environ Microbiol , vol.62 , pp. 2850-2853
    • Townsend, G.1    Suflita, J.2
  • 118
    • 35748974830 scopus 로고    scopus 로고
    • Occurrence, classification, and biological function of hydrogenases: an overview
    • Vignais, P.M., and 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
  • 119
    • 65349170600 scopus 로고    scopus 로고
    • Biohalogenation: nature's way to synthesize halogenated metabolites
    • Wagner, C., El Omari, M., and Konig, G. (2009) Biohalogenation: nature's way to synthesize halogenated metabolites. J Nat Prod 72: 540-553.
    • (2009) J Nat Prod , vol.72 , pp. 540-553
    • Wagner, C.1    El Omari, M.2    Konig, G.3
  • 120
    • 84861217829 scopus 로고    scopus 로고
    • Genomic determinants of organohalide-respiration in Geobacter lovleyi, an unusual member of the Geobacteraceae
    • Wagner, D.D., Hug, L.A., Hatt, J.K., Spitzmiller, M.R., Padilla-Crespo, E., Ritalahti, K.M., etal. (2012) Genomic determinants of organohalide-respiration in Geobacter lovleyi, an unusual member of the Geobacteraceae. BMC Genomics 13: 200. doi:10.1186/1471-2164-13-200.
    • (2012) BMC Genomics , vol.13 , pp. 200
    • Wagner, D.D.1    Hug, L.A.2    Hatt, J.K.3    Spitzmiller, M.R.4    Padilla-Crespo, E.5    Ritalahti, K.M.6
  • 121
    • 84857080584 scopus 로고    scopus 로고
    • Transcriptional analysis of a Dehalococcoides-containing microbial consortium reveals prophage activation
    • Waller, A., Hug, L., Mo, K., Radford, D., Maxwell, K., and Edwards, E. (2012) Transcriptional analysis of a Dehalococcoides-containing microbial consortium reveals prophage activation. Appl Environ Microbiol 78: 1178-1186.
    • (2012) Appl Environ Microbiol , vol.78 , pp. 1178-1186
    • Waller, A.1    Hug, L.2    Mo, K.3    Radford, D.4    Maxwell, K.5    Edwards, E.6
  • 123
    • 0037307079 scopus 로고    scopus 로고
    • Pesticides and other micro-organic contaminants in freshwater sedimentary environments - a review
    • Warren, N., Allan, I., Carter, J., House, W., and Parker, A. (2003) Pesticides and other micro-organic contaminants in freshwater sedimentary environments - a review. Appl Geochem 18: 159-194.
    • (2003) Appl Geochem , vol.18 , pp. 159-194
    • Warren, N.1    Allan, I.2    Carter, J.3    House, W.4    Parker, A.5
  • 124
    • 38649086396 scopus 로고    scopus 로고
    • The Campylobacter jejuni NADH:ubiquinone oxidoreductase (complex I) utilizes flavodoxin rather than NADH
    • Weerakoon, D.R., and Olson, J.W. (2008) The Campylobacter jejuni NADH:ubiquinone oxidoreductase (complex I) utilizes flavodoxin rather than NADH. J Bacteriol 190: 915-925.
    • (2008) J Bacteriol , vol.190 , pp. 915-925
    • Weerakoon, D.R.1    Olson, J.W.2
  • 125
    • 0023909061 scopus 로고
    • Two biochemically distinct classes of fumarase in Escherichia coli
    • Woods, S.A., Schwartzbach, S.D., and Guest, J.R. (1988) Two biochemically distinct classes of fumarase in Escherichia coli. Biochim Biophys Acta 954: 14-26.
    • (1988) Biochim Biophys Acta , vol.954 , pp. 14-26
    • Woods, S.A.1    Schwartzbach, S.D.2    Guest, J.R.3
  • 126
    • 77649097294 scopus 로고    scopus 로고
    • Reductive dehalogenation of brominated ethenes by Sulfurospirillum multivorans and Desulfitobacterium hafniense PCE-S
    • Ye, L., Schilhabel, A., Bartram, S., Boland, W., and Diekert, G. (2010) Reductive dehalogenation of brominated ethenes by Sulfurospirillum multivorans and Desulfitobacterium hafniense PCE-S. Environ Microbiol 12: 501-509.
    • (2010) Environ Microbiol , vol.12 , pp. 501-509
    • Ye, L.1    Schilhabel, A.2    Bartram, S.3    Boland, W.4    Diekert, G.5


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