메뉴 건너뛰기




Volumn 188, Issue 4, 2006, Pages 1473-1488

The genome sequence of the obligately chemolithoautotrophic, facultatively anaerobic bacterium Thiobacillus denitrificans

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE PHOSPHATE; CARBON; CYTOCHROME C; FERROUS ION; GROUND WATER; HEAVY METAL; HYDROGENASE; NITROGEN; ORGANIC COMPOUND; SULFATE; SULFITE; SULFUR DERIVATIVE; URANIUM;

EID: 32444438519     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.188.4.1473-1488.2006     Document Type: Article
Times cited : (305)

References (94)
  • 2
    • 0016207966 scopus 로고
    • An AMP-independent sulphite oxidase from Thiobacillus denitrificans: Purification and properties
    • Aminuddin, M., and D. J. D. Nicholas. 1974. An AMP-independent sulphite oxidase from Thiobacillus denitrificans: purification and properties. J. Gen. Microbiol. 82:103-113.
    • (1974) J. Gen. Microbiol. , vol.82 , pp. 103-113
    • Aminuddin, M.1    Nicholas, D.J.D.2
  • 3
    • 0038240633 scopus 로고    scopus 로고
    • Bacterial mercury resistance from atoms to ecosystems
    • Barkay, T., S. M. Miller, and A. O. Summers. 2003. Bacterial mercury resistance from atoms to ecosystems. FEMS Microbiol. Rev. 27:355-384.
    • (2003) FEMS Microbiol. Rev. , vol.27 , pp. 355-384
    • Barkay, T.1    Miller, S.M.2    Summers, A.O.3
  • 4
    • 0007661810 scopus 로고
    • Phénomènes de réduction produits par les microbes (Conférence avec demonstrations faite-Delft, le 16 avril 1903)
    • Beijerinck, M. W. 1904. Phénomènes de réduction produits par les microbes (Conférence avec demonstrations faite-Delft, le 16 avril 1903). Arch. Neerl. Sci. Ser. 29:131-157.
    • (1904) Arch. Neerl. Sci. Ser. , vol.29 , pp. 131-157
    • Beijerinck, M.W.1
  • 5
    • 17444392874 scopus 로고    scopus 로고
    • Anaerobic, nitrate-dependent oxidation of U(IV) oxide minerals by the chemolithoautotrophic bacterium Thiobacillus denitrificans
    • Beller, H. R. 2005. Anaerobic, nitrate-dependent oxidation of U(IV) oxide minerals by the chemolithoautotrophic bacterium Thiobacillus denitrificans. Appl. Environ. Microbiol. 71:2170-2174.
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 2170-2174
    • Beller, H.R.1
  • 6
    • 2942717244 scopus 로고    scopus 로고
    • Biogeochemistry and natural attenuation of nitrate in groundwater at an explosives test facility
    • Beller, H. R., V. Madrid, G. B. Hudson, W. W. McNab, and T. Carlsen. 2004. Biogeochemistry and natural attenuation of nitrate in groundwater at an explosives test facility. Appl. Geochem. 19:1483-1494.
    • (2004) Appl. Geochem. , vol.19 , pp. 1483-1494
    • Beller, H.R.1    Madrid, V.2    Hudson, G.B.3    McNab, W.W.4    Carlsen, T.5
  • 8
    • 0028944291 scopus 로고
    • Sequence analysis of subunits of the membrane-bound nitrate reductase from a denitrifying bacterium: The integral membrane subunit provides a prototype for the dihaem electron-carrying arm of a redox loop
    • Berks, B. C., M. D. Page, D. J. Richardson, A. Reilly, A. Cavill, F. Outen, and S. J. Ferguson. 1995. Sequence analysis of subunits of the membrane-bound nitrate reductase from a denitrifying bacterium: the integral membrane subunit provides a prototype for the dihaem electron-carrying arm of a redox loop. Mol. Microbiol. 15:319-331.
    • (1995) Mol. Microbiol. , vol.15 , pp. 319-331
    • Berks, B.C.1    Page, M.D.2    Richardson, D.J.3    Reilly, A.4    Cavill, A.5    Outen, F.6    Ferguson, S.J.7
  • 9
    • 0002739485 scopus 로고    scopus 로고
    • Linkage map of Escherichia coli K12
    • edition 9, F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.). ASM Press, Washington, D.C.
    • Berlyn, M. K. B., K. B. Low, K. E. Rudd, and M. Singer. 1996. Linkage map of Escherichia coli K12, edition 9, p. 1715-1902. In F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella: cellular and molecular biology, 2nd ed., vol. 2. ASM Press, Washington, D.C.
    • (1996) Escherichia Coli and Salmonella: Cellular and Molecular Biology, 2nd Ed. , vol.2 , pp. 1715-1902
    • Berlyn, M.K.B.1    Low, K.B.2    Rudd, K.E.3    Singer, M.4
  • 10
    • 2642585084 scopus 로고
    • Occurrence, structure and function of intracellular polyglucose in the obligate chemolithotroph Thiobacillus neapolitanus
    • Beudeker, R. F., J. W. M. Kerver, and J. G. Kuenen. 1981. Occurrence, structure and function of intracellular polyglucose in the obligate chemolithotroph Thiobacillus neapolitanus. Arch. Microbiol. 129:221-226.
    • (1981) Arch. Microbiol. , vol.129 , pp. 221-226
    • Beudeker, R.F.1    Kerver, J.W.M.2    Kuenen, J.G.3
  • 11
    • 0019842983 scopus 로고
    • Heterolactic fermentation of intracellular polyglucose by the obligate chemolithotroph Thiobacillus neapolitanus under anaerobic conditions
    • Beudeker, R. F., W. de Boer, and J. G. Kuenen. 1981. Heterolactic fermentation of intracellular polyglucose by the obligate chemolithotroph Thiobacillus neapolitanus under anaerobic conditions. FEMS Microbiol. Lett. 12:337-342.
    • (1981) FEMS Microbiol. Lett. , vol.12 , pp. 337-342
    • Beudeker, R.F.1    De Boer, W.2    Kuenen, J.G.3
  • 12
    • 0014016711 scopus 로고
    • Studies on the adenosine-5′-phosphosulfate reductase from Thiobacillus denitrificans
    • Bowen, T. J., F. C. Happold, and B. F. Taylor. 1966. Studies on the adenosine-5′-phosphosulfate reductase from Thiobacillus denitrificans. Biochim. Biophys. Acta 118:566-576.
    • (1966) Biochim. Biophys. Acta , vol.118 , pp. 566-576
    • Bowen, T.J.1    Happold, F.C.2    Taylor, B.F.3
  • 13
    • 0040786729 scopus 로고    scopus 로고
    • "ADP sulfurylase" from Thiobacillus denitrificans is an adenylylsulfate:phosphate adenylyltransferase and belongs to a new family of nucleotidyltransferases
    • Brüser, T., T. Selmer, and C. Dahl. 2000. "ADP sulfurylase" from Thiobacillus denitrificans is an adenylylsulfate: phosphate adenylyltransferase and belongs to a new family of nucleotidyltransferases. J. Biol. Chem. 275:1691-1698.
    • (2000) J. Biol. Chem. , vol.275 , pp. 1691-1698
    • Brüser, T.1    Selmer, T.2    Dahl, C.3
  • 17
    • 14544272337 scopus 로고    scopus 로고
    • Novel genes of the dsr gene cluster and evidence for close interaction of Dsr proteins during sulfur oxidation in the phototrophic sulfur bacterium Allochromatium vinosum
    • Dahl, C., S. Engels, A. S. Pott-Sperling, A. Schulte, J. Sander, Y. Lübbe, O. Deuster, and D. C. Brune. 2005. Novel genes of the dsr gene cluster and evidence for close interaction of Dsr proteins during sulfur oxidation in the phototrophic sulfur bacterium Allochromatium vinosum. J. Bacteriol. 187:1392-1404.
    • (2005) J. Bacteriol. , vol.187 , pp. 1392-1404
    • Dahl, C.1    Engels, S.2    Pott-Sperling, A.S.3    Schulte, A.4    Sander, J.5    Lübbe, Y.6    Deuster, O.7    Brune, D.C.8
  • 18
    • 0035014565 scopus 로고    scopus 로고
    • The ABC of ABCs: A phylogenetic and functional classification of ABC systems in living organisms
    • Dassa, E., and P. Bouige. 2001. The ABC of ABCs: a phylogenetic and functional classification of ABC systems in living organisms. Res. Microbiol. 152:211-229.
    • (2001) Res. Microbiol. , vol.152 , pp. 211-229
    • Dassa, E.1    Bouige, P.2
  • 19
    • 0015596223 scopus 로고
    • Assimilation and toxicity of some exogenous C-1 compounds, alcohols, sugars and acetate in the methane-oxidizing bacterium Methylococcus capsulatus
    • Eccleston, M., and D. P. Kelly. 1973. Assimilation and toxicity of some exogenous C-1 compounds, alcohols, sugars and acetate in the methane-oxidizing bacterium Methylococcus capsulatus. J. Gen. Microbiol. 75:211-221.
    • (1973) J. Gen. Microbiol. , vol.75 , pp. 211-221
    • Eccleston, M.1    Kelly, D.P.2
  • 21
    • 0026652711 scopus 로고
    • Two forms of ribulose 1,5-bisphosphate carboxylase/oxygenase from Thiobacillus denitrificans
    • English, R. S., C. A. Williams, S. C. Lorbach, and J. M. Shively. 1992. Two forms of ribulose 1,5-bisphosphate carboxylase/oxygenase from Thiobacillus denitrificans. FEMS Microbiol. Lett. 73:111-119.
    • (1992) FEMS Microbiol. Lett. , vol.73 , pp. 111-119
    • English, R.S.1    Williams, C.A.2    Lorbach, S.C.3    Shively, J.M.4
  • 22
    • 0031978181 scopus 로고    scopus 로고
    • Basecalling of automated sequencer traces using phred. II. Error probabilities
    • Ewing, B., and P. Green. 1998. Basecalling of automated sequencer traces using phred. II. Error probabilities. Genome Res. 8:186-194.
    • (1998) Genome Res. , vol.8 , pp. 186-194
    • Ewing, B.1    Green, P.2
  • 23
    • 0031955518 scopus 로고    scopus 로고
    • Basecalling of automated sequencer traces using phred. I. Accuracy assessment
    • Ewing, B., L. Hillier, M. Wendl, and P. Green. 1998. Basecalling of automated sequencer traces using phred. I. Accuracy assessment. Genome Res. 8:175-185.
    • (1998) Genome Res. , vol.8 , pp. 175-185
    • Ewing, B.1    Hillier, L.2    Wendl, M.3    Green, P.4
  • 24
    • 0000122573 scopus 로고
    • PHYLIP-Phytogeny Inference Package (version 3.2)
    • Felsenstein, J. 1989. PHYLIP-Phytogeny Inference Package (version 3.2). Cladistics 5:164-166.
    • (1989) Cladistics , vol.5 , pp. 164-166
    • Felsenstein, J.1
  • 26
    • 0037701544 scopus 로고    scopus 로고
    • Molecular analysis of the copper-transporting efflux system CusCFBA of Escherichia coli
    • Franke, S., G. Grass, C. Rensing, and D. H. Nies. 2003. Molecular analysis of the copper-transporting efflux system CusCFBA of Escherichia coli. J. Bacteriol. 185:3804-3812.
    • (2003) J. Bacteriol. , vol.185 , pp. 3804-3812
    • Franke, S.1    Grass, G.2    Rensing, C.3    Nies, D.H.4
  • 29
    • 0343618612 scopus 로고    scopus 로고
    • Adenylylsulfate reductases from archaea and bacteria are 1:1 αβ-heterodimeric iron-sulfur flavoenzymes-high similarity of molecular properties emphasizes their central role in sulfur metabolism
    • Fritz, G., T. Büchert, H. Huber, K. O. Stetter, and P. M. H. Kroneck. 2000. Adenylylsulfate reductases from archaea and bacteria are 1:1 αβ-heterodimeric iron-sulfur flavoenzymes-high similarity of molecular properties emphasizes their central role in sulfur metabolism. FEBS Lett. 473:63-66.
    • (2000) FEBS Lett. , vol.473 , pp. 63-66
    • Fritz, G.1    Büchert, T.2    Huber, H.3    Stetter, K.O.4    Kroneck, P.M.H.5
  • 30
    • 12144278799 scopus 로고    scopus 로고
    • Biochemical characterization of phosphoryl transfer involving HPr of the phosphoenolpyruvate-dependent phosphotransferase system in Treponema denticola, an organism that lacks PTS permeases
    • Gonzalez, C. F., A. J. Stonestrom, G. L. Lorca, and M. H. Saier. 2005. Biochemical characterization of phosphoryl transfer involving HPr of the phosphoenolpyruvate-dependent phosphotransferase system in Treponema denticola, an organism that lacks PTS permeases. Biochemistry 44:598-608.
    • (2005) Biochemistry , vol.44 , pp. 598-608
    • Gonzalez, C.F.1    Stonestrom, A.J.2    Lorca, G.L.3    Saier, M.H.4
  • 31
    • 0031955116 scopus 로고    scopus 로고
    • Consed: A graphical tool for sequence finishing
    • Gordon, D., C. Abajian, and P. Green. 1998. Consed: a graphical tool for sequence finishing. Genome Res. 8:195-202.
    • (1998) Genome Res. , vol.8 , pp. 195-202
    • Gordon, D.1    Abajian, C.2    Green, P.3
  • 32
    • 0034817086 scopus 로고    scopus 로고
    • CueO is a multi-copper oxidase that confers copper tolerance in Escherichia coli
    • Grass, G., and C. Rensing. 2001. CueO is a multi-copper oxidase that confers copper tolerance in Escherichia coli. Biochem. Biophys. Res. Commun. 286:902-908.
    • (2001) Biochem. Biophys. Res. Commun. , vol.286 , pp. 902-908
    • Grass, G.1    Rensing, C.2
  • 33
    • 0031577711 scopus 로고    scopus 로고
    • The novel genes, cbbQ and cbbO, located downstream from the RubisCO genes of Pseudomonas hydrogenothermophila, affect the conformational states and activity of RubisCO
    • Hayashi, N. R., H. Arai, T. Kodama, and Y. Igarashi. 1997. The novel genes, cbbQ and cbbO, located downstream from the RubisCO genes of Pseudomonas hydrogenothermophila, affect the conformational states and activity of RubisCO. Biochem. Biophys. Res. Commun. 241:565-569.
    • (1997) Biochem. Biophys. Res. Commun. , vol.241 , pp. 565-569
    • Hayashi, N.R.1    Arai, H.2    Kodama, T.3    Igarashi, Y.4
  • 35
    • 0030033929 scopus 로고    scopus 로고
    • Deduced amino acid sequence, functional expression, and unique enzymatic properties of the form I and form II ribulose bisphosphate carboxylase/oxygenase from the chemoautotrophic bacterium Thiobacillus denitrificans
    • Hernandez, J. M., S. H. Baker, S. C. Lorbach, J. M. Shively, and F. R. Tabita. 1996. Deduced amino acid sequence, functional expression, and unique enzymatic properties of the form I and form II ribulose bisphosphate carboxylase/oxygenase from the chemoautotrophic bacterium Thiobacillus denitrificans. J. Bacteriol. 178:347-356.
    • (1996) J. Bacteriol. , vol.178 , pp. 347-356
    • Hernandez, J.M.1    Baker, S.H.2    Lorbach, S.C.3    Shively, J.M.4    Tabita, F.R.5
  • 37
    • 0344393479 scopus 로고    scopus 로고
    • Chemolithoorganotrophic growth of Nitrosomonas europaea on fructose
    • Hommes, N. G., L. A. Sayavedra-Soto, and D. J. Arp. 2003. Chemolithoorganotrophic growth of Nitrosomonas europaea on fructose. J. Bacteriol. 185:6809-6814.
    • (2003) J. Bacteriol. , vol.185 , pp. 6809-6814
    • Hommes, N.G.1    Sayavedra-Soto, L.A.2    Arp, D.J.3
  • 39
    • 0035093274 scopus 로고    scopus 로고
    • Evidence for two pathways of thiosulfate oxidation in Starkeya novella (formerly Thiobacillus novellas)
    • Kappler, U., C. G. Friedrich, H. G. Trüper, and C. Dabl. 2001. Evidence for two pathways of thiosulfate oxidation in Starkeya novella (formerly Thiobacillus novellas). Arch. Microbiol. 175:102-111.
    • (2001) Arch. Microbiol. , vol.175 , pp. 102-111
    • Kappler, U.1    Friedrich, C.G.2    Trüper, H.G.3    Dabl, C.4
  • 40
    • 1842332701 scopus 로고    scopus 로고
    • Compositional biases of bacterial genomes and evolutionary implications
    • Karlin, S., J. Mrazek, and A. M. Campbell. 1997. Compositional biases of bacterial genomes and evolutionary implications. J. Bacteriol. 179:3899-3913.
    • (1997) J. Bacteriol. , vol.179 , pp. 3899-3913
    • Karlin, S.1    Mrazek, J.2    Campbell, A.M.3
  • 41
    • 0014164828 scopus 로고
    • The incorporation of acetate by the chemoautotroph Thiobacillus neapolitanus strain C
    • Kelly, D. P. 1967. The incorporation of acetate by the chemoautotroph Thiobacillus neapolitanus strain C. Arch. Mikrobiol. 58:99-116.
    • (1967) Arch. Mikrobiol. , vol.58 , pp. 99-116
    • Kelly, D.P.1
  • 42
    • 0020481782 scopus 로고
    • Biochemistry of the chemolithotrophic oxidation of inorganic sulphur
    • Kelly, D. P. 1982. Biochemistry of the chemolithotrophic oxidation of inorganic sulphur. Philos. Trans. R. Soc. Lond. B Biol. Sci. 298:499-528.
    • (1982) Philos. Trans. R. Soc. Lond. B Biol. Sci. , vol.298 , pp. 499-528
    • Kelly, D.P.1
  • 43
    • 0000897154 scopus 로고
    • Physiology and biochemistry of unicellular sulfur bacteria
    • H. G. Schlegel and B. Bowien (ed.). Science Tech Publishers, Madison, Wis.
    • Kelly, D. P. 1989. Physiology and biochemistry of unicellular sulfur bacteria, p. 193-217. In H. G. Schlegel and B. Bowien (ed.), Biology of autotrophic bacteria. Science Tech Publishers, Madison, Wis.
    • (1989) Biology of Autotrophic Bacteria , pp. 193-217
    • Kelly, D.P.1
  • 44
    • 0041198806 scopus 로고
    • Energetics of chemolithotrophic bacteria
    • T. A. Krulwich (ed.). Academic Press, San Diego, Calif.
    • Kelly, D. P. 1990. Energetics of chemolithotrophic bacteria, p. 479-503. In T. A. Krulwich (ed.), Bacterial energetics, Academic Press, San Diego, Calif.
    • (1990) Bacterial Energetics , pp. 479-503
    • Kelly, D.P.1
  • 45
    • 0032940452 scopus 로고    scopus 로고
    • Thermodynamic aspects of energy conservation by chemolithotrophic sulfur bacteria in relation to the sulfur oxidation pathways
    • Kelly, D. P. 1999. Thermodynamic aspects of energy conservation by chemolithotrophic sulfur bacteria in relation to the sulfur oxidation pathways. Arch. Microbiol. 171:219-229.
    • (1999) Arch. Microbiol. , vol.171 , pp. 219-229
    • Kelly, D.P.1
  • 46
    • 0000650063 scopus 로고
    • Genus Thiobacillus
    • J. T. Staley, M. P. Bryant, N. Pfennig, and J. G. Holt (ed.). Williams & Wilkins, Baltimore, Md.
    • Kelly, D. P., and A. P. Harrison. 1989. Genus Thiobacillus, p. 1842-1858. In J. T. Staley, M. P. Bryant, N. Pfennig, and J. G. Holt (ed.), Bergey's manual of systematic bacteriology, 1st ed., vol. 3. Williams & Wilkins, Baltimore, Md.
    • (1989) Bergey's Manual of Systematic Bacteriology, 1st Ed. , vol.3 , pp. 1842-1858
    • Kelly, D.P.1    Harrison, A.P.2
  • 47
    • 0034108430 scopus 로고    scopus 로고
    • Confirmation of Thiobacillus denitrificans as a species of the genus Thiobacillus, in the beta-subclass of the Proteobacteria, with strain NCIMB 9548 as the type strain
    • Kelly, D. P., and A. P. Wood. 2000. Confirmation of Thiobacillus denitrificans as a species of the genus Thiobacillus, in the beta-subclass of the Proteobacteria, with strain NCIMB 9548 as the type strain. Int. J. Syst. Evol. Microbiol. 50:547-550.
    • (2000) Int. J. Syst. Evol. Microbiol. , vol.50 , pp. 547-550
    • Kelly, D.P.1    Wood, A.P.2
  • 48
    • 2642517373 scopus 로고    scopus 로고
    • The chemolithotrophic prokaryotes
    • M. Dworkin, S. Falkow, E. Rosenberg, K.-H. Schleifer, and E. Stackebrandt (ed.). Springer-Verlag, New York, N.Y. [Online]
    • Kelly, D. P., and A. P. Wood. 2000. The chemolithotrophic prokaryotes. In M. Dworkin, S. Falkow, E. Rosenberg, K.-H. Schleifer, and E. Stackebrandt (ed.), The prokaryotes, an evolving electronic resource for the microbiological community (PKIIIE). Springer-Verlag, New York, N.Y. [Online.] http: //www.prokaryotes.com.
    • (2000) The Prokaryotes, An Evolving Electronic Resource for the Microbiological Community (PKIIIE)
    • Kelly, D.P.1    Wood, A.P.2
  • 49
    • 32444441814 scopus 로고    scopus 로고
    • Genus II. Thiobacillus Beijerinck
    • G. M. Garrity (eds.). Springer, New York, N.Y.
    • Kelly, D. P., A. P. Wood, and E. Stackebrandt. 2005. Genus II. Thiobacillus Beijerinck, p. 764-769. In G. M. Garrity (eds.), Bergey's manual of systematic bacteriology, 2nd ed., vol. 2, part C. Springer, New York, N.Y.
    • (2005) Bergey's Manual of Systematic Bacteriology, 2nd Ed. , vol.2 , Issue.PART C , pp. 764-769
    • Kelly, D.P.1    Wood, A.P.2    Stackebrandt, E.3
  • 50
    • 0031032795 scopus 로고    scopus 로고
    • Oxidative metabolism of inorganic sulfur compounds by bacteria
    • Kelly, D. P., J. K. Shergill, W. P. Lu, and A. P. Wood. 1997. Oxidative metabolism of inorganic sulfur compounds by bacteria. Antonie Leeuwenhoek 71:95-107.
    • (1997) Antonie Leeuwenhoek , vol.71 , pp. 95-107
    • Kelly, D.P.1    Shergill, J.K.2    Lu, W.P.3    Wood, A.P.4
  • 51
    • 0035883519 scopus 로고    scopus 로고
    • Behavior of restriction-modification systems as selfish mobile elements and their impact on genome evolution
    • Kobayashi, I. 2001. Behavior of restriction-modification systems as selfish mobile elements and their impact on genome evolution. Nucleic Acids Res. 29:3742-3756.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 3742-3756
    • Kobayashi, I.1
  • 52
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes
    • Krogh, A., B. Larsson, G. von Heijne, and E. L. L. Sonnhammer. 2001. Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes. J. Mol. Biol. 305:567-580.
    • (2001) J. Mol. Biol. , vol.305 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    Von Heijne, G.3    Sonnhammer, E.L.L.4
  • 53
    • 0141814895 scopus 로고    scopus 로고
    • Membrane-bound hydrogenase and sulfur reductase of the hyperthermophilic and acidophilic archaeon Acidianus ambivalens
    • Laska, S., F. Lottspeich, and A. Kletzin. 2003. Membrane-bound hydrogenase and sulfur reductase of the hyperthermophilic and acidophilic archaeon Acidianus ambivalens. Microbiology 149:2357-2371.
    • (2003) Microbiology , vol.149 , pp. 2357-2371
    • Laska, S.1    Lottspeich, F.2    Kletzin, A.3
  • 55
    • 0037565061 scopus 로고    scopus 로고
    • Efflux-mediated heavy metal resistance in prokaryotes
    • Nies, D. H. 2003. Efflux-mediated heavy metal resistance in prokaryotes. FEMS Microbiol. Rev. 27:313-339.
    • (2003) FEMS Microbiol. Rev. , vol.27 , pp. 313-339
    • Nies, D.H.1
  • 57
    • 0014879992 scopus 로고
    • The tricarboxylic acid cycle in Thiobacillus denitrificans and Thiobacillus-A2
    • Peeters, T. L., M. S. Liu, and M. I. H. Aleem. 1970. The tricarboxylic acid cycle in Thiobacillus denitrificans and Thiobacillus-A2. J. Gen. Microbiol. 64:29-35.
    • (1970) J. Gen. Microbiol. , vol.64 , pp. 29-35
    • Peeters, T.L.1    Liu, M.S.2    Aleem, M.I.H.3
  • 58
    • 1942504686 scopus 로고    scopus 로고
    • Proton pathways, ligand binding and dynamics of the catalytic site in haem-copper oxygen reductases: A comparison between the three families
    • Pereira, M. M., and M. Teixeira. 2004. Proton pathways, ligand binding and dynamics of the catalytic site in haem-copper oxygen reductases: a comparison between the three families. Biochim. Biophys. Acta 1655:340-346.
    • (2004) Biochim. Biophys. Acta , vol.1655 , pp. 340-346
    • Pereira, M.M.1    Teixeira, M.2
  • 59
    • 0035853451 scopus 로고    scopus 로고
    • Phytogeny and distribution of the soxB gene among thiosulfate-oxidizing bacteria
    • Petri, R., L. Podgorsek, and J. F. Imhoff. 2001. Phytogeny and distribution of the soxB gene among thiosulfate-oxidizing bacteria. FEMS Microbiol. Lett. 197:171-178.
    • (2001) FEMS Microbiol. Lett. , vol.197 , pp. 171-178
    • Petri, R.1    Podgorsek, L.2    Imhoff, J.F.3
  • 60
    • 0037184270 scopus 로고    scopus 로고
    • Denitrifying genes in bacterial and Archaeal genomes
    • Philippot, L. 2002. Denitrifying genes in bacterial and Archaeal genomes. Biochim. Biophys. Acta 1577:355-376.
    • (2002) Biochim. Biophys. Acta , vol.1577 , pp. 355-376
    • Philippot, L.1
  • 62
    • 0031855745 scopus 로고    scopus 로고
    • Sirohaem sulfite reductase and other proteins encoded by genes at the dsr locus of Chromatium vinosum are involved in the oxidation of intracellular sulfur
    • Pott, A. S., and C. Dahl. 1998. Sirohaem sulfite reductase and other proteins encoded by genes at the dsr locus of Chromatium vinosum are involved in the oxidation of intracellular sulfur. Microbiology (Reading) 144:1881-1894.
    • (1998) Microbiology (Reading) , vol.144 , pp. 1881-1894
    • Pott, A.S.1    Dahl, C.2
  • 63
    • 0344495378 scopus 로고    scopus 로고
    • Sulfur oxidation in Paracoccus pantotrophus: Interaction of the sulfur-binding protein SoxYZ with the dimanganese SoxB protein
    • Quentmeier, A., P. Hellwig, F. Bardichewsky, G. Grolle, R. Kraft, and C. G. Friedrich. 2003. Sulfur oxidation in Paracoccus pantotrophus: interaction of the sulfur-binding protein SoxYZ with the dimanganese SoxB protein. Biochem. Biophys. Res. Commun. 312:1011-1018.
    • (2003) Biochem. Biophys. Res. Commun. , vol.312 , pp. 1011-1018
    • Quentmeier, A.1    Hellwig, P.2    Bardichewsky, F.3    Grolle, G.4    Kraft, R.5    Friedrich, C.G.6
  • 64
    • 8744255663 scopus 로고    scopus 로고
    • Sulfide dehydrogenase activity of the monomeric flavoprotein SoxF of Paracoccus pantotrophus
    • Quentmeier, A., P. Hellwig, F. Bardichewsky, R. Wichmann, and C. G. Friedrich. 2004. Sulfide dehydrogenase activity of the monomeric flavoprotein SoxF of Paracoccus pantotrophus. Biochemistry 43:14696-14703.
    • (2004) Biochemistry , vol.43 , pp. 14696-14703
    • Quentmeier, A.1    Hellwig, P.2    Bardichewsky, F.3    Wichmann, R.4    Friedrich, C.G.5
  • 65
    • 0033976381 scopus 로고    scopus 로고
    • Characterization of a new type of sulfite dehydrogenase from Paracoccus pantotrophus GB17
    • Quentmeier, A., R. Kraft, S. Kostka, R. Klockemkaper, and C. G. Friedrich. 2000. Characterization of a new type of sulfite dehydrogenase from Paracoccus pantotrophus GB17. Arch. Microbiol. 173:117-125.
    • (2000) Arch. Microbiol. , vol.173 , pp. 117-125
    • Quentmeier, A.1    Kraft, R.2    Kostka, S.3    Klockemkaper, R.4    Friedrich, C.G.5
  • 66
    • 0031894326 scopus 로고    scopus 로고
    • Unusual organization of the genes coding for HydSL, the stable [NiFe]hydrogenase in the photosynthetic bacterium Thiocapsa roseopersicina BBS
    • Rakhely, G., A. Colbeau, J. Garin, P. M. Vignais, and K. L. Kovacs. 1998. Unusual organization of the genes coding for HydSL, the stable [NiFe]hydrogenase in the photosynthetic bacterium Thiocapsa roseopersicina BBS. J. Bacteriol. 180:1460-1465.
    • (1998) J. Bacteriol. , vol.180 , pp. 1460-1465
    • Rakhely, G.1    Colbeau, A.2    Garin, J.3    Vignais, P.M.4    Kovacs, K.L.5
  • 67
    • 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 C. G. Friedrich. 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
  • 68
    • 0034932333 scopus 로고    scopus 로고
    • Novel genes of the sox gene cluster, mutagenesis of the flavoprotein SoxF, and evidence for a general sulfur-oxidizing system in Paracoccus pantotrophus GB17
    • Rother, D., H. J. Henrich, A. Quentmeier, F. Bardichewsky, and C. G. Friedrich. 2001. Novel genes of the sox gene cluster, mutagenesis of the flavoprotein SoxF, and evidence for a general sulfur-oxidizing system in Paracoccus pantotrophus GB17. J. Bacteriol. 183:4499-4508.
    • (2001) J. Bacteriol. , vol.183 , pp. 4499-4508
    • Rother, D.1    Henrich, H.J.2    Quentmeier, A.3    Bardichewsky, F.4    Friedrich, C.G.5
  • 69
    • 0017388181 scopus 로고
    • Sulphite-dependent nitrate reductase and NADH-dependent nitrate reductase from Thiobacillus denitrificans
    • Sawnhey, V., and D. J. D. Nicholas. 1977. Sulphite-dependent nitrate reductase and NADH-dependent nitrate reductase from Thiobacillus denitrificans. J. Gen. Microbiol. 100:49-58.
    • (1977) J. Gen. Microbiol. , vol.100 , pp. 49-58
    • Sawnhey, V.1    Nicholas, D.J.D.2
  • 70
    • 0017814120 scopus 로고
    • Sulphide-linked nitrite reductase from Thiobacillus denitrificans with cytochrome oxidase activity: Purification and properties
    • Sawnhey, V., and D. J. D. Nicholas. 1978. Sulphide-linked nitrite reductase from Thiobacillus denitrificans with cytochrome oxidase activity: purification and properties. J. Gen. Microbiol. 106:119-128.
    • (1978) J. Gen. Microbiol. , vol.106 , pp. 119-128
    • Sawnhey, V.1    Nicholas, D.J.D.2
  • 71
    • 0018429082 scopus 로고
    • Purification of Thiobacillus-denitrificans siroheme sulfite reductase and investigation of some molecular and catalytic properties
    • Schedel, M., and H. G. Trüper. 1979. Purification of Thiobacillus-denitrificans siroheme sulfite reductase and investigation of some molecular and catalytic properties. Biochim. Biophys. Acta 568:454-466.
    • (1979) Biochim. Biophys. Acta , vol.568 , pp. 454-466
    • Schedel, M.1    Trüper, H.G.2
  • 72
    • 0014735658 scopus 로고
    • Comparative ultrastructure of the thiobacilli
    • Shively, J. M., G. L. Decker, and J. W. Greenawalt. 1970. Comparative ultrastructure of the thiobacilli. J. Bacteriol. 101:618-627.
    • (1970) J. Bacteriol. , vol.101 , pp. 618-627
    • Shively, J.M.1    Decker, G.L.2    Greenawalt, J.W.3
  • 73
    • 0017395208 scopus 로고
    • Specialist phototrophs, lithotrophs, and methylotrophs: A unity among a diversity of prokaryotes?
    • Smith, A. J., and D. S. Hoare. 1977. Specialist phototrophs, lithotrophs, and methylotrophs: a unity among a diversity of prokaryotes? Bacteriol. Rev. 41:419-448.
    • (1977) Bacteriol. Rev. , vol.41 , pp. 419-448
    • Smith, A.J.1    Hoare, D.S.2
  • 74
    • 1642500161 scopus 로고    scopus 로고
    • A novel evolutionary lineage of carbonic anhydrase (ε class) is a component of the carboxysome shell
    • So, A. K.-C., G. S. Espie, E. B. Williams, J. M. Shively, S. Heinhorst, and G. C. Cannon. 2004. A novel evolutionary lineage of carbonic anhydrase (ε class) is a component of the carboxysome shell. J. Bacteriol. 186:623-630.
    • (2004) J. Bacteriol. , vol.186 , pp. 623-630
    • So, A.K.-C.1    Espie, G.S.2    Williams, E.B.3    Shively, J.M.4    Heinhorst, S.5    Cannon, G.C.6
  • 75
    • 0031614678 scopus 로고    scopus 로고
    • A hidden Markov model for predicting transmembrane helices in protein sequences
    • J. Glasgow, T. Littlejohn, F. Major, R. Lathrop, D. Sankoff, and C. Sensen (ed.). AAAI Press, Menlo Park, CA
    • Sonnhammer, E. L. L., G. von Heijne, and A. Krogh. 1998. A hidden Markov model for predicting transmembrane helices in protein sequences, p. 175-182. In J. Glasgow, T. Littlejohn, F. Major, R. Lathrop, D. Sankoff, and C. Sensen (ed.), Proceedings of the Sixth International Conference on Intelligent Systems for Molecular Biology. AAAI Press, Menlo Park, CA.
    • (1998) Proceedings of the Sixth International Conference on Intelligent Systems for Molecular Biology , pp. 175-182
    • Sonnhammer, E.L.L.1    Von Heijne, G.2    Krogh, A.3
  • 76
    • 4344621662 scopus 로고    scopus 로고
    • Anaerobic growth of the haloalkaliphilic denitrifying sulfur-oxidizing bacterium Thialkalivibrio thiocyanodenitrificans sp. nov. with thiocyanate
    • Sorokin, D. Y., T. P. Tourova, A. N. Antipov, G. Muyzer, and J. G. Kuenen. 2004. Anaerobic growth of the haloalkaliphilic denitrifying sulfur-oxidizing bacterium Thialkalivibrio thiocyanodenitrificans sp. nov. with thiocyanate. Microbiology (Reading) 150:2435-2442.
    • (2004) Microbiology (Reading) , vol.150 , pp. 2435-2442
    • Sorokin, D.Y.1    Tourova, T.P.2    Antipov, A.N.3    Muyzer, G.4    Kuenen, J.G.5
  • 78
    • 0029898080 scopus 로고    scopus 로고
    • Anaerobic, nitrate-dependent microbial oxidation of ferrous iron
    • Straub, K. L., M. Benz, B. Schink, and F. Widdel. 1996. Anaerobic, nitrate-dependent microbial oxidation of ferrous iron. Appl. Environ. Microbiol. 62:1458-1460.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 1458-1460
    • Straub, K.L.1    Benz, M.2    Schink, B.3    Widdel, F.4
  • 79
    • 0032428054 scopus 로고    scopus 로고
    • Sulfur oxidation in rice field soil: Activity, enumeration, isolation and characterization of thiosulfate-oxidizing bacteria
    • Stubner, S., T. Wind, and R. Conrad. 1998. Sulfur oxidation in rice field soil: activity, enumeration, isolation and characterization of thiosulfate-oxidizing bacteria. Syst. Appl. Microbiol. 21:569-578.
    • (1998) Syst. Appl. Microbiol. , vol.21 , pp. 569-578
    • Stubner, S.1    Wind, T.2    Conrad, R.3
  • 80
    • 0344837851 scopus 로고    scopus 로고
    • Microbial populations stimulated for hexavalent uranium reduction in uranium mine sediment
    • Suzuki, Y., S. D. Kelly, K. M. Kemner, and J. F. Banfield. 2003. Microbial populations stimulated for hexavalent uranium reduction in uranium mine sediment. Appl. Environ. Microbiol. 69:1337-1346.
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 1337-1346
    • Suzuki, Y.1    Kelly, S.D.2    Kemner, K.M.3    Banfield, J.F.4
  • 81
    • 0344066218 scopus 로고    scopus 로고
    • Identification and characterization of genes required for biosynthesis and transport of the siderophore vibrioferrin in Vibrio parahaemolyticus
    • Tanabe, T., T. Funahashi, H. Nakao, S. Miyoshi, S. Shinoda, and S. Yamamoto. 2003. Identification and characterization of genes required for biosynthesis and transport of the siderophore vibrioferrin in Vibrio parahaemolyticus. J. Bacteriol. 185:6938-6949.
    • (2003) J. Bacteriol. , vol.185 , pp. 6938-6949
    • Tanabe, T.1    Funahashi, T.2    Nakao, H.3    Miyoshi, S.4    Shinoda, S.5    Yamamoto, S.6
  • 82
    • 0033956060 scopus 로고    scopus 로고
    • The COG database: A tool for genome-scale analysis of protein functions and evolution
    • Tatusov, R. L., M. Y. Galperin, D. A. Natale, and E. V. Koonin. 2000. The COG database: a tool for genome-scale analysis of protein functions and evolution. Nucleic Acids Res. 28:33-36.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 33-36
    • Tatusov, R.L.1    Galperin, M.Y.2    Natale, D.A.3    Koonin, E.V.4
  • 83
    • 0015168640 scopus 로고
    • Thiobacillus denitrificans as an obligate chemolithoautotroph. Cell suspension and enzymic studies
    • Taylor, B. F., and D. S. Hoare. 1971. Thiobacillus denitrificans as an obligate chemolithoautotroph. Cell suspension and enzymic studies. Arch. Mikrobiol. 80:262-276.
    • (1971) Arch. Mikrobiol. , vol.80 , pp. 262-276
    • Taylor, B.F.1    Hoare, D.S.2
  • 84
    • 0014993547 scopus 로고
    • Thiobacillus denitrificans as an obligate chemolithoautotroph. Isolation and growth studies
    • Taylor, B. F., D. S. Hoare, and S. L. Hoare. 1971. Thiobacillus denitrificans as an obligate chemolithoautotroph. Isolation and growth studies. Arch. Mikrobiol. 78:193-204.
    • (1971) Arch. Mikrobiol. , vol.78 , pp. 193-204
    • Taylor, B.F.1    Hoare, D.S.2    Hoare, S.L.3
  • 85
    • 49549142424 scopus 로고
    • A new type of thiosulfate oxidizing, nitrate reducing microorganism: Thiomicrospira denitrificans sp. nov
    • Timmer-Ten Hoor, A. 1975. A new type of thiosulfate oxidizing, nitrate reducing microorganism: Thiomicrospira denitrificans sp. nov. Neth. J. Sea Res. 9:344-350.
    • (1975) Neth. J. Sea Res. , vol.9 , pp. 344-350
    • Timmer-Ten Hoor, A.1
  • 86
    • 0028673855 scopus 로고
    • Reverse siroheme sulfite reductase from Thiobacillus denitrificans
    • Trüper, H. G. 1994. Reverse siroheme sulfite reductase from Thiobacillus denitrificans. Meth. Enzymol. 243:422-426.
    • (1994) Meth. Enzymol. , vol.243 , pp. 422-426
    • Trüper, H.G.1
  • 87
    • 0034886919 scopus 로고    scopus 로고
    • Classification and phytogeny of hydrogenases
    • Vignais, P. M., B. Billoud, and J. Meyer. 2001. Classification and phytogeny of hydrogenases. FEMS Microbiol. Rev. 25:455-501.
    • (2001) FEMS Microbiol. Rev. , vol.25 , pp. 455-501
    • Vignais, P.M.1    Billoud, B.2    Meyer, J.3
  • 88
    • 0030872086 scopus 로고    scopus 로고
    • Characterization of Thiobacillus thioparus LV43 and its distribution in a chemoautotrophically based groundwater ecosystem
    • Vlasceanu, L., R. Popa, and B. K. Kinkle. 1997. Characterization of Thiobacillus thioparus LV43 and its distribution in a chemoautotrophically based groundwater ecosystem. Appl. Environ. Microbiol. 63:3123-3127.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 3123-3127
    • Vlasceanu, L.1    Popa, R.2    Kinkle, B.K.3
  • 91
    • 0028149485 scopus 로고
    • Identification and sequence analysis of the soxB gene essential for sulfur oxidation of Paracoccus denitrificans GB17
    • Wodara, C., S. Kostka, M. Egert, D. P. Kelly, and C. G. Friedrich. 1994. Identification and sequence analysis of the soxB gene essential for sulfur oxidation of Paracoccus denitrificans GB17. J. Bacteriol. 176:6188-6191.
    • (1994) J. Bacteriol. , vol.176 , pp. 6188-6191
    • Wodara, C.1    Kostka, S.2    Egert, M.3    Kelly, D.P.4    Friedrich, C.G.5
  • 92
    • 2642562680 scopus 로고    scopus 로고
    • A challenge for 21st century molecular biology and biochemistry: What are the causes of obligate autotrophy and methanotrophy?
    • Wood, A. P., J. P. Aurikko, and D. P. Kelly. 2004. A challenge for 21st century molecular biology and biochemistry: what are the causes of obligate autotrophy and methanotrophy? FEMS Microbiol. Rev. 28:335-352.
    • (2004) FEMS Microbiol. Rev. , vol.28 , pp. 335-352
    • Wood, A.P.1    Aurikko, J.P.2    Kelly, D.P.3
  • 93
    • 0033564555 scopus 로고    scopus 로고
    • Transcription factor GCN4 for control of amino acid biosynthesis also regulates the expression of the gene for lipoamide dehydrogenase
    • Zaman, Z., S. B. Bowman, G. D. Kornfeld, A. J. Brown, and I. W. Dawes. 1999. Transcription factor GCN4 for control of amino acid biosynthesis also regulates the expression of the gene for lipoamide dehydrogenase. Biochem. J. 340:855-862.
    • (1999) Biochem. J. , vol.340 , pp. 855-862
    • Zaman, Z.1    Bowman, S.B.2    Kornfeld, G.D.3    Brown, A.J.4    Dawes, I.W.5
  • 94
    • 0031456471 scopus 로고    scopus 로고
    • Cell biology and molecular basis of denitrification
    • Zumft, W. G. 1997. Cell biology and molecular basis of denitrification. Microbiol. Mol. Biol. Rev. 61:533-616.
    • (1997) Microbiol. Mol. Biol. Rev. , vol.61 , pp. 533-616
    • Zumft, W.G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.