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Volumn 5, Issue 1, 2005, Pages 18-29

Domain evolution and functional diversification of sulfite reductases

Author keywords

Anaerobic sulfite reductase; Assimilatory sulfite reductase; Dissimilatory sulfite reductase; Low molecular weight assimilatory sulfite reductase

Indexed keywords

OXIDOREDUCTASE;

EID: 14844304279     PISSN: 15311074     EISSN: None     Source Type: Journal    
DOI: 10.1089/ast.2005.5.18     Document Type: Article
Times cited : (52)

References (53)
  • 4
    • 0019999193 scopus 로고
    • Sulfate and sulfate reduction in early Precambrian oceans
    • Cameron, E.M. (1982) Sulfate and sulfate reduction in early Precambrian oceans. Nature 296, 145-148.
    • (1982) Nature , vol.296 , pp. 145-148
    • Cameron, E.M.1
  • 5
    • 0039657184 scopus 로고    scopus 로고
    • The evolution of the sulfur cycle
    • Canfield, D.E. and Raiswell, R. (1999) The evolution of the sulfur cycle. Am. J. Sci. 299, 697-723.
    • (1999) Am. J. Sci. , vol.299 , pp. 697-723
    • Canfield, D.E.1    Raiswell, R.2
  • 6
    • 0035094993 scopus 로고    scopus 로고
    • 12 dependent anaerobic growth of Salmonella enterica serovar typhimurium on ethanolamine or 1,2 propane-diol
    • 12 dependent anaerobic growth of Salmonella enterica serovar typhimurium on ethanolamine or 1,2 propane-diol. J. Bacteriol. 183, 2463-2475.
    • (2001) J. Bacteriol. , vol.183 , pp. 2463-2475
    • Carter, M.P.1    Tingey, J.2    Bobik, T.A.3    Roth, J.R.4
  • 7
    • 0023262821 scopus 로고
    • The phs gene and hydrogen sulfide production by Salmonella typhimurium
    • Clark, M. and Barrett, E.L. (1987) The phs gene and hydrogen sulfide production by Salmonella typhimurium. J. Bacteriol. 169, 2391-2397.
    • (1987) J. Bacteriol. , vol.169 , pp. 2391-2397
    • Clark, M.1    Barrett, E.L.2
  • 8
    • 0028809514 scopus 로고
    • Sulfite reductase structure at 1.6Å: Evolution and catalysis for reduction of inorganic anions
    • Crane, B.R. and Getzoff, E.D. (1995) Sulfite reductase structure at 1.6Å: Evolution and catalysis for reduction of inorganic anions. Science 270, 59-67.
    • (1995) Science , vol.270 , pp. 59-67
    • Crane, B.R.1    Getzoff, E.D.2
  • 9
    • 0030472457 scopus 로고    scopus 로고
    • The relation between structure and function for sulfite reductases
    • Crane, B.R., Siegel, L.M., and Getzoff, E.D. (1996) The relation between structure and function for sulfite reductases. Curr. Opin. Struct. Biol. 6, 744-756.
    • (1996) Curr. Opin. Struct. Biol. , vol.6 , pp. 744-756
    • Crane, B.R.1    Siegel, L.M.2    Getzoff, E.D.3
  • 10
    • 0025034584 scopus 로고
    • Purification and characterization of ATP sulfurylase from the extremely thermophilic archaebacterial sulfate reducer, Archaeoglobus fulgidus
    • Dahl, C., Koch, H.G., Keuken, O., and Trüper, H.G. (1990) Purification and characterization of ATP sulfurylase from the extremely thermophilic archaebacterial sulfate reducer, Archaeoglobus fulgidus. FEMS Microbiol. Lett. 67, 27-32.
    • (1990) FEMS Microbiol. Lett. , vol.67 , pp. 27-32
    • Dahl, C.1    Koch, H.G.2    Keuken, O.3    Trüper, H.G.4
  • 11
    • 0027275049 scopus 로고
    • Dissimilatory sulfite reductase from Archaeoglobus fulgidus: Physico-chemical properties of the enzyme and cloning, sequencing and analysis of reductase genes
    • Dahl, C., Kredich, N.M., Deutzmann, R., and Trüper, H.G. (1993) Dissimilatory sulfite reductase from Archaeoglobus fulgidus: Physico-chemical properties of the enzyme and cloning, sequencing and analysis of reductase genes. J. Gen. Microbiol. 139, 1817-1828.
    • (1993) J. Gen. Microbiol. , vol.139 , pp. 1817-1828
    • Dahl, C.1    Kredich, N.M.2    Deutzmann, R.3    Trüper, H.G.4
  • 12
    • 0013258174 scopus 로고    scopus 로고
    • Molecular characterization of sulfate reducing bacteria in the Guaymas Basin
    • Dhillon, A., Teske, A., Dillon, J., Stahl, D., and Sogin, M.L. (2003) Molecular characterization of sulfate reducing bacteria in the Guaymas Basin. Appl. Environ. Microbiol. 69, 2765-2772.
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 2765-2772
    • Dhillon, A.1    Teske, A.2    Dillon, J.3    Stahl, D.4    Sogin, M.L.5
  • 13
    • 0027983037 scopus 로고
    • Convergent evolution: The need to be explicit
    • Doolittle, R.F. (1994) Convergent evolution: The need to be explicit. Trends Biochem. Sci. 19, 15-18.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 15-18
    • Doolittle, R.F.1
  • 15
    • 0036136241 scopus 로고    scopus 로고
    • Phylogenetic analysis reveals multiple lateral transfers of adenosine-5′-phosphosulfate reductase genes among sulfate-reducing microorganisms
    • Friedrich, M. (2002) Phylogenetic analysis reveals multiple lateral transfers of adenosine-5′-phosphosulfate reductase genes among sulfate-reducing microorganisms. J. Bacteriol. 184, 278-289.
    • (2002) J. Bacteriol. , vol.184 , pp. 278-289
    • Friedrich, M.1
  • 16
  • 17
    • 0027239614 scopus 로고
    • The ferredoxin: Sulfite reductase gene from Synechoccous PCC7942
    • Gisselmann, G., Klausmeier, P., and Schwenn, J.D. (1993) The ferredoxin: sulfite reductase gene from Synechoccous PCC7942. Biochim. Biophys. Acta 1144, 102-106.
    • (1993) Biochim. Biophys. Acta , vol.1144 , pp. 102-106
    • Gisselmann, G.1    Klausmeier, P.2    Schwenn, J.D.3
  • 18
    • 0021245669 scopus 로고
    • Purification and characterization of an inducible dissimilatory type sulfite reductase from Clostridium pasteurianum
    • Harrison, G., Curle, C., and Laishley, E.J. (1984) Purification and characterization of an inducible dissimilatory type sulfite reductase from Clostridium pasteurianum. Arch. Microbiol. 138, 72-78.
    • (1984) Arch. Microbiol. , vol.138 , pp. 72-78
    • Harrison, G.1    Curle, C.2    Laishley, E.J.3
  • 19
    • 0032954667 scopus 로고    scopus 로고
    • Structure and function of a cysBJIH gene cluster in the purple sulfur bacterium Thiocapsa roseopersicina
    • Haverkamp, T. and Schwenn, J. (1999) Structure and function of a cysBJIH gene cluster in the purple sulfur bacterium Thiocapsa roseopersicina. Microbiology 145, 115-125.
    • (1999) Microbiology , vol.145 , pp. 115-125
    • Haverkamp, T.1    Schwenn, J.2
  • 20
    • 0030821694 scopus 로고    scopus 로고
    • Towards the phylogeny of APS reductase and sirohaem sulfite reductases in sulfate reducing and sulfur-oxidizing prokaryotes
    • Hipp, W.M., Pott, A.S., Schmitz, N.T., Faath, I., Dahl, C., and Trüper, H.G. (1997) Towards the phylogeny of APS reductase and sirohaem sulfite reductases in sulfate reducing and sulfur-oxidizing prokaryotes. Microbiology 143, 2891-2902.
    • (1997) Microbiology , vol.143 , pp. 2891-2902
    • Hipp, W.M.1    Pott, A.S.2    Schmitz, N.T.3    Faath, I.4    Dahl, C.5    Trüper, H.G.6
  • 21
    • 0025973280 scopus 로고
    • Sequence analysis and expression of the Salmonella typhimurium asr operon encoding production of hydrogen sulfide from sulfite
    • Huang, C.J. and Barrett, E.L. (1991) Sequence analysis and expression of the Salmonella typhimurium asr operon encoding production of hydrogen sulfide from sulfite. J. Bacteriol. 173, 1544-1553.
    • (1991) J. Bacteriol. , vol.173 , pp. 1544-1553
    • Huang, C.J.1    Barrett, E.L.2
  • 22
    • 0345563260 scopus 로고    scopus 로고
    • Phylogenetic relationships among the Chromatiaceae, their taxonomic reclassification and description of the new genera Allochromatium, Halochromatium, Isochromatium, Marichromatium, Thiococcus, Thiohalo-capsa and Thermochromatium
    • Imhoff, J.F., Suling, J., and Petri, R. (1998) Phylogenetic relationships among the Chromatiaceae, their taxonomic reclassification and description of the new genera Allochromatium, Halochromatium, Isochromatium, Marichromatium, Thiococcus, Thiohalo-capsa and Thermochromatium. Int. J. Syst. Bacteriol. 48, 1129-1143.
    • (1998) Int. J. Syst. Bacteriol. , vol.48 , pp. 1129-1143
    • Imhoff, J.F.1    Suling, J.2    Petri, R.3
  • 23
    • 0031824941 scopus 로고    scopus 로고
    • Thermocladium modesticus gen. nov. sp. nov., a new genus of rod-shaped, extremely thermophilic creanarchaeota
    • Itoh, T., Suzuki, K., and Nakase, T. (1998) Thermocladium modesticus gen. nov. sp. nov., a new genus of rod-shaped, extremely thermophilic creanarchaeota. Int. J. Syst. Bacteriol. 48, 879-887.
    • (1998) Int. J. Syst. Bacteriol. , vol.48 , pp. 879-887
    • Itoh, T.1    Suzuki, K.2    Nakase, T.3
  • 24
    • 0033031775 scopus 로고    scopus 로고
    • Caldivirga maquilingensis gen. nov., sp. nov., a new genus of rod-shaped crenarchaeota isolated from a hot spring in the Phillippines
    • Itoh, T., Suzuki, K., Sanchez, P.C., and Nakase, T. (1999) Caldivirga maquilingensis gen. nov., sp. nov., a new genus of rod-shaped crenarchaeota isolated from a hot spring in the Phillippines. Int. J. Syst. Bacteriol. 49, 1157-1163.
    • (1999) Int. J. Syst. Bacteriol. , vol.49 , pp. 1157-1163
    • Itoh, T.1    Suzuki, K.2    Sanchez, P.C.3    Nakase, T.4
  • 25
    • 0041810237 scopus 로고    scopus 로고
    • Caldisphaera lagunensis gen. nov., sp. nov., a novel thermoacidophilic crenarchaeote isolated from a hot spring at Mt Maquiling, Philippines
    • Itoh, T., Suzuki, K., Sanchez, P.C., and Nakase, T. (2003) Caldisphaera lagunensis gen. nov., sp. nov., a novel thermoacidophilic crenarchaeote isolated from a hot spring at Mt Maquiling, Philippines. Int. J. Syst. Evol. Microbiol. 53, 1149-1154.
    • (2003) Int. J. Syst. Evol. Microbiol. , vol.53 , pp. 1149-1154
    • Itoh, T.1    Suzuki, K.2    Sanchez, P.C.3    Nakase, T.4
  • 27
    • 0000077259 scopus 로고    scopus 로고
    • Isotopic inferences on early ecosystems
    • edited by W.L. Manger and L.K. Meeks, The Palaeontological Society, Pittsburgh
    • Knoll, A.H. and Canfield, D.E. (1998) Isotopic inferences on early ecosystems. In Isotope Paleobiology and Paleoecology, edited by W.L. Manger and L.K. Meeks, The Palaeontological Society, Pittsburgh, pp. 212-243.
    • (1998) Isotope Paleobiology and Paleoecology , pp. 212-243
    • Knoll, A.H.1    Canfield, D.E.2
  • 28
    • 0002624786 scopus 로고    scopus 로고
    • Biosynthesis of cysteine
    • 2nd ed., edited by F.C. Neidhardt, R. Curtiss III, J.L. Ingrahm, E.C.C. Lin, K.B. Low, B. Magasanik, W.S. Reznikoff, M. Riley, M. Schaechter, and H.E. Umbarger, American Society for Microbiology, Washington, DC
    • Kredich, N. (1996) Biosynthesis of cysteine. In Escherichia coli and Salmonella: Cellular and Molecular Biology, Vol. 1, 2nd ed., edited by F.C. Neidhardt, R. Curtiss III, J.L. Ingrahm, E.C.C. Lin, K.B. Low, B. Magasanik, W.S. Reznikoff, M. Riley, M. Schaechter, and H.E. Umbarger, American Society for Microbiology, Washington, DC, pp. 514-527.
    • (1996) Escherichia Coli and Salmonella: Cellular and Molecular Biology , vol.1 , pp. 514-527
    • Kredich, N.1
  • 30
    • 0033021380 scopus 로고    scopus 로고
    • Dissimilatory sulfite reductases from Archaeoglobus profundus and Desulfotomaculum thermocisternum: Phylogenetic and structural implications from gene sequences
    • Larsen, O., Lien, T., and Birkeland, N.K. (1999) Dissimilatory sulfite reductases from Archaeoglobus profundus and Desulfotomaculum thermocisternum: Phylogenetic and structural implications from gene sequences. Extremophiles 3, 63-70.
    • (1999) Extremophiles , vol.3 , pp. 63-70
    • Larsen, O.1    Lien, T.2    Birkeland, N.K.3
  • 31
    • 0030980121 scopus 로고    scopus 로고
    • Taurine reaction in anaerobic respiration of Bilophila wadsworthia RZATAU
    • Laue, H., Degner, K., and Cook, A.M. (1997) Taurine reaction in anaerobic respiration of Bilophila wadsworthia RZATAU. Appl. Environ. Microbiol. 63, 2016-2021.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 2016-2021
    • Laue, H.1    Degner, K.2    Cook, A.M.3
  • 32
    • 0035110831 scopus 로고    scopus 로고
    • Dissimilatory sulfite reductase (desulfoviridin) of the taurine-degrading, non-sulfate-reducing bacterium Bilophila wadsworthia RZATAU contains a fused dsrB-dsriD subunit
    • Laue, H., Friedrich, M., Ruff, J., and Cook, A. (2001) Dissimilatory sulfite reductase (desulfoviridin) of the taurine-degrading, non-sulfate-reducing bacterium Bilophila wadsworthia RZATAU contains a fused dsrB-dsriD subunit. J. Bacteriol. 183, 1727-1733.
    • (2001) J. Bacteriol. , vol.183 , pp. 1727-1733
    • Laue, H.1    Friedrich, M.2    Ruff, J.3    Cook, A.4
  • 33
    • 0004294399 scopus 로고    scopus 로고
    • Biochemistry and energetics of sulfate reduction
    • Pearson Education, Inc., Upper Saddle River, NJ
    • Madigan, M., Martinko, J., and Parker, J. (2003) Biochemistry and energetics of sulfate reduction. In Brock Biology of Microorganisms Pearson Education, Inc., Upper Saddle River, NJ, p. 580.
    • (2003) Brock Biology of Microorganisms , pp. 580
    • Madigan, M.1    Martinko, J.2    Parker, J.3
  • 34
    • 0031913670 scopus 로고    scopus 로고
    • A dissimilatory sirohaem-sulfite reductase type protein from the hyperthermophilic archaeon Pyrobaculum islandicum
    • Molitor, M., Dahl, C., Molitor, I., Schäfer, U., Speich, N., Huber, R., Deutzmann, R., and Trüper, H.G. (1998) A dissimilatory sirohaem-sulfite reductase type protein from the hyperthermophilic archaeon Pyrobaculum islandicum. Microbiology 144, 529-541.
    • (1998) Microbiology , vol.144 , pp. 529-541
    • Molitor, M.1    Dahl, C.2    Molitor, I.3    Schäfer, U.4    Speich, N.5    Huber, R.6    Deutzmann, R.7    Trüper, H.G.8
  • 35
    • 0842291638 scopus 로고    scopus 로고
    • A novel lineage of sulfate-reducing microorganisms: Thermodesulfobiaceae fam. nov., Thermodesulfobium narugense, gen. nov., sp. nov., a new thermophilic isolate from a hot spring
    • Mori, K., Kim, H., Kakegawa, T., and Hanada, S. (2003) A novel lineage of sulfate-reducing microorganisms: Thermodesulfobiaceae fam. nov., Thermodesulfobium narugense, gen. nov., sp. nov., a new thermophilic isolate from a hot spring. Extremophiles 7, 283-290.
    • (2003) Extremophiles , vol.7 , pp. 283-290
    • Mori, K.1    Kim, H.2    Kakegawa, T.3    Hanada, S.4
  • 36
  • 37
    • 0023870575 scopus 로고
    • Characterization of two dissimilatory sulfite reductases (desulforubidin and desulfoviridin) from sulfate-reducing bacteria. Mössbauer and EPR Studies
    • Moura, I., LeGall, J., Lino, A.R., Peck, H.D., Fauque, G., Xavier, A.V., DerVartanian, D.V., Moura, J.J.G., and Huynh, B.H. (1988) Characterization of two dissimilatory sulfite reductases (desulforubidin and desulfoviridin) from sulfate-reducing bacteria. Mössbauer and EPR Studies. J. Am. Chem. Soc. 110, 1075-1082.
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 1075-1082
    • Moura, I.1    LeGall, J.2    Lino, A.R.3    Peck, H.D.4    Fauque, G.5    Xavier, A.V.6    DerVartanian, D.V.7    Moura, J.J.G.8    Huynh, B.H.9
  • 38
    • 0015907498 scopus 로고
    • Siroheme and sirohydrochlorin. The basis for a new type of porphyrinrelated prosthetic group common to both assimilatory and dissimilatory sulfite reductases
    • Murphy, M.J. and Siegel, L.M. (1973) Siroheme and sirohydrochlorin. The basis for a new type of porphyrinrelated prosthetic group common to both assimilatory and dissimilatory sulfite reductases. J. Biol. Chem. 248, 6911-6919.
    • (1973) J. Biol. Chem. , vol.248 , pp. 6911-6919
    • Murphy, M.J.1    Siegel, L.M.2
  • 39
    • 0034156863 scopus 로고    scopus 로고
    • Characterization of the Cys gene locus from Allochromatium vinosum indicates an unusual sulfate assimilation pathway
    • Neumann, S., Wynen, A., Trüper, H.G., and Dahl, C. (2000) Characterization of the Cys gene locus from Allochromatium vinosum indicates an unusual sulfate assimilation pathway. Mol. Biol. Rep. 27, 27-33.
    • (2000) Mol. Biol. Rep. , vol.27 , pp. 27-33
    • Neumann, S.1    Wynen, A.2    Trüper, H.G.3    Dahl, C.4
  • 40
    • 0021197001 scopus 로고
    • Hydrogenase, electron-transfer proteins, and energy coupling in the sulfate reducing bacteria Desulfovibrio
    • Odom, J.M. and Peck, H.D. (1984) Hydrogenase, electron-transfer proteins, and energy coupling in the sulfate reducing bacteria Desulfovibrio. Annu. Rev. Microbiol. 38, 551-592.
    • (1984) Annu. Rev. Microbiol. , vol.38 , pp. 551-592
    • Odom, J.M.1    Peck, H.D.2
  • 41
    • 0024462430 scopus 로고
    • Characterization of the flavoprotein moieties of NADPH-sulfite reductase from Salmonella typhimurium and E. coli: Physiochemical and catalytic properties, amino acid sequences deduced from DNA sequence of cysJ and comparison with NADPH-cytochrome P-450 reductase
    • Ostrowski, J., Barber, M.J., Rueger, D.C., Miller, B.E., Siegel, L.M., and Kredich, N.M. (1989a) Characterization of the flavoprotein moieties of NADPH-sulfite reductase from Salmonella typhimurium and E. coli: Physiochemical and catalytic properties, amino acid sequences deduced from DNA sequence of cysJ and comparison with NADPH-cytochrome P-450 reductase. J. Biol. Chem. 264, 15796-15808.
    • (1989) J. Biol. Chem. , vol.264 , pp. 15796-15808
    • Ostrowski, J.1    Barber, M.J.2    Rueger, D.C.3    Miller, B.E.4    Siegel, L.M.5    Kredich, N.M.6
  • 43
    • 0031855745 scopus 로고    scopus 로고
    • Siroheme sulfite reductases and other proteins encoded by genes at dsr locus of Chromatium vinosum are involved in the oxidation of intracellular sulfur
    • Pott, A.S. and Dahl, C. (1998) Siroheme sulfite reductases and other proteins encoded by genes at dsr locus of Chromatium vinosum are involved in the oxidation of intracellular sulfur. Microbiology 144, 1881-1894.
    • (1998) Microbiology , vol.144 , pp. 1881-1894
    • Pott, A.S.1    Dahl, C.2
  • 44
    • 0018429082 scopus 로고
    • Purification of Thiobacillus denitrificans siroheme sulfite reductase and investigation of some molecular and catalytic properties
    • Schedel, M. and Trüper, H.G. (1979) Purification of Thiobacillus denitrificans siroheme sulfite reductase and investigation of some molecular and catalytic properties. Biochim. Biophys. Acta 568, 454-467.
    • (1979) Biochim. Biophys. Acta , vol.568 , pp. 454-467
    • Schedel, M.1    Trüper, H.G.2
  • 45
    • 0002308927 scopus 로고
    • Isotopic inferences of ancient biochemistries: Carbon, sulfur, hydrogen and nitrogen
    • edited by J.W. Schopf, Princeton University Press, Princeton, NJ
    • Schidlowski, M., Hayes, J.M., and Kaplan, I.R. (1983) Isotopic inferences of ancient biochemistries: Carbon, sulfur, hydrogen and nitrogen. In Earth's Earliest Biosphere, edited by J.W. Schopf, Princeton University Press, Princeton, NJ, pp. 149-186.
    • (1983) Earth's Earliest Biosphere , pp. 149-186
    • Schidlowski, M.1    Hayes, J.M.2    Kaplan, I.R.3
  • 47
    • 0035282466 scopus 로고    scopus 로고
    • Isotopic evidence for microbial sulphate reduction in the early Archaean era
    • Shen, Y., Buick, R., and Canfield, D.E. (2001) Isotopic evidence for microbial sulphate reduction in the early Archaean era. Nature 410, 77-81.
    • (2001) Nature , vol.410 , pp. 77-81
    • Shen, Y.1    Buick, R.2    Canfield, D.E.3
  • 48
    • 0034618559 scopus 로고    scopus 로고
    • Genome sequences of the endocellular bacterial symbiont of aphids Buchnera sp APS
    • Shigenobu, S., Watanabe, H., Hattori, M., Sakaki, Y. and Ishikawa, H. (2000) Genome sequences of the endocellular bacterial symbiont of aphids Buchnera sp APS. Nature 407, 81-86.
    • (2000) Nature , vol.407 , pp. 81-86
    • Shigenobu, S.1    Watanabe, H.2    Hattori, M.3    Sakaki, Y.4    Ishikawa, H.5
  • 51
    • 0025942475 scopus 로고
    • Primary structure of the assimilatory-type sulfite reductase Desulfovobrio vulgaris (Hildenborough): Cloning and nucleotide sequence of the reductase gene
    • Tan, J., Helms, L.R., Swenson, R.P., and Cowan, J.A. (1991) Primary structure of the assimilatory-type sulfite reductase Desulfovobrio vulgaris (Hildenborough): Cloning and nucleotide sequence of the reductase gene. Biochemistry 30, 9000-9007.
    • (1991) Biochemistry , vol.30 , pp. 9000-9007
    • Tan, J.1    Helms, L.R.2    Swenson, R.P.3    Cowan, J.A.4
  • 52
    • 0027968068 scopus 로고
    • Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position specific gap penalties and weight matrix choice
    • Thompson, J.D., Higgins, D.G., and Gibson, T.J. (1994) Clustal W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position specific gap penalties and weight matrix choice. Nucleic Acids Res. 22, 4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3    Clustal, W.4
  • 53
    • 0032463021 scopus 로고    scopus 로고
    • Phylogeny of dissimilatory sulfite reductases supports an early origin of sulfate respiration
    • Wagner, M., Roger, A.J., Flax, J.L., Brusseau, G.A., and Stahl, D.A. (1998) Phylogeny of dissimilatory sulfite reductases supports an early origin of sulfate respiration. J. Bacteriol. 180, 2975-2982.
    • (1998) J. Bacteriol. , vol.180 , pp. 2975-2982
    • Wagner, M.1    Roger, A.J.2    Flax, J.L.3    Brusseau, G.A.4    Stahl, D.A.5


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