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Volumn 73, Issue 1, 2007, Pages 64-72

Respiration and growth of Shewanella decolorationis S12 with an azo compound as the sole electron acceptor

Author keywords

[No Author keywords available]

Indexed keywords

CELL MEMBRANES; ELECTRONS; ENZYMES; GROWTH KINETICS; MOLECULAR BIOLOGY; STOICHIOMETRY;

EID: 33846139642     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.01415-06     Document Type: Article
Times cited : (114)

References (45)
  • 1
    • 0022518468 scopus 로고
    • Inhibitor studies of dissimilative Fe(III) reduction by Pseudomonas sp. strain 200 ("Pseudomonas ferrireductans")
    • Arnold, R. G., T. J. Dichristing, and M. R. Hoffmann. 1986. Inhibitor studies of dissimilative Fe(III) reduction by Pseudomonas sp. strain 200 ("Pseudomonas ferrireductans"). Appl. Environ. Microbiol. 52:281-289.
    • (1986) Appl. Environ. Microbiol , vol.52 , pp. 281-289
    • Arnold, R.G.1    Dichristing, T.J.2    Hoffmann, M.R.3
  • 2
    • 3042578045 scopus 로고    scopus 로고
    • Expression and characteristics of the gene encoding azoreductase from Rhodobacter sphaeroides AS1.1737
    • Bin, Y., Z. Jiti, W. Jing, D. Cuihong, H. Hongman, S. Zhiyong, and B. Yongming. 2004. Expression and characteristics of the gene encoding azoreductase from Rhodobacter sphaeroides AS1.1737. FEMS Microbiol. Lett. 236:129-136.
    • (2004) FEMS Microbiol. Lett , vol.236 , pp. 129-136
    • Bin, Y.1    Jiti, Z.2    Jing, W.3    Cuihong, D.4    Hongman, H.5    Zhiyong, S.6    Yongming, B.7
  • 3
    • 0043164772 scopus 로고    scopus 로고
    • Cloning and characterization of the gene coding for the aerobic azoreductase from Pigmentiphaga kullae K24
    • Bhimel, S., and A. Stolz. 2003. Cloning and characterization of the gene coding for the aerobic azoreductase from Pigmentiphaga kullae K24. Appl. Microbiol. Biotechnol. 62:186-190.
    • (2003) Appl. Microbiol. Biotechnol , vol.62 , pp. 186-190
    • Bhimel, S.1    Stolz, A.2
  • 4
    • 0036324837 scopus 로고    scopus 로고
    • Molecular cloning and characterization of the gene coding for the aerobic azoreductase from Xenophilus azovorans KF46F
    • Blumel, S., H. J. Knackmuss, and A. Stolz. 2002. Molecular cloning and characterization of the gene coding for the aerobic azoreductase from Xenophilus azovorans KF46F. Appl. Environ. Microbiol. 68:3948-3955.
    • (2002) Appl. Environ. Microbiol , vol.68 , pp. 3948-3955
    • Blumel, S.1    Knackmuss, H.J.2    Stolz, A.3
  • 5
    • 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
  • 7
    • 0019813419 scopus 로고
    • Reduction of polymeric azo and nitro dyes by intestinal bacteria
    • Brown, J. P. 1981. Reduction of polymeric azo and nitro dyes by intestinal bacteria. Appl. Environ. Microbiol. 41:1283-1286.
    • (1981) Appl. Environ. Microbiol , vol.41 , pp. 1283-1286
    • Brown, J.P.1
  • 9
    • 18244388960 scopus 로고    scopus 로고
    • Respiration and growth of Shewanella oneidensis MR-1 using vanadate as the sole electron acceptor
    • Carpentier, W., L. De Smet, J. Van Beeumen, and A. Brigé. 2005. Respiration and growth of Shewanella oneidensis MR-1 using vanadate as the sole electron acceptor. J. Bacteriol. 187:3293-3301.
    • (2005) J. Bacteriol , vol.187 , pp. 3293-3301
    • Carpentier, W.1    De Smet, L.2    Van Beeumen, J.3    Brigé, A.4
  • 10
    • 1642354143 scopus 로고    scopus 로고
    • Molecular cloning, over expression, purification, and characterization of an aerobic FMN-dependent azoreductase from Enterococcus faecalis
    • Chen, H., R. F. Wang, and C. E. Cerniglia. 2004. Molecular cloning, over expression, purification, and characterization of an aerobic FMN-dependent azoreductase from Enterococcus faecalis. Protein Expr. Purif. 34:302-310.
    • (2004) Protein Expr. Purif , vol.34 , pp. 302-310
    • Chen, H.1    Wang, R.F.2    Cerniglia, C.E.3
  • 11
    • 13844321063 scopus 로고
    • Mutagenicity of azo dyes: Structure-activity relationships
    • Chung, K. T., and C. E. Cerniglia. 1992. Mutagenicity of azo dyes: structure-activity relationships. Mutat. Res. 77:201-220.
    • (1992) Mutat. Res , vol.77 , pp. 201-220
    • Chung, K.T.1    Cerniglia, C.E.2
  • 12
    • 0017947910 scopus 로고
    • Reduction of azo dyes by intestinal anaerobes
    • Chung, K. T., G. E. Fulk, and M. Egan. 1978. Reduction of azo dyes by intestinal anaerobes. Appl. Environ. Microbiol. 35:558-562.
    • (1978) Appl. Environ. Microbiol , vol.35 , pp. 558-562
    • Chung, K.T.1    Fulk, G.E.2    Egan, M.3
  • 13
    • 0016839221 scopus 로고
    • Reduction of azo food dyes in cultures of Proteus vulgaris
    • Dubin, P., and K. L. Wright. 1975. Reduction of azo food dyes in cultures of Proteus vulgaris. Xenobiotica 5:563-571.
    • (1975) Xenobiotica , vol.5 , pp. 563-571
    • Dubin, P.1    Wright, K.L.2
  • 14
    • 0024963305 scopus 로고
    • Inhibition of Desulfovibrio gigas hydrogenase with copper salts and other metal ions
    • Fernandez, V. M., M. L. Rua, P. Reyes, R. Cammack, and E. C. Hatchikian. 1989. Inhibition of Desulfovibrio gigas hydrogenase with copper salts and other metal ions. Eur. J. Biochem. 185:449-454.
    • (1989) Eur. J. Biochem , vol.185 , pp. 449-454
    • Fernandez, V.M.1    Rua, M.L.2    Reyes, P.3    Cammack, R.4    Hatchikian, E.C.5
  • 15
    • 17144362509 scopus 로고    scopus 로고
    • Competitive binding of quinone and antibiotic stigmatellin to reaction centers of photosynthetic bacteria
    • Gerencsér, L., L. Rinyu, L. Kámán, E. Takahashi, C. A. Wraight, and P. Maroti. 2004. Competitive binding of quinone and antibiotic stigmatellin to reaction centers of photosynthetic bacteria. Acta Biol. Szeged. 48:25-33.
    • (2004) Acta Biol. Szeged , vol.48 , pp. 25-33
    • Gerencsér, L.1    Rinyu, L.2    Kámán, L.3    Takahashi, E.4    Wraight, C.A.5    Maroti, P.6
  • 16
    • 0017123829 scopus 로고
    • Electron transport components of the MnO2 reductase system and the location of the terminal reductase in a marine Bacillus
    • Ghiorse, W. C., and H. L. Ehrlich. 1976. Electron transport components of the MnO2 reductase system and the location of the terminal reductase in a marine Bacillus. Appl. Environ. Microbiol. 31:977-985.
    • (1976) Appl. Environ. Microbiol , vol.31 , pp. 977-985
    • Ghiorse, W.C.1    Ehrlich, H.L.2
  • 17
    • 0036842611 scopus 로고    scopus 로고
    • Heidelberg, J. F., I. T. Paulsen, K. E. Nelson, E. J. Gaidos, W. C. Nelson, T. D. Read, J. A. Eisen, R. Seshadri, N. Ward, B. Methe, R. A. Clayton, T. Meyer, A. Tsapin, J. Scott, M. Beanan, L. Brinkac, S. Daugherty, R. T. DeBoy, R. J. Dodson, A. S. Durkin, D. H. Haft, J. F. Kolonay, R. Madupu, J. D. Peterson, L. A. Umayam, O. White, A. M. Wolf, J. Vamathevan, J. Weidman, M. Impraim, K. Lee, K. Berry, C. Lee, J. Mueller, H. Khouri, J. Gill, T. R. Utterback, L. A. McDonald, T. V. Feldblyum, H. O. Smith, J. C. Venter, K. H. Nealson, and C. M. Fraser. 2002. Genome sequence of the dissimilatory metal ion-reducing bacterium Shewanella oneidensis. Nat. Biotech. 20:1118-1123.
    • Heidelberg, J. F., I. T. Paulsen, K. E. Nelson, E. J. Gaidos, W. C. Nelson, T. D. Read, J. A. Eisen, R. Seshadri, N. Ward, B. Methe, R. A. Clayton, T. Meyer, A. Tsapin, J. Scott, M. Beanan, L. Brinkac, S. Daugherty, R. T. DeBoy, R. J. Dodson, A. S. Durkin, D. H. Haft, J. F. Kolonay, R. Madupu, J. D. Peterson, L. A. Umayam, O. White, A. M. Wolf, J. Vamathevan, J. Weidman, M. Impraim, K. Lee, K. Berry, C. Lee, J. Mueller, H. Khouri, J. Gill, T. R. Utterback, L. A. McDonald, T. V. Feldblyum, H. O. Smith, J. C. Venter, K. H. Nealson, and C. M. Fraser. 2002. Genome sequence of the dissimilatory metal ion-reducing bacterium Shewanella oneidensis. Nat. Biotech. 20:1118-1123.
  • 18
    • 0028168949 scopus 로고
    • Decolourization of reactive azo dyes by transformation with Pseudomonas luteola
    • Hu, T. L. 1994. Decolourization of reactive azo dyes by transformation with Pseudomonas luteola. Bioresour. Technol. 49:47-51.
    • (1994) Bioresour. Technol , vol.49 , pp. 47-51
    • Hu, T.L.1
  • 19
    • 0030822677 scopus 로고    scopus 로고
    • Localization of the enzyme system involved in anaerobic reduction of azo dyes by Sphingomonas sp. strain BN6 and effect of artificial redox mediators on the rate of azo dye reduction
    • Kudlich, M., A. Keck, J. Klein, and A. Stolz. 1997. Localization of the enzyme system involved in anaerobic reduction of azo dyes by Sphingomonas sp. strain BN6 and effect of artificial redox mediators on the rate of azo dye reduction. Appl. Environ. Microbiol. 63:3691-3694.
    • (1997) Appl. Environ. Microbiol , vol.63 , pp. 3691-3694
    • Kudlich, M.1    Keck, A.2    Klein, J.3    Stolz, A.4
  • 20
    • 0344573100 scopus 로고    scopus 로고
    • Evidence for a chemiosmotic model of dehalorespiration in Desulfomonile tiedjei DCB-1
    • Louie, T. M., and W. W. Mohn. 1999. Evidence for a chemiosmotic model of dehalorespiration in Desulfomonile tiedjei DCB-1. J. Bacteriol. 181:40-46.
    • (1999) J. Bacteriol , vol.181 , pp. 40-46
    • Louie, T.M.1    Mohn, W.W.2
  • 21
    • 2142763872 scopus 로고    scopus 로고
    • Cleaning up with genomics applying molecular biology to bioremediation
    • Lovley, D. R. 2003. Cleaning up with genomics applying molecular biology to bioremediation. Nat. Rev. Microbiol. 1:35-44.
    • (2003) Nat. Rev. Microbiol , vol.1 , pp. 35-44
    • Lovley, D.R.1
  • 22
    • 0035943380 scopus 로고    scopus 로고
    • Anaerobes to the rescue
    • Lovley, D. R. 2001. Anaerobes to the rescue. Science 24:1444-1445.
    • (2001) Science , vol.24 , pp. 1444-1445
    • Lovley, D.R.1
  • 23
    • 0034042695 scopus 로고    scopus 로고
    • Novel form of anaerobic respiration of environmental relevance
    • Lovley, D. R., and J. D. Coates. 2000. Novel form of anaerobic respiration of environmental relevance. Curr. Opin. Microbiol. 3:252-256.
    • (2000) Curr. Opin. Microbiol , vol.3 , pp. 252-256
    • Lovley, D.R.1    Coates, J.D.2
  • 26
    • 0028359079 scopus 로고
    • Ferric iron reduction-linked growth yields of Shewanella putrefaciens MR-1
    • Myers, C. R., and J. M. Myers. 1994. Ferric iron reduction-linked growth yields of Shewanella putrefaciens MR-1. J. Appl. Bacteriol. 76:253-258.
    • (1994) J. Appl. Bacteriol , vol.76 , pp. 253-258
    • Myers, C.R.1    Myers, J.M.2
  • 27
    • 0024219883 scopus 로고    scopus 로고
    • Bacterial manganese reduction and growth with manganese oxide as sole electron acceptor
    • Myers, C. R., and K. H. Nealson. 1998. Bacterial manganese reduction and growth with manganese oxide as sole electron acceptor. Science 240:1319-1321.
    • (1998) Science , vol.240 , pp. 1319-1321
    • Myers, C.R.1    Nealson, K.H.2
  • 28
    • 0025018122 scopus 로고
    • Respiration-linked proton translocation coupled to anaerobic reduction of manganese(IV) and iron(III) in Shewanella putrefaciens MR-1
    • Myers, C. R., and K. H. Nealson. 1990. Respiration-linked proton translocation coupled to anaerobic reduction of manganese(IV) and iron(III) in Shewanella putrefaciens MR-1. J. Bacteriol. 172:6232-6238.
    • (1990) J. Bacteriol , vol.172 , pp. 6232-6238
    • Myers, C.R.1    Nealson, K.H.2
  • 29
    • 0035824553 scopus 로고    scopus 로고
    • Putative ACP phosphodiesterase gene (acpD) encodes an azoreductase
    • Nakanishi, M., C. Yatome, N. Ishida, and Y. Kitade. 2001. Putative ACP phosphodiesterase gene (acpD) encodes an azoreductase. J. Biol. Chem. 276:46394-46399.
    • (2001) J. Biol. Chem , vol.276 , pp. 46394-46399
    • Nakanishi, M.1    Yatome, C.2    Ishida, N.3    Kitade, Y.4
  • 30
    • 0016339106 scopus 로고
    • Separation of the inner (cytoplasmic) and outer membranes of gram-negative bacteria
    • Osborn, M. J., and R. Munson. 1974. Separation of the inner (cytoplasmic) and outer membranes of gram-negative bacteria. Methods Enzymol. 31:642-653.
    • (1974) Methods Enzymol , vol.31 , pp. 642-653
    • Osborn, M.J.1    Munson, R.2
  • 32
    • 0025309508 scopus 로고
    • Azoreductase activity of anaerobic bacteria isolated from human intestinal microflora
    • Rafii, F., W. Franklin, and C. E. Cerniglia. 1990. Azoreductase activity of anaerobic bacteria isolated from human intestinal microflora. Appl. Environ. Microbiol. 56:2146-2151.
    • (1990) Appl. Environ. Microbiol , vol.56 , pp. 2146-2151
    • Rafii, F.1    Franklin, W.2    Cerniglia, C.E.3
  • 33
    • 0037641012 scopus 로고    scopus 로고
    • Oxygen-insensitive nitroreductases NfsA and NfsB of Escherichia coli function under anaerobic conditions as lawsone-dependent azo reductases
    • Rau, J., and A. Stolz. 2003. Oxygen-insensitive nitroreductases NfsA and NfsB of Escherichia coli function under anaerobic conditions as lawsone-dependent azo reductases. Appl. Environ. Microbiol. 69:3448-3455.
    • (2003) Appl. Environ. Microbiol , vol.69 , pp. 3448-3455
    • Rau, J.1    Stolz, A.2
  • 34
    • 0034015380 scopus 로고    scopus 로고
    • Bacterial respiration: A flexible process for a changing environment
    • Richardson, D. J. 2000. Bacterial respiration: a flexible process for a changing environment. Microbiology 146:551-571.
    • (2000) Microbiology , vol.146 , pp. 551-571
    • Richardson, D.J.1
  • 35
    • 0038220925 scopus 로고    scopus 로고
    • The ars detoxification system is advantageous but not required for As(V) respiration by the genetically tractable Shewanella species strain ANA-3
    • Saltikov, C. W., A. Cifuentes, K. Venkateswaran, and D. K. Newman. 2003. The ars detoxification system is advantageous but not required for As(V) respiration by the genetically tractable Shewanella species strain ANA-3. Appl. Environ. Microbiol. 69:2800-2809.
    • (2003) Appl. Environ. Microbiol , vol.69 , pp. 2800-2809
    • Saltikov, C.W.1    Cifuentes, A.2    Venkateswaran, K.3    Newman, D.K.4
  • 36
    • 0037934657 scopus 로고    scopus 로고
    • A simple energy-conserving system: Proton reduction coupled to proton translocation
    • Sapra, R., K. Bagramyan, and M. W. W. Adams. 2003. A simple energy-conserving system: proton reduction coupled to proton translocation. Proc. Natl. Acad. Sci. USA 100:7545-7550.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 7545-7550
    • Sapra, R.1    Bagramyan, K.2    Adams, M.W.W.3
  • 37
    • 0014739488 scopus 로고
    • Enzymatic reduction of the azo dye, acid yellow, by extracts of Streptococcus faecalis, isolated from rat intestine
    • Scheline, R. R., R. T. Nygaard, and B. Longberg. 1970. Enzymatic reduction of the azo dye, acid yellow, by extracts of Streptococcus faecalis, isolated from rat intestine. Food Cosmet. Toxicol. 8:55-58.
    • (1970) Food Cosmet. Toxicol , vol.8 , pp. 55-58
    • Scheline, R.R.1    Nygaard, R.T.2    Longberg, B.3
  • 38
    • 0034921274 scopus 로고    scopus 로고
    • Basic and applied aspects in the microbial degradation of azo dyes
    • Stolz, A. 2001. Basic and applied aspects in the microbial degradation of azo dyes. Appl. Microbiol. Biotechnol. 56:69-80.
    • (2001) Appl. Microbiol. Biotechnol , vol.56 , pp. 69-80
    • Stolz, A.1
  • 39
    • 0035937804 scopus 로고    scopus 로고
    • Molecular cloning and characterization of the gene coding for azoreductase from Bacillus sp. OY1-2 isolated from soil
    • Suzuki, Y., T. Yoda, A. Ruhul, and W. Sugiura. 2001. Molecular cloning and characterization of the gene coding for azoreductase from Bacillus sp. OY1-2 isolated from soil. J. Biol. Chem. 276:9059-9065.
    • (2001) J. Biol. Chem , vol.276 , pp. 9059-9065
    • Suzuki, Y.1    Yoda, T.2    Ruhul, A.3    Sugiura, W.4
  • 40
    • 33846145188 scopus 로고    scopus 로고
    • Shewanella-the environmentally versatile genomes
    • Tiejie, J. M. 2002. Shewanella-the environmentally versatile genomes. Nat. Biotechnol. 20:1903-1904.
    • (2002) Nat. Biotechnol , vol.20 , pp. 1903-1904
    • Tiejie, J.M.1
  • 41
    • 0032480241 scopus 로고    scopus 로고
    • Microbiological evidence for Fe(III) reduction on early Earth
    • Vargas, M., K. Kashefi, E. L. Blunt-Harris, and D. R. Lovely. 1998. Microbiological evidence for Fe(III) reduction on early Earth. Nature 395:65-67.
    • (1998) Nature , vol.395 , pp. 65-67
    • Vargas, M.1    Kashefi, K.2    Blunt-Harris, E.L.3    Lovely, D.R.4
  • 43
    • 10644224511 scopus 로고
    • Formation of methane by bacterial extracts
    • Wolin, E. A., M. J. Wolin, and R. S. Wolfe. 1963. Formation of methane by bacterial extracts. J. Biol. Chem. 238:2882-2886.
    • (1963) J. Biol. Chem , vol.238 , pp. 2882-2886
    • Wolin, E.A.1    Wolin, M.J.2    Wolfe, R.S.3
  • 44
    • 13244254009 scopus 로고    scopus 로고
    • Shewanella decolorationis sp. nov., a dye-decolorizing bacterium isolated from activated sludge of a waste-water treatment plant
    • Xu, M., J. Guo, Y. Cen, X. Zhong, W. Cao, and G. Sun. 2005. Shewanella decolorationis sp. nov., a dye-decolorizing bacterium isolated from activated sludge of a waste-water treatment plant. Int. J. Syst. Evol. Microbiol. 55: 363-368.
    • (2005) Int. J. Syst. Evol. Microbiol , vol.55 , pp. 363-368
    • Xu, M.1    Guo, J.2    Cen, Y.3    Zhong, X.4    Cao, W.5    Sun, G.6
  • 45
    • 0003914501 scopus 로고
    • 2nd ed. VCH Publishers, Inc, New York, NY
    • Zollinger, H. 1991. Color chemistry, 2nd ed. VCH Publishers, Inc., New York, NY.
    • (1991) Color chemistry
    • Zollinger, H.1


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