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Volumn 92, Issue 2, 2011, Pages 393-405

Molecular determinants of azo reduction activity in the strain Pseudomonas putida MET94

Author keywords

Azo dyes; Azoreductase; Decolourisation; Pseudomonas putida; Whole cell catalysis

Indexed keywords

ANAEROBIC CONDITIONS; AROMATIC AMINES; AZO DYE REDUCTION; AZO REDUCTIONS; AZOREDUCTASE; BACTERIAL STRAINS; CRUDE EXTRACT; DECOLOURISATION; DIOXYGENS; DYE WASTEWATERS; ENVIRONMENTAL POLLUTANTS; GROWING CONDITIONS; HOMODIMERS; KINETIC MECHANISM; MOLECULAR DETERMINANTS; OXIDOREDUCTASES; PSEUDOMONAS PUTIDA; REACTION SCHEMES; SUBSTRATE SPECIFICITY; WHOLE CELL;

EID: 82455167939     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-011-3366-4     Document Type: Article
Times cited : (38)

References (45)
  • 2
    • 3042578045 scopus 로고    scopus 로고
    • Expression and characteristics of the gene encoding azoreductase from Rhodobacter sphaeroides AS1.1737
    • DOI 10.1016/j.femsle.2004.05.034, PII S0378109704003726
    • Bin Y, Jiti Z, Jing W, Cuihong D, Hongman H, Zhiyong S, Yongming B (2004) Expression and characteristics of the gene encoding azoreductase from Rhodobacter sphaeroides AS1.1737. FEMS Microbiol Lett 236:129-136 (Pubitemid 38801505)
    • (2004) FEMS Microbiology Letters , vol.236 , Issue.1 , 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
    • DOI 10.1007/s00253-003-1316-5
    • Blumel S, Stolz A (2003) Cloning and characterization of the gene coding for the aerobic azoreductase from Pigmentiphaga kullae K24. Appl Microbiol Biotechnol 62:186-190 (Pubitemid 36995171)
    • (2003) Applied Microbiology and Biotechnology , vol.62 , Issue.2-3 , pp. 186-190
    • Blumel, 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
    • DOI 10.1128/AEM.68.8.3948-3955.2002
    • Blumel S, Knackmuss HJ, Stolz A (2002) Molecular cloning and characterization of the gene coding for the aerobic azoreductase from Xenophilus azovorans KF46F. Appl Environ Microbiol 68:3948-3955 (Pubitemid 34836708)
    • (2002) Applied and Environmental Microbiology , vol.68 , Issue.8 , pp. 3948-3955
    • Blumel, S.1    Knackmuss, H.-J.2    Stolz, A.3
  • 5
    • 33646181980 scopus 로고    scopus 로고
    • Recent advances in azo dye degrading enzyme research
    • Chen H (2006) Recent advances in azo dye degrading enzyme research. Curr Protein Pept Sci 7:101-111
    • (2006) Curr Protein Pept Sci , vol.7 , pp. 101-111
    • Chen, H.1
  • 6
    • 1642354143 scopus 로고    scopus 로고
    • Molecular cloning, overexpression, purification, and characterization of an aerobic FMN-dependent azoreductase from Enterococcus faecalis
    • DOI 10.1016/j.pep.2003.12.016
    • Chen H, Wang RF, Cerniglia CE (2004) Molecular cloning, overexpression, purification, and characterization of an aerobic FMNdependent azoreductase from Enterococcus faecalis. Protein Expr Purif 34:302-310 (Pubitemid 38390580)
    • (2004) Protein Expression and Purification , vol.34 , Issue.2 , pp. 302-310
    • Chen, H.1    Wang, R.-F.2    Cerniglia, C.E.3
  • 7
    • 19044389145 scopus 로고    scopus 로고
    • Biochemical and molecular characterization of an azoreductase from Staphylococcus aureus, a tetrameric NADPH-dependent flavoprotein
    • DOI 10.1099/mic.0.27805-0
    • Chen H, Hopper SL, Cerniglia CE (2005) Biochemical and molecular characterization of an azoreductase from Staphylococcus aureus, a tetrameric NADPH-dependent flavoprotein. Microbiology 151:1433-1441 (Pubitemid 40711790)
    • (2005) Microbiology , vol.151 , Issue.5 , pp. 1433-1441
    • Chen, H.1    Hopper, S.L.2    Cerniglia, C.E.3
  • 8
    • 53449100677 scopus 로고    scopus 로고
    • Functional role of Trp-105 of Enterococcus faecalis azoreductase (AzoA) as resolved by structural and mutational analysis
    • Chen H, Xu H, Kweon O, Chen S, Cerniglia CE (2008) Functional role of Trp-105 of Enterococcus faecalis azoreductase (AzoA) as resolved by structural and mutational analysis. Microbiology 154:2659-2667
    • (2008) Microbiology , vol.154 , pp. 2659-2667
    • Chen, H.1    Xu, H.2    Kweon, O.3    Chen, S.4    Cerniglia, C.E.5
  • 9
    • 77951566064 scopus 로고    scopus 로고
    • Identification and molecular characterization of a novel flavin-free NADPH preferred azoreductase encoded by azoB in Pigmentiphaga kullae K24
    • Chen H, Feng J, Kweon O, Xu H, Cerniglia CE (2010) Identification and molecular characterization of a novel flavin-free NADPH preferred azoreductase encoded by azoB in Pigmentiphaga kullae K24. BMC Biochem 11:13
    • (2010) BMC Biochem , vol.11 , pp. 13
    • Chen, H.1    Feng, J.2    Kweon, O.3    Xu, H.4    Cerniglia, C.E.5
  • 12
    • 33847351352 scopus 로고    scopus 로고
    • Comparative study on reaction selectivity of azo dye decolorization by Pseudomonas luteola
    • Hsueh CC, Chen BY (2007) Comparative study on reaction selectivity of azo dye decolorization by Pseudomonas luteola. J Hazard Mater 141:842-849
    • (2007) J Hazard Mater , vol.141 , pp. 842-849
    • Hsueh, C.C.1    Chen, B.Y.2
  • 13
    • 33750919303 scopus 로고    scopus 로고
    • Potential applications of the oxidoreductive enzymes in the decolorization and detoxification of textile and other synthetic dyes from polluted water: A review
    • DOI 10.1080/07388550600969936, PII V4N572WQ760V9602
    • Husain Q (2006) Potential applications of the oxidoreductive enzymes in the decolorization and detoxification of textile and other synthetic dyes from polluted water: A review. Crit Rev Biotechnol 26:201-221 (Pubitemid 44729813)
    • (2006) Critical Reviews in Biotechnology , vol.26 , Issue.4 , pp. 201-221
    • Husain, Q.1
  • 15
    • 84892083722 scopus 로고    scopus 로고
    • Bioremediation for the decolorization of textile dyes-A review
    • Kandelbauer A, Guebitz GM (2005) Bioremediation for the decolorization of textile dyes-a review. Env Chem 269-288
    • (2005) Env Chem , pp. 269-288
    • Kandelbauer, A.1    Guebitz, G.M.2
  • 16
    • 77953623874 scopus 로고    scopus 로고
    • Enzyme promiscuity: A mechanistic and evolutionary perspective
    • Khersonsky O, Tawfik DS (2010) Enzyme promiscuity: A mechanistic and evolutionary perspective. Annu Rev Biochem 79:471-505
    • (2010) Annu Rev Biochem , vol.79 , pp. 471-505
    • Khersonsky, O.1    Tawfik, D.S.2
  • 17
    • 38849183395 scopus 로고    scopus 로고
    • Regulation of quinone detoxification by the thiol stress sensing DUF24/MarR-like repressor, YodB in Bacillus subtilis
    • DOI 10.1111/j.1365-2958.2008.06110.x
    • Leelakriangsak M, Huyen NT, Towe S, van Duy N, Becher D, Hecker M, Antelmann H, Zuber P (2008) Regulation of quinone detoxification by the thiol stress sensing DUF24/MarR-like repressor, YodB in Bacillus subtilis. Mol Microbiol 67:1108-1124 (Pubitemid 351207337)
    • (2008) Molecular Microbiology , vol.67 , Issue.5 , pp. 1108-1124
    • Leelakriangsak, M.1    Huyen, N.T.T.2    Towe, S.3    Van Duy, N.4    Becher, D.5    Hecker, M.6    Antelmann, H.7    Zuber, P.8
  • 18
    • 33746592530 scopus 로고    scopus 로고
    • The FAD-dependent tricarballylate dehydrogenase (TcuA) enzyme of Salmonella enterica converts tricarballylate into cis-aconitate
    • DOI 10.1128/JB.00514-06
    • Lewis JA, Escalante-Semerena JC (2006) The FAD-dependent tricarballylate dehydrogenase (TcuA) enzyme of Salmonella enterica converts tricarballylate into cis-aconitate. J Bacteriol 188:5479-5486 (Pubitemid 44157304)
    • (2006) Journal of Bacteriology , vol.188 , Issue.15 , pp. 5479-5486
    • Lewis, J.A.1    Escalante-Semerena, J.C.2
  • 19
    • 34648830900 scopus 로고    scopus 로고
    • Azoreductase from Rhodobacter sphaeroides AS1.1737 is a flavodoxin that also functions as nitroreductase and flavin mononucleotide reductase
    • DOI 10.1007/s00253-007-1087-5
    • Liu G, Zhou J, Lv H, Xiang X, Wang J, Zhou M, Qu Y (2007a) Azoreductase from Rhodobacter sphaeroides AS1.1737 is a flavodoxin that also functions as nitroreductase and flavin mononucleotide reductase. Appl Microbiol Biotechnol 76:1271-1279 (Pubitemid 47459768)
    • (2007) Applied Microbiology and Biotechnology , vol.76 , Issue.6 , pp. 1271-1279
    • Liu, G.1    Zhou, J.2    Lv, H.3    Xiang, X.4    Wang, J.5    Zhou, M.6    Qv, Y.7
  • 21
    • 41549168117 scopus 로고    scopus 로고
    • Site-directed mutagenesis of substrate binding sites of azoreductase from Rhodobacter sphaeroides
    • Liu G, Zhou J,Wang J, Yan B, Li J, Lu H, Qu Y, Jin R (2008) Site-directed mutagenesis of substrate binding sites of azoreductase from Rhodobacter sphaeroides. Biotechnol Lett 30:869-875
    • (2008) Biotechnol Lett , vol.30 , pp. 869-875
    • Liu, G.1    Zhou, J.2    Wang, J.3    Yan, B.4    Li, J.5    Lu, H.6    Qu, Y.7    Jin, R.8
  • 22
    • 70350436344 scopus 로고    scopus 로고
    • The Escherichia coli AzoR is involved in resistance to thiol-specific stress caused by electrophilic quinones
    • Liu G, Zhou J, Fu Q, Wang J (2009) The Escherichia coli AzoR is involved in resistance to thiol-specific stress caused by electrophilic quinones. J Bacteriol 191:6394-6400
    • (2009) J Bacteriol , vol.191 , pp. 6394-6400
    • Liu, G.1    Zhou, J.2    Fu, Q.3    Wang, J.4
  • 23
    • 43949102015 scopus 로고    scopus 로고
    • Paradigm in biodegradation using Pseudomonas putida-A review of proteomics studies
    • Loh KC, Cao B (2008) Paradigm in biodegradation using Pseudomonas putida-a review of proteomics studies. Enzym Microb Technol 42:1-12
    • (2008) Enzym Microb Technol , vol.42 , pp. 1-12
    • Loh, K.C.1    Cao, B.2
  • 25
    • 34547128364 scopus 로고    scopus 로고
    • Evaluation of genotoxicity and pro-oxidant effect of the azo dyes: Acids yellow 17, violet 7 and orange 52, and of their degradation products by Pseudomonas putida mt-2
    • DOI 10.1016/j.fct.2007.02.033, PII S0278691507000907
    • Mansour H, Corroler D, Barillier D, Ghedira K, Chekir L, Mosrati R (2007) Evaluation of genotoxicity and pro-oxidant effect of the azo dyes: Acids yellow 17, violet 7, and orange 52, and of their degradation products by Pseudomonas putida mt-2. Food Chem Toxicol 45:1670-1677 (Pubitemid 47102504)
    • (2007) Food and Chemical Toxicology , vol.45 , Issue.9 , pp. 1670-1677
    • Ben Mansour, H.1    Corroler, D.2    Barillier, D.3    Ghedira, K.4    Chekir, L.5    Mosrati, R.6
  • 26
    • 59649110563 scopus 로고    scopus 로고
    • In vitro mutagenicity of Acid Violet 7 and its degradation products by Pseudomonas putida mt-2: Correlation with chemical structures
    • Mansour H, Mosrati R, Corroler D, Ghedira K, Barillier D, Chekir L (2009) In vitro mutagenicity of Acid Violet 7 and its degradation products by Pseudomonas putida mt-2: Correlation with chemical structures. Environ Toxicol Pharmacol 27:231-236
    • (2009) Environ Toxicol Pharmacol , vol.27 , pp. 231-236
    • Mansour, H.1    Mosrati, R.2    Corroler, D.3    Ghedira, K.4    Barillier, D.5    Chekir, L.6
  • 27
    • 77952887285 scopus 로고    scopus 로고
    • Characterization of thermostable FMN-dependent NADH azoreductase from the moderate thermophile Geobacillus stearothermophilus
    • Matsumoto K, Mukai Y, Ogata D, Shozui F, Nduko J, Taguchi S, Ooi T (2010) Characterization of thermostable FMN-dependent NADH azoreductase from the moderate thermophile Geobacillus stearothermophilus. Appl Microbiol Biotechnol 86:1431-1438
    • (2010) Appl Microbiol Biotechnol , vol.86 , pp. 1431-1438
    • Matsumoto, K.1    Mukai, Y.2    Ogata, D.3    Shozui, F.4    Nduko, J.5    Taguchi, S.6    Ooi, T.7
  • 29
    • 13244259667 scopus 로고    scopus 로고
    • Purification and characterization of an oxygen insensitive azoreductase from Pseudomonas aeruginosa
    • Nachyar C, Rajakumar G (2005) Purification and characterization of an oxygen insensitive azoreductase from Pseudomonas aeruginosa. Enz Microb Tecnhol 36:505-509
    • (2005) Enz Microb Tecnhol , vol.36 , pp. 505-509
    • Nachyar, C.1    Rajakumar, G.2
  • 30
    • 0035824553 scopus 로고    scopus 로고
    • Putative ACP phosphodiesterase gene (acpD) encodes an azoreductase
    • Nakanishi M, Yatome C, Ishida N, Kitade Y (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
  • 34
    • 44749088936 scopus 로고    scopus 로고
    • Decolourisation and detoxification of textile effluents by fungal biosorption
    • Prigione V, Tigini V, Pezzella C, Anastasi A, Sannia G, Varese G (2008) Decolourisation and detoxification of textile effluents by fungal biosorption. Water Res 42:2911-2920
    • (2008) Water Res , vol.42 , pp. 2911-2920
    • Prigione, V.1    Tigini, V.2    Pezzella, C.3    Anastasi, A.4    Sannia, G.5    Varese, G.6
  • 35
    • 15444370108 scopus 로고    scopus 로고
    • Removal of dyes from the effluent of textile and dyestuff manufacturing industry: A review of emerging techniques with reference to biological treatment
    • DOI 10.1080/10643380590917932
    • Rai HS, Bhattacharyya MS, Singh J, Vats P, Banerjee UC (2005) Removal of dyes from the effluent of textile and dyestuff manufacturing industry: A review of emerging techniques withreference to biological treatment. Critical Rev Environ Sc Tech 35:219-238 (Pubitemid 40396857)
    • (2005) Critical Reviews in Environmental Science and Technology , vol.35 , Issue.3 , pp. 219-238
    • Rai, H.S.1    Bhattacharyya, M.S.2    Singh, J.3    Bansal, T.K.4    Vats, P.5    Banerjee, U.C.6
  • 36
    • 76749144100 scopus 로고    scopus 로고
    • Enzymatic biotransformation of synthetic dyes
    • Rodriguez-Couto S (2009) Enzymatic biotransformation of synthetic dyes. Curr Drug Metab 10:1048-1054
    • (2009) Curr Drug Metab , vol.10 , pp. 1048-1054
    • Rodriguez-Couto, S.1
  • 38
    • 33846970531 scopus 로고    scopus 로고
    • Lot6p from Saccharomyces cerevisiae is a FMN-dependent reductase with a potential role in quinone detoxification
    • Sollner S, Nebauer R, Ehammer H, Prem A, Deller S, Palfey BA, Daum G, Macheroux P (2007) Lot6p from Saccharomyces cerevisiae is a FMN-dependent reductase with a potential role in quinone detoxification. FEBS J 274:1328-1339
    • (2007) FEBS J , vol.274 , pp. 1328-1339
    • Sollner, S.1    Nebauer, R.2    Ehammer, H.3    Prem, A.4    Deller, S.5    Palfey, B.A.6    Daum, G.7    Macheroux, P.8
  • 39
    • 70149114201 scopus 로고    scopus 로고
    • Mechanism of flavin reduction and oxidation in the redox-sensing quinone reductase Lot6p from Saccharomyces cerevisiae
    • Sollner S, Deller S, Macheroux P, Palfey BA (2009) Mechanism of flavin reduction and oxidation in the redox-sensing quinone reductase Lot6p from Saccharomyces cerevisiae. Biochemistry 48:8636-8643
    • (2009) Biochemistry , vol.48 , pp. 8636-8643
    • Sollner, S.1    Deller, S.2    Macheroux, P.3    Palfey, B.A.4
  • 40
    • 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, Yoda T, Ruhul A, Sugiura W (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
  • 41
    • 0032795933 scopus 로고    scopus 로고
    • Bacteria designed for bioremediation
    • Timmis KN, Pieper DH (1999) Bacteria designed for bioremediation. Trends Biotechnol 17:200-204
    • (1999) Trends Biotechnol , vol.17 , pp. 200-204
    • Timmis, K.N.1    Pieper, D.H.2
  • 42
    • 34548677758 scopus 로고    scopus 로고
    • The MarR-type repressor MhqR (YkvE) regulates multiple dioxygenases/ glyoxalases and an azoreductase which confer resistance to 2-methylhydroquinone and catechol in Bacillus subtilis
    • DOI 10.1111/j.1365-2958.2007.05891.x
    • Towe S, Leelakriangsak M, Kobayashi K, Van Duy N, Hecker M, Zuber P, Antelmann H (2007) The MarR-type repressor MhqR (YkvE) regulates multiple dioxygenases/glyoxalases and an azoreductase which confer resistance to 2- methylhydroquinone and catechol in Bacillus subtilis. Mol Microbiol 66:40-54 (Pubitemid 47414789)
    • (2007) Molecular Microbiology , vol.66 , Issue.1 , pp. 40-54
    • Towe, S.1    Leelakriangsak, M.2    Kobayashi, K.3    Van Duy, N.4    Hecker, M.5    Zuber, P.6    Antelmann, H.7
  • 43
    • 18344394806 scopus 로고    scopus 로고
    • Combined anaerobic-aerobic treatment of azo dyes - A short review of bioreactor studies
    • DOI 10.1016/j.watres.2005.03.007, PII S0043135405000990
    • van der Zee FP, Villaverde S (2005) Combined anaerobic-aerobic treatment of azo dyes-a short review of bioreactor studies. Water Res 39:1425-1440 (Pubitemid 40637188)
    • (2005) Water Research , vol.39 , Issue.8 , pp. 1425-1440
    • Van Der Zee, F.P.1    Villaverde, S.2
  • 44
    • 35148864753 scopus 로고    scopus 로고
    • Molecular Cloning, Characterisation and Ligand-bound Structure of an Azoreductase from Pseudomonas aeruginosa
    • DOI 10.1016/j.jmb.2007.08.048, PII S0022283607011199
    • Wang CJ, Hagemeier C, Rahman N, Lowe E, NobleM, CoughtrieM, Sim E, Westwood I (2007) Molecular cloning, characterization and ligand-bound structure of an azoreductase from Pseudomonas aeruginosa. J Mol Biol 373:1213-1228 (Pubitemid 47539482)
    • (2007) Journal of Molecular Biology , vol.373 , Issue.5 , pp. 1213-1228
    • Wang, C.-J.1    Hagemeier, C.2    Rahman, N.3    Lowe, E.4    Noble, M.5    Coughtrie, M.6    Sim, E.7    Westwood, I.8
  • 45
    • 0020410057 scopus 로고
    • Properties of purified Orange II azoreductase, the enzyme initiating azo dye degradation by Pseudomonas KF46
    • DOI 10.1111/j.1432-1033.1982.tb07040.x
    • Zimmermann T, Kulla HG, Leisinger T (1982) Properties of purified Orange II azoreductase, the enzyme initiating azo dye degradation by Pseudomonas KF46. Eur J Biochem 129:197-203 (Pubitemid 13183778)
    • (1982) European Journal of Biochemistry , vol.129 , Issue.1 , pp. 197-203
    • Zimmermann, T.1    Kulla, H.G.2    Leisinger, T.3


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