메뉴 건너뛰기




Volumn 73, Issue 4, 2006, Pages 827-838

Orthric Rieske dioxygenases for degrading mixtures of 2,4-dinitrotoluene/ naphthalene and 2-amino-4,6-dinitrotoluene/4-amino-2,6-dinitrotoluene

Author keywords

Dinitrotoluene; Dioxygenases; Hybrid enzyme; Naphthalene

Indexed keywords

DINITROTOLUENE; DIOXYGENASES; HYBRID ENZYME;

EID: 33751512080     PISSN: 01757598     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00253-006-0538-8     Document Type: Article
Times cited : (21)

References (39)
  • 1
    • 33751544834 scopus 로고    scopus 로고
    • ATSDR. Hamilton County, Tennessee. Agency for Toxic Substances and Disease Registry, Atlanta, GA
    • ATSDR (2004) Public Health Assessment Volunteer Army Ammunition Plant Chattanooga, Hamilton County, Tennessee. Agency for Toxic Substances and Disease Registry, Atlanta, GA
    • (2004) Public Health Assessment Volunteer Army Ammunition Plant Chattanooga
  • 2
    • 0033024795 scopus 로고    scopus 로고
    • Functionality of biphenyl 2,3-dioxygenase components in naphthalene 1,2-dioxygenase
    • Barriault D, Sylvestre M (1999) Functionality of biphenyl 2,3-dioxygenase components in naphthalene 1,2-dioxygenase. Appl Microbiol Biotechnol 51:592-597
    • (1999) Appl Microbiol Biotechnol , vol.51 , pp. 592-597
    • Barriault, D.1    Sylvestre, M.2
  • 3
    • 0036136382 scopus 로고    scopus 로고
    • Directed evolution of toluene ortho-monooxygenase for enhanced 1-naphthol synthesis and chlorinated ethene degradation
    • Canada KA, Iwashita S, Shim H, Wood TK (2002) Directed evolution of toluene ortho-monooxygenase for enhanced 1-naphthol synthesis and chlorinated ethene degradation. J Bacteriol 184:344-349
    • (2002) J Bacteriol , vol.184 , pp. 344-349
    • Canada, K.A.1    Iwashita, S.2    Shim, H.3    Wood, T.K.4
  • 4
    • 0034480510 scopus 로고    scopus 로고
    • A cluster exposed: Structure of the Rieske ferredoxin from biphenyl dioxygenase and the redox properties of Rieske Fe-S proteins
    • Colbert CL, Couture MM-J, Eltis LD, Bolin JT (2000) A cluster exposed: structure of the Rieske ferredoxin from biphenyl dioxygenase and the redox properties of Rieske Fe-S proteins. Structure 8:1267-1278
    • (2000) Structure , vol.8 , pp. 1267-1278
    • Colbert, C.L.1    Couture, M.M.-J.2    Eltis, L.D.3    Bolin, J.T.4
  • 5
    • 0027368828 scopus 로고
    • Enhanced biodegradation of polychlorinated biphenyls after site-directed mutagenesis of a biphenyl dioxygenase gene
    • Erickson BD, Mondello FJ (1993) Enhanced biodegradation of polychlorinated biphenyls after site-directed mutagenesis of a biphenyl dioxygenase gene. Appl Environ Microbiol 59:3858-3862
    • (1993) Appl Environ Microbiol , vol.59 , pp. 3858-3862
    • Erickson, B.D.1    Mondello, F.J.2
  • 6
    • 0026956872 scopus 로고
    • Characterization of polycyclic aromatic hydrocarbons degradative soil Pseudomonas
    • Fuenmayor SL, Lemoine VR (1992) Characterization of polycyclic aromatic hydrocarbons degradative soil Pseudomonas. Acta Cient Venez 43:349-354
    • (1992) Acta Cient Venez , vol.43 , pp. 349-354
    • Fuenmayor, S.L.1    Lemoine, V.R.2
  • 7
    • 0031967070 scopus 로고    scopus 로고
    • A gene cluster encoding steps in conversion of naphthalene to gentisate in Pseudomonas sp. strain U2
    • Fuenmayor SL, Wild M, Boyes AL, Williams PA (1998) A gene cluster encoding steps in conversion of naphthalene to gentisate in Pseudomonas sp. strain U2. J Bacteriol 180:2522-2530
    • (1998) J Bacteriol , vol.180 , pp. 2522-2530
    • Fuenmayor, S.L.1    Wild, M.2    Boyes, A.L.3    Williams, P.A.4
  • 11
    • 0035656170 scopus 로고    scopus 로고
    • Oxidative transformation of aminodinitrotoluene isomers by multicomponent dioxygenases
    • Johnson GR, Smets BF, Spain JC (2001) Oxidative transformation of aminodinitrotoluene isomers by multicomponent dioxygenases. Appl Environ Microbiol 67:5460-5466
    • (2001) Appl Environ Microbiol , vol.67 , pp. 5460-5466
    • Johnson, G.R.1    Smets, B.F.2    Spain, J.C.3
  • 12
    • 0036064709 scopus 로고    scopus 로고
    • Origins of the 2,4-dinitrotoluene pathway
    • Johnson GR, Jain RK, Spain JC (2002) Origins of the 2,4-dinitrotoluene pathway. J Bacteriol 184:4219-4232
    • (2002) J Bacteriol , vol.184 , pp. 4219-4232
    • Johnson, G.R.1    Jain, R.K.2    Spain, J.C.3
  • 13
    • 0028331811 scopus 로고
    • Phototoxicity 3. Comparative toxicity of trinitrotoluene and aminodinitrotoluenes to Daphnia magna, Dugesia dorotocephala, and sheep erythrocytes
    • Johnson LR, Davenport R, Balbach H, Schaeffer DJ (1994) Phototoxicity 3. Comparative toxicity of trinitrotoluene and aminodinitrotoluenes to Daphnia magna, Dugesia dorotocephala, and sheep erythrocytes. Ecotoxicol Environ Saf 27:34-49
    • (1994) Ecotoxicol Environ Saf , vol.27 , pp. 34-49
    • Johnson, L.R.1    Davenport, R.2    Balbach, H.3    Schaeffer, D.J.4
  • 14
    • 2942530416 scopus 로고    scopus 로고
    • Saturation mutagenesis of Burkholderia cepacia R34 2,4-dinitrotoluene dioxygenase at DntAc valine 350 for synthesizing nitrohydroquinone, methylhydroquinone, and methoxyhydroquinone
    • Keenan BG, Leungsakul T, Smets BF, Wood TK (2004) Saturation mutagenesis of Burkholderia cepacia R34 2,4-dinitrotoluene dioxygenase at DntAc valine 350 for synthesizing nitrohydroquinone, methylhydroquinone, and methoxyhydroquinone. Appl Environ Microbiol 70:3221-3222
    • (2004) Appl Environ Microbiol , vol.70 , pp. 3221-3222
    • Keenan, B.G.1    Leungsakul, T.2    Smets, B.F.3    Wood, T.K.4
  • 15
    • 18244374438 scopus 로고    scopus 로고
    • Protein engineering of the archetypal nitroarene dioxygenase of Ralstonia sp. strain U2 for activity on aminonitrotoluenes and dinitrotoluenes through alpha-subunit residues leucine 225, phenylalanine 350, and glycine 407
    • Keenan BG, Leungsakul T, Smets BF, Mori M, Henderson DE, Wood TK (2005) Protein engineering of the archetypal nitroarene dioxygenase of Ralstonia sp. strain U2 for activity on aminonitrotoluenes and dinitrotoluenes through alpha-subunit residues leucine 225, phenylalanine 350, and glycine 407. J Bacteriol 187:3302-3310
    • (2005) J Bacteriol , vol.187 , pp. 3302-3310
    • Keenan, B.G.1    Leungsakul, T.2    Smets, B.F.3    Mori, M.4    Henderson, D.E.5    Wood, T.K.6
  • 17
    • 0031874757 scopus 로고    scopus 로고
    • Enhanced degradation of polychlorinated biphenyls by directed evolution of biphenyl dioxygenase
    • Kumamaru T, Suenaga H, Mitsuoka M, Watanabe T, Furukawa K (1998) Enhanced degradation of polychlorinated biphenyls by directed evolution of biphenyl dioxygenase. Nat Biotechnol 16:663-666
    • (1998) Nat Biotechnol , vol.16 , pp. 663-666
    • Kumamaru, T.1    Suenaga, H.2    Mitsuoka, M.3    Watanabe, T.4    Furukawa, K.5
  • 18
    • 0031688853 scopus 로고    scopus 로고
    • Involvement of electrostatic interactions between the components of toluene dioxygenase from Pseudomonas putida F1
    • Lee K (1998) Involvement of electrostatic interactions between the components of toluene dioxygenase from Pseudomonas putida F1. J Microbiol Biotechnol 8:416-421
    • (1998) J Microbiol Biotechnol , vol.8 , pp. 416-421
    • Lee, K.1
  • 19
    • 0036158077 scopus 로고    scopus 로고
    • Molecular characterization and substrate specificity of nitrobenzene dioxygenase from Comamonas sp. strain JS765
    • Lessner DJ, Johnson GR, Parales RE, Spain JC, Gibson DT (2002) Molecular characterization and substrate specificity of nitrobenzene dioxygenase from Comamonas sp. strain JS765. Appl Environ Microbiol 68:634-641
    • (2002) Appl Environ Microbiol , vol.68 , pp. 634-641
    • Lessner, D.J.1    Johnson, G.R.2    Parales, R.E.3    Spain, J.C.4    Gibson, D.T.5
  • 20
    • 28444458447 scopus 로고    scopus 로고
    • Saturation mutagenesis of 2,4-DNT dioxygenase of Burkholderia sp. strain DNT for enhanced dinitrotoluene degradation
    • Leungsakul T, Keenan BG, Yin H, Smets BF, Wood TK (2005) Saturation mutagenesis of 2,4-DNT dioxygenase of Burkholderia sp. strain DNT for enhanced dinitrotoluene degradation. Biotechnol Bioeng 92:510-517
    • (2005) Biotechnol Bioeng , vol.92 , pp. 510-517
    • Leungsakul, T.1    Keenan, B.G.2    Yin, H.3    Smets, B.F.4    Wood, T.K.5
  • 21
    • 0033778985 scopus 로고    scopus 로고
    • Secondary metabolism of dinitrobenzyl glucuronide related to production of genotoxic compounds of dinitrotoluene in male Wistar rat
    • Mori M, Shoji M, Sayama M, Kondo T, Inoue M, Kodaira K (2000) Secondary metabolism of dinitrobenzyl glucuronide related to production of genotoxic compounds of dinitrotoluene in male Wistar rat. J Health Sci 46:329-335
    • (2000) J Health Sci , vol.46 , pp. 329-335
    • Mori, M.1    Shoji, M.2    Sayama, M.3    Kondo, T.4    Inoue, M.5    Kodaira, K.6
  • 22
    • 13944256249 scopus 로고    scopus 로고
    • Crystal structure of the ferredoxin component of carbazole 1,9a-dioxygenase of Pseudomonas resinovorans strain CA10, a novel Rieske non-heme iron oxygenase system
    • Nam J-W, Noguchi H, Fujimoto Z, Mizuno H, Ashikawa Y, Abo M, Fushinobu S, Kobashi N, Wakagi T, Iwata K et al (2005) Crystal structure of the ferredoxin component of carbazole 1,9a-dioxygenase of Pseudomonas resinovorans strain CA10, a novel Rieske non-heme iron oxygenase system. Proteins 58:779-789
    • (2005) Proteins , vol.58 , pp. 779-789
    • Nam, J.-W.1    Noguchi, H.2    Fujimoto, Z.3    Mizuno, H.4    Ashikawa, Y.5    Abo, M.6    Fushinobu, S.7    Kobashi, N.8    Wakagi, T.9    Iwata, K.10
  • 23
    • 0029070669 scopus 로고
    • Oxidative pathway for the biodegradation of nitrobenzene by Comamonas sp. strain JS765
    • Nishino SF, Spain JC (1995) Oxidative pathway for the biodegradation of nitrobenzene by Comamonas sp. strain JS765. Appl Environ Microbiol 61:2308-2313
    • (1995) Appl Environ Microbiol , vol.61 , pp. 2308-2313
    • Nishino, S.F.1    Spain, J.C.2
  • 24
    • 0034061462 scopus 로고    scopus 로고
    • Aerobic degradation of dinitrotoluenes and pathway for bacterial degradation of 2,6-dinitrotoluene
    • Nishino SF, Paoli GC, Spain JC (2000) Aerobic degradation of dinitrotoluenes and pathway for bacterial degradation of 2,6-dinitrotoluene. Appl Environ Microbiol 66:2139-2147
    • (2000) Appl Environ Microbiol , vol.66 , pp. 2139-2147
    • Nishino, S.F.1    Paoli, G.C.2    Spain, J.C.3
  • 25
    • 0031932850 scopus 로고    scopus 로고
    • Enzyme specificity of 2-nitrotoluene 2,3-dioxygenase from Pseudomonas sp. strain JS42 is determined by the C-terminal region of the alpha-subunit of the oxygenase component
    • Parales JV, Parales RE, Resnick SM, Gibson DT (1998a) Enzyme specificity of 2-nitrotoluene 2,3-dioxygenase from Pseudomonas sp. strain JS42 is determined by the C-terminal region of the alpha-subunit of the oxygenase component. J Bacteriol 180:1194-1199
    • (1998) J Bacteriol , vol.180 , pp. 1194-1199
    • Parales, J.V.1    Parales, R.E.2    Resnick, S.M.3    Gibson, D.T.4
  • 26
    • 0031958521 scopus 로고    scopus 로고
    • Substrate specificities of hybrid naphthalene and 2,4-dinitrotoluene dioxygenase enzyme systems
    • Parales RE, Emig MD, Lynch NA, Gibson DT (1998b) Substrate specificities of hybrid naphthalene and 2,4-dinitrotoluene dioxygenase enzyme systems. J Bacteriol 180:2337-2344
    • (1998) J Bacteriol , vol.180 , pp. 2337-2344
    • Parales, R.E.1    Emig, M.D.2    Lynch, N.A.3    Gibson, D.T.4
  • 27
    • 0034051818 scopus 로고    scopus 로고
    • Substrate specificity of naphthalene dioxygenase: Effect of specific amino acids at the active site of the enzyme
    • Parales RE, Lee K, Resnick SM, Jiang H, Lessner DJ, Gibson DT (2000a) Substrate specificity of naphthalene dioxygenase: effect of specific amino acids at the active site of the enzyme. J Bacteriol 182:1641-1649
    • (2000) J Bacteriol , vol.182 , pp. 1641-1649
    • Parales, R.E.1    Lee, K.2    Resnick, S.M.3    Jiang, H.4    Lessner, D.J.5    Gibson, D.T.6
  • 28
    • 0033797753 scopus 로고    scopus 로고
    • Regioselectivity and enantioselectivity of naphthalene dioxygenase during arene cis-dihydroxylation: Control by phenylalanine 352 in the alpha-subunit
    • Parales RE, Resnick SM, Yu C-L, Boyd DR, Sharma ND, Gibson DT (2000b) Regioselectivity and enantioselectivity of naphthalene dioxygenase during arene cis-dihydroxylation: control by phenylalanine 352 in the alpha-subunit. J Bacteriol 182:5495-5504
    • (2000) J Bacteriol , vol.182 , pp. 5495-5504
    • Parales, R.E.1    Resnick, S.M.2    Yu, C.-L.3    Boyd, D.R.4    Sharma, N.D.5    Gibson, D.T.6
  • 30
    • 12144272238 scopus 로고    scopus 로고
    • Protein engineering of toluene ortho-monooxygenase of Burkholderia cepacia G4 for regiospecific hydroxylation of indole to form various indigoid compounds
    • Rui L, Reardon K, Wood TK (2005) Protein engineering of toluene ortho-monooxygenase of Burkholderia cepacia G4 for regiospecific hydroxylation of indole to form various indigoid compounds. Appl Microbiol Biotechnol 66:422-429
    • (2005) Appl Microbiol Biotechnol , vol.66 , pp. 422-429
    • Rui, L.1    Reardon, K.2    Wood, T.K.3
  • 33
    • 0037201961 scopus 로고    scopus 로고
    • Naphthalene toxicity and antioxidant nutrients
    • Stohs SJ, Ohia S, Bagchi D (2002) Naphthalene toxicity and antioxidant nutrients. Toxicology 180:97-105
    • (2002) Toxicology , vol.180 , pp. 97-105
    • Stohs, S.J.1    Ohia, S.2    Bagchi, D.3
  • 34
    • 0029779548 scopus 로고    scopus 로고
    • 2,4-Dinitrotoluene dioxygenase from Burkholderia sp. strain DNT: Similarity to naphthalene dioxygenase
    • Suen WC, Haigler BE, Spain JC (1996) 2,4-Dinitrotoluene dioxygenase from Burkholderia sp. strain DNT: similarity to naphthalene dioxygenase. J Bacteriol 178:4926-4934
    • (1996) J Bacteriol , vol.178 , pp. 4926-4934
    • Suen, W.C.1    Haigler, B.E.2    Spain, J.C.3
  • 35
    • 0029845403 scopus 로고    scopus 로고
    • Sequencing of Comamonas testosteroni strain B-356-biphenyl/chlorobiphenyl dioxygenase genes: Evolutionary relationships among gram-negative bacterial biphenyl dioxygenases
    • Sylvestre M, Sirois M, Hurtubise Y, Bergeron J, Ahmad D, Shareck F, Barriault D, Guillemette I, Juteau JM (1996) Sequencing of Comamonas testosteroni strain B-356-biphenyl/chlorobiphenyl dioxygenase genes: evolutionary relationships among gram-negative bacterial biphenyl dioxygenases. Gene 174:195-202
    • (1996) Gene , vol.174 , pp. 195-202
    • Sylvestre, M.1    Sirois, M.2    Hurtubise, Y.3    Bergeron, J.4    Ahmad, D.5    Shareck, F.6    Barriault, D.7    Guillemette, I.8    Juteau, J.M.9
  • 36
    • 0026640186 scopus 로고
    • Analysis of bph operon from the polychlorinated biphenyl-degrading strain of KF707
    • Taira K, Hirose J, Hayashida S, Furukawa K (1992) Analysis of bph operon from the polychlorinated biphenyl-degrading strain of KF707. J Biol Chem 267:4844-4853
    • (1992) J Biol Chem , vol.267 , pp. 4844-4853
    • Taira, K.1    Hirose, J.2    Hayashida, S.3    Furukawa, K.4
  • 37
    • 0031771290 scopus 로고    scopus 로고
    • Oxygen-insensitive nitroreductases: Analysis of the roles of nfsA and nfsB in development of resistance to 5-nitrofuran derivatives in Escherichia coli
    • Whiteway J, Koziarz P, Veall J, Sandhu N, Kumar P, Hoecher B, Lambert IB (1998) Oxygen-insensitive nitroreductases: analysis of the roles of nfsA and nfsB in development of resistance to 5-nitrofuran derivatives in Escherichia coli. J Bacteriol 180:5529-5539
    • (1998) J Bacteriol , vol.180 , pp. 5529-5539
    • Whiteway, J.1    Koziarz, P.2    Veall, J.3    Sandhu, N.4    Kumar, P.5    Hoecher, B.6    Lambert, I.B.7
  • 38
    • 18244376061 scopus 로고    scopus 로고
    • Reductive transformation of TNT by Escherichia coli: Pathway description
    • Yin H, Wood TK, Smets BF (2005) Reductive transformation of TNT by Escherichia coli: pathway description. Appl Microbiol Biotechnol 67:397-404
    • (2005) Appl Microbiol Biotechnol , vol.67 , pp. 397-404
    • Yin, H.1    Wood, T.K.2    Smets, B.F.3
  • 39
    • 0024427069 scopus 로고
    • Toluene degradation by Pseudomonas putida F1
    • Zylstra GJ, Gibson DT (1989) Toluene degradation by Pseudomonas putida F1. J Biol Chem 264:14940-14946
    • (1989) J Biol Chem , vol.264 , pp. 14940-14946
    • Zylstra, G.J.1    Gibson, D.T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.