메뉴 건너뛰기




Volumn 184, Issue 3, 2005, Pages 158-167

Biochemical characterization of trinitrotoluene transforming oxygen-insensitive nitroreductases from Clostridium acetobutylicum ATCC 824

Author keywords

Flavoprotein; Oxygen insensitive nitroreductase; Trinitrotoluene biotransformation

Indexed keywords

2,4 DINITROTOLUENE; BACTERIAL ENZYME; DICOUMAROL; FLAVOPROTEIN; GENE PRODUCT; HYDROXAMIC ACID DERIVATIVE; NITROFURAL; NITROFURANTOIN; NITROREDUCTASE; OXYGEN; PROTEIN NITA; PROTEIN NITB; QUERCETIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; TRINITROTOLUENE; UNCLASSIFIED DRUG;

EID: 27744503862     PISSN: 03028933     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00203-005-0036-x     Document Type: Article
Times cited : (42)

References (54)
  • 1
    • 0026745562 scopus 로고
    • The bioactivation of a 5-(aziridin-1-yl)-2,4-dinitrobenzamide (CB1954)-I. Purification and properties of a nitroreductase enzyme from Echerichia coli-a potential enzyme for antibody-directed enzyme prodrug therapy (ADEPT)
    • Anlezark GM, Melton RG, Sherwood RF, Coles B, Friedlos F, Knox RJ (1992) The bioactivation of a 5-(aziridin-1-yl)-2,4-dinitrobenzamide (CB1954)-I. Purification and properties of a nitroreductase enzyme from Echerichia coli-a potential enzyme for antibody-directed enzyme prodrug therapy (ADEPT). Biochem Pharmacol 44:2289-2295
    • (1992) Biochem Pharmacol , vol.44 , pp. 2289-2295
    • Anlezark, G.M.1    Melton, R.G.2    Sherwood, R.F.3    Coles, B.4    Friedlos, F.5    Knox, R.J.6
  • 2
    • 0020986323 scopus 로고
    • On nitroaryl reductase activities in several Clostridia
    • Angermaier L, Simon H (1983) On nitroaryl reductase activities in several Clostridia. Hoppe Seylers Z Physiol Chem 364:1653-1663
    • (1983) Hoppe Seylers Z Physiol Chem , vol.364 , pp. 1653-1663
    • Angermaier, L.1    Simon, H.2
  • 3
    • 0032416047 scopus 로고    scopus 로고
    • Degradation of nitrate ester and nitroaromatic explosives by Enterobacter cloacae PB2
    • Basran A, French CE, Williams RE, Nicklin S, Bruce NC (1998) Degradation of nitrate ester and nitroaromatic explosives by Enterobacter cloacae PB2. Biochem Soc Trans 26:680-685
    • (1998) Biochem Soc Trans , vol.26 , pp. 680-685
    • Basran, A.1    French, C.E.2    Williams, R.E.3    Nicklin, S.4    Bruce, N.C.5
  • 4
    • 0032738032 scopus 로고    scopus 로고
    • Cloning and sequence analysis of two Pseudomonas flavoprotein xenobiotic reductases
    • Blehert DS, Fox BG, Chambliss GH (1999) Cloning and sequence analysis of two Pseudomonas flavoprotein xenobiotic reductases. J Bacteriol 181:6254-6263
    • (1999) J Bacteriol , vol.181 , pp. 6254-6263
    • Blehert, D.S.1    Fox, B.G.2    Chambliss, G.H.3
  • 5
    • 0028101791 scopus 로고
    • Transformation of nitroaromatic compounds by a methanogenic bacterium, Methanococcus sp.(strain B)
    • Boopathy R (1994) Transformation of nitroaromatic compounds by a methanogenic bacterium, Methanococcus sp.(strain B) Arch Microbiol 162:167-172
    • (1994) Arch Microbiol , vol.162 , pp. 167-172
    • Boopathy, R.1
  • 6
    • 0028171154 scopus 로고
    • Metabolism of trinitrobenzene by a Pseudomonas consortium
    • Boopathy R, Manning J, Montemagno C (1994) Metabolism of trinitrobenzene by a Pseudomonas consortium. Can J Microbiol 40:787-790
    • (1994) Can J Microbiol , vol.40 , pp. 787-790
    • Boopathy, R.1    Manning, J.2    Montemagno, C.3
  • 7
    • 0027166967 scopus 로고
    • Metabolism of 2,4,6-trinitrotoluene (TNT) by Desulfovibrio sp. (B strain)
    • Boopathy R, Kulpa CF, Wilson M (1993) Metabolism of 2,4,6-trinitrotoluene (TNT) by Desulfovibrio sp. (B strain). Appl Microbiol Biotechnol 39:270-275
    • (1993) Appl Microbiol Biotechnol , vol.39 , pp. 270-275
    • Boopathy, R.1    Kulpa, C.F.2    Wilson, M.3
  • 8
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantitites of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantitites 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
  • 9
    • 0025892415 scopus 로고
    • Purification and characterization of an oxygen-insensitive NAD(P)H nitroreductase from Enterobacter cloacae
    • Bryant C, DeLuca M (1991) Purification and characterization of an oxygen-insensitive NAD(P)H nitroreductase from Enterobacter cloacae. J Biol Chem 266:4119-4125
    • (1991) J Biol Chem , vol.266 , pp. 4119-4125
    • Bryant, C.1    DeLuca, M.2
  • 10
    • 0033775615 scopus 로고    scopus 로고
    • Absolute quantification of mRNA using real-time reverse transcription polymerase
    • Bustin SA (2000) Absolute quantification of mRNA using real-time reverse transcription polymerase. J Mol Endocrinol 25:169-193
    • (2000) J Mol Endocrinol , vol.25 , pp. 169-193
    • Bustin, S.A.1
  • 11
    • 0025946763 scopus 로고
    • Decision making - Is bioremediation a viable option
    • Fiorenza S, Dunston KL, Ward CH (1991) Decision making - is bioremediation a viable option. J Hazard Mater 28:171-283
    • (1991) J Hazard Mater , vol.28 , pp. 171-283
    • Fiorenza, S.1    Dunston, K.L.2    Ward, C.H.3
  • 12
    • 0030902355 scopus 로고    scopus 로고
    • Transformation of 2,4,6-trinitrotoluene by Pseudomonas pseudoalcaligenes JS52
    • Fiorella P, Spain J (1997) Transformation of 2,4,6-trinitrotoluene by Pseudomonas pseudoalcaligenes JS52. Appl Environ Microbiol 63:2007-2201
    • (1997) Appl Environ Microbiol , vol.63 , pp. 2007-2201
    • Fiorella, P.1    Spain, J.2
  • 13
    • 0028774535 scopus 로고
    • Old yellow enzyme at 2 Å resolution: Overall structure, ligand binding, and comparison with related flavoproteins
    • Fox KM, Karplus PA (1994) Old yellow enzyme at 2 Å resolution: overall structure, ligand binding, and comparison with related flavoproteins. Structure 2:1089-1105
    • (1994) Structure , vol.2 , pp. 1089-1105
    • Fox, K.M.1    Karplus, P.A.2
  • 14
    • 0031948118 scopus 로고    scopus 로고
    • Aerobic degradation of 2,4,6-trinitrotoluene by Enterobacter cloacae PB2 and by pentaerythritol tetranitrate reductase
    • French CE, Nicklin S, Bruce NC (1998) Aerobic degradation of 2,4,6-trinitrotoluene by Enterobacter cloacae PB2 and by pentaerythritol tetranitrate reductase. Appl Environ Microbiol 64:2864-2868
    • (1998) Appl Environ Microbiol , vol.64 , pp. 2864-2868
    • French, C.E.1    Nicklin, S.2    Bruce, N.C.3
  • 15
    • 0029846031 scopus 로고    scopus 로고
    • Genetic manipulation of acid formation pathways by gene inactivation in Clostridium acetobutylicum ATCC 824
    • Green EM, Boynton ZL, Harris LM, Rudolph FB, Papoutsakis ET, Bennett GN (1996) Genetic manipulation of acid formation pathways by gene inactivation in Clostridium acetobutylicum ATCC 824. Microbiology 142:2079-2086
    • (1996) Microbiology , vol.142 , pp. 2079-2086
    • Green, E.M.1    Boynton, Z.L.2    Harris, L.M.3    Rudolph, F.B.4    Papoutsakis, E.T.5    Bennett, G.N.6
  • 17
    • 14744306436 scopus 로고
    • Simultaneous amplification and detection of specific DNA sequences
    • NY
    • Higuchi R, Dollinger G, Walsh PS, Griffith R (1992) Simultaneous amplification and detection of specific DNA sequences. Biotechnol (NY) 10:413-417
    • (1992) Biotechnol , vol.10 , pp. 413-417
    • Higuchi, R.1    Dollinger, G.2    Walsh, P.S.3    Griffith, R.4
  • 20
    • 0141790765 scopus 로고    scopus 로고
    • Studies on the nitroreductase prodrug-activating system. Crystal structures of complexes with the inhibitor dicoumarol and dinitrobenzamide prodrugs and of the enzyme active form
    • Johansson E, Parkinson GN, Denny WA, Neidle S (2003) Studies on the nitroreductase prodrug-activating system. Crystal structures of complexes with the inhibitor dicoumarol and dinitrobenzamide prodrugs and of the enzyme active form. J Med Chem 11:4009-4020
    • (2003) J Med Chem , vol.11 , pp. 4009-4020
    • Johansson, E.1    Parkinson, G.N.2    Denny, W.A.3    Neidle, S.4
  • 22
    • 0029557273 scopus 로고
    • Structure-function relations for old yellow enzyme
    • Karplus AP, Fox KM, Massey V (1995) Structure-function relations for old yellow enzyme. FASEB J. 9:1518-1526
    • (1995) FASEB J. , vol.9 , pp. 1518-1526
    • Karplus, A.P.1    Fox, K.M.2    Massey, V.3
  • 23
    • 0030779793 scopus 로고    scopus 로고
    • Anaerobic transformation of 2,4,6-trinitrotoluene and related nitroaromatic compounds by Clostridium acetobutylicum
    • Khan TA, Bhadra R, Hughes JB (1997) Anaerobic transformation of 2,4,6-trinitrotoluene and related nitroaromatic compounds by Clostridium acetobutylicum. J Ind Microbiol Biotechnol 18:198-203
    • (1997) J Ind Microbiol Biotechnol , vol.18 , pp. 198-203
    • Khan, T.A.1    Bhadra, R.2    Hughes, J.B.3
  • 24
    • 27544485007 scopus 로고    scopus 로고
    • Purification and characterization of NAD(P)H-dependent nitroreductase I from Klebsiella sp. C1 and enzymatic transformation of 2,4,6-trinitrotoluene
    • Epub ahead of print
    • Kim HY, Song HG (2005) Purification and characterization of NAD(P)H-dependent nitroreductase I from Klebsiella sp. C1 and enzymatic transformation of 2,4,6-trinitrotoluene. Appl Microbiol Biotechnol Mar 24 [Epub ahead of print]
    • (2005) Appl Microbiol Biotechnol Mar , vol.24
    • Kim, H.Y.1    Song, H.G.2
  • 25
    • 0034064329 scopus 로고    scopus 로고
    • Type I nitroreductases in soil enterobacteria reduce TNT (2,4,6,-trinitrotoluene) and RDX (hexahydro-1,3,5-trinitro-1,3,5-triazine)
    • Kitts CL, Green CE, Otley RA, Alvarez MA, Unkefer PJ (2000). Type I nitroreductases in soil enterobacteria reduce TNT (2,4,6,-trinitrotoluene) and RDX (hexahydro-1,3,5-trinitro-1,3,5-triazine). Can J Microbiol 46:278-282
    • (2000) Can J Microbiol , vol.46 , pp. 278-282
    • Kitts, C.L.1    Green, C.E.2    Otley, R.A.3    Alvarez, M.A.4    Unkefer, P.J.5
  • 26
    • 0035951874 scopus 로고    scopus 로고
    • Structure and site-directed mutagenesis of a flavoprotein from Escherichia coli that reduces nitrocompounds: Alteration of pyridine nucleotide binding by a single amino acid substitution
    • Kobori T, Sasaki H, Lee WC, Zenno S, Saigo K, Murphy ME, Tanokura M (2001) Structure and site-directed mutagenesis of a flavoprotein from Escherichia coli that reduces nitrocompounds: alteration of pyridine nucleotide binding by a single amino acid substitution. J Biol Chem 276:2816-2823
    • (2001) J Biol Chem , vol.276 , pp. 2816-2823
    • Kobori, T.1    Sasaki, H.2    Lee, W.C.3    Zenno, S.4    Saigo, K.5    Murphy, M.E.6    Tanokura, M.7
  • 27
    • 0032483986 scopus 로고    scopus 로고
    • The oxidative half-reaction of old yellow enzyme
    • Kohli RM, Massey V (1998) The oxidative half-reaction of old yellow enzyme. J Biol Chem 273:32763-32770
    • (1998) J Biol Chem , vol.273 , pp. 32763-32770
    • Kohli, R.M.1    Massey, V.2
  • 28
    • 0032503694 scopus 로고    scopus 로고
    • 1.8 Å crystal structure of the major NAD(P)H:FMN oxidoreductase of a bioluminescent bacterium, Vibrio fischeri: Overall structure, cofactor and substrate-analog binding, and comparison with related flavoproteins
    • Koike H, Sasaki H, Kobori T, Zenno S, Saigo K, Murphy ME, Adman ET, Tanokura M (1998) 1.8 Å crystal structure of the major NAD(P)H:FMN oxidoreductase of a bioluminescent bacterium, Vibrio fischeri: overall structure, cofactor and substrate-analog binding, and comparison with related flavoproteins. J Mol Biol 280:259-273
    • (1998) J Mol Biol , vol.280 , pp. 259-273
    • Koike, H.1    Sasaki, H.2    Kobori, T.3    Zenno, S.4    Saigo, K.5    Murphy, M.E.6    Adman, E.T.7    Tanokura, M.8
  • 29
    • 12444281969 scopus 로고    scopus 로고
    • Perspectives of bioelimination of polynitroaromatic compounds
    • Spain JC, Hughes JB, Knackmuss HJ (eds) CRC Press, Boca Raton Fla
    • Lenke H, Achtnich C, Knackmuss HJ (2000) Perspectives of bioelimination of polynitroaromatic compounds. In: Spain JC, Hughes JB, Knackmuss HJ (eds) Biodegradation of nitroaromatic compounds and explosives. CRC Press, Boca Raton Fla, pp 91-126
    • (2000) Biodegradation of Nitroaromatic Compounds and Explosives , pp. 91-126
    • Lenke, H.1    Achtnich, C.2    Knackmuss, H.J.3
  • 30
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of Relative gene expression data using real-time quantitative PCR and the 22DDCT method
    • Livak KJ, Schmittgen TD (2001) Analysis of Relative gene expression data using real-time quantitative PCR and the 22DDCT method. Methods 25:402-408
    • (2001) Methods , vol.25 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 31
    • 0033616612 scopus 로고    scopus 로고
    • Nitroreductase A is regulated as a member of the soxRS regulon of Escherichia coli
    • USA
    • Liochev SI, Hausladen A, Fridovich I (1999) Nitroreductase A is regulated as a member of the soxRS regulon of Escherichia coli. Proc Natl Acad Sci USA 96:3537-3539
    • (1999) Proc Natl Acad Sci , vol.96 , pp. 3537-3539
    • Liochev, S.I.1    Hausladen, A.2    Fridovich, I.3
  • 32
    • 0016766271 scopus 로고
    • Identification of p-hydroxybenzaldehyde as the ligand in the green form of old yellow enzyme
    • Matthews RG, Massey V, Sweeley CC (1975) Identification of p-hydroxybenzaldehyde as the ligand in the green form of old yellow enzyme. J Biol Chem 250:9294-9298
    • (1975) J Biol Chem , vol.250 , pp. 9294-9298
    • Matthews, R.G.1    Massey, V.2    Sweeley, C.C.3
  • 34
    • 0027251005 scopus 로고
    • Degradation of nitrobenzene by a Pseudomonas pseudoalcaligenes
    • Nishino SF, Spain JC (1993) Degradation of nitrobenzene by a Pseudomonas pseudoalcaligenes. Appl Environ Microbiology 59:2520-2525
    • (1993) Appl Environ Microbiology , vol.59 , pp. 2520-2525
    • Nishino, S.F.1    Spain, J.C.2
  • 37
    • 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, Stolz A (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
  • 38
    • 0027233523 scopus 로고
    • Comparison of the azoreductase and nitroreductase from Clostridium perfringens
    • Rafii F, Cerniglia CE (1993) Comparison of the azoreductase and nitroreductase from Clostridium perfringens. Appl Environ Microbiol 59:1731-1734
    • (1993) Appl Environ Microbiol , vol.59 , pp. 1731-1734
    • Rafii, F.1    Cerniglia, C.E.2
  • 39
    • 0001941045 scopus 로고
    • Basic knowledge and perspectives on biodegradation of 2,4,6-trinitrotoluene and related nitroaromatic compounds in contaminated soil
    • Spain JC (ed) Plenum, New York
    • Rieger PG, Knackmuss HJ (1995) Basic knowledge and perspectives on biodegradation of 2,4,6-trinitrotoluene and related nitroaromatic compounds in contaminated soil. In: Spain JC (ed) Biodegradation of nitroaromatic compounds. vol 49. Plenum, New York, pp 1-18
    • (1995) Biodegradation of Nitroaromatic Compounds , vol.49 , pp. 1-18
    • Rieger, P.G.1    Knackmuss, H.J.2
  • 40
    • 0345205320 scopus 로고
    • A study of enzymes, mechanisms of enzyme action
    • Kuby SA (ed) CRC, Boca Raton
    • Schopfer LM, Massey V (1991) A study of enzymes, mechanisms of enzyme action. In: Kuby SA (ed) Old yellow enzyme. CRC, Boca Raton, pp 247-269
    • (1991) Old Yellow Enzyme , pp. 247-269
    • Schopfer, L.M.1    Massey, V.2
  • 41
    • 0029007418 scopus 로고
    • Purification and characterization of nitrobenzene nitroreductase from Pseudomonas pseudoalcaligenes JS45
    • Somerville CC, Nishino SF, Spain JC (1995) Purification and characterization of nitrobenzene nitroreductase from Pseudomonas pseudoalcaligenes JS45. J Bacteriol 177:3837-3842
    • (1995) J Bacteriol , vol.177 , pp. 3837-3842
    • Somerville, C.C.1    Nishino, S.F.2    Spain, J.C.3
  • 42
    • 0028841595 scopus 로고
    • Biodegradation of nitroaromatic compounds
    • Spain JC (1995) Biodegradation of nitroaromatic compounds Annu Rev Microbiol 49:523-555
    • (1995) Annu Rev Microbiol , vol.49 , pp. 523-555
    • Spain, J.C.1
  • 44
    • 0026651506 scopus 로고
    • Mutagenicity of trinitrotoluene and its metabolites formed during composting
    • Tan EL, Ho CH, Griest WH, Tyndall RL (1992) Mutagenicity of trinitrotoluene and its metabolites formed during composting. J Toxicol Environ Health 36:165-175
    • (1992) J Toxicol Environ Health , vol.36 , pp. 165-175
    • Tan, E.L.1    Ho, C.H.2    Griest, W.H.3    Tyndall, R.L.4
  • 45
    • 0029960505 scopus 로고    scopus 로고
    • Flavin reductase P: Structure of a dimeric enzyme that reduces flavin
    • Tanner JJ, Lei B, Tu SC, Krause KL (1996) Flavin reductase P: structure of a dimeric enzyme that reduces flavin. Biochemistry 35:13531-13539
    • (1996) Biochemistry , vol.35 , pp. 13531-13539
    • Tanner, J.J.1    Lei, B.2    Tu, S.C.3    Krause, K.L.4
  • 46
    • 0020423788 scopus 로고
    • Oxygen-insensitive nitrofuran reductases in Salmonella typhimurium TA 100
    • Tatsumi K, Doi T, Yoshimura H, Koga H, Horiuchi T (1982) Oxygen-insensitive nitrofuran reductases in Salmonella typhimurium TA 100. J. Pharm Dyn 5:423-429
    • (1982) J. Pharm Dyn , vol.5 , pp. 423-429
    • Tatsumi, K.1    Doi, T.2    Yoshimura, H.3    Koga, H.4    Horiuchi, T.5
  • 48
    • 0017235834 scopus 로고
    • Toxicity and mutagenicity of 2,4,6-trinitrotoluene and its microbial metabolites
    • Won WD, DiSalvo LH, Ng J (1976) Toxicity and mutagenicity of 2,4,6-trinitrotoluene and its microbial metabolites. Appl Environ Microbiol 31:576-580
    • (1976) Appl Environ Microbiol , vol.31 , pp. 576-580
    • Won, W.D.1    DiSalvo, L.H.2    Ng, J.3
  • 49
  • 50
    • 18244376061 scopus 로고    scopus 로고
    • Reductive transformation of TNT by Escherichia coli:pathway description
    • Yin H, Wood TK, Smet 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    Smet, B.F.3
  • 51
    • 0031952137 scopus 로고    scopus 로고
    • Conversion of NfsA, the major Escherichia coli nitroreductase, to a flavin reductase with an activity similar to that of Frp, a flavin reductase in Vibrio harveyi, by a single amino acid substitution
    • Zenno ST, Kobori T, Tanokura M, Saigo K (1998) Conversion of NfsA, the major Escherichia coli nitroreductase, to a flavin reductase with an activity similar to that of Frp, a flavin reductase in Vibrio harveyi, by a single amino acid substitution. J Bacteriol 180:422-425
    • (1998) J Bacteriol , vol.180 , pp. 422-425
    • Zenno, S.T.1    Kobori, T.2    Tanokura, M.3    Saigo, K.4
  • 52
    • 0029745672 scopus 로고    scopus 로고
    • Biochemical characterization of NfsA, the Escherichia coli major nitroreductase exhibiting a high amino acid sequence homology to Frp, a Vibrio harveyi flavin oxidoreductase
    • Zenno S, Koike H, Kumar AN, Jayaraman R, Tanokura M, Saigo K (1996a) Biochemical characterization of NfsA, the Escherichia coli major nitroreductase exhibiting a high amino acid sequence homology to Frp, a Vibrio harveyi flavin oxidoreductase. J Bacteriol 178:4508-4514
    • (1996) J Bacteriol , vol.178 , pp. 4508-4514
    • Zenno, S.1    Koike, H.2    Kumar, A.N.3    Jayaraman, R.4    Tanokura, M.5    Saigo, K.6
  • 53
    • 0029808844 scopus 로고    scopus 로고
    • Gene cloning, purification, and characterization of NfsB, a minor oxygen-insensitive nitroreductase from Escherichia coli, similar in biochemical properties to FRase 1, the major flavin reductase in Vibrio fischeri
    • Tokyo
    • Zenno S, Koike H, Tanokura M, Saigo K (1996b) Gene cloning, purification, and characterization of NfsB, a minor oxygen-insensitive nitroreductase from Escherichia coli, similar in biochemical properties to FRase 1, the major flavin reductase in Vibrio fischeri. J Biochem (Tokyo) 120:736-744
    • (1996) J Biochem , vol.120 , pp. 736-744
    • Zenno, S.1    Koike, H.2    Tanokura, M.3    Saigo, K.4
  • 54
    • 0029770130 scopus 로고    scopus 로고
    • Conversion of NfsB, a minor Escherichia coli nitroreductase, to a flavin reductase similar in biochemical properties to FRase I, the major flavin reductase in Vibrio fischeri, by a single amino acid substitution
    • Zenno S, Koike H, Tanokura M, Saigo K (1996c) Conversion of NfsB, a minor Escherichia coli nitroreductase, to a flavin reductase similar in biochemical properties to FRase I, the major flavin reductase in Vibrio fischeri, by a single amino acid substitution. J Bacteriol 178:4731-4733
    • (1996) J Bacteriol , vol.178 , pp. 4731-4733
    • Zenno, S.1    Koike, H.2    Tanokura, M.3    Saigo, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.