메뉴 건너뛰기




Volumn 192, Issue 11, 2010, Pages 2737-2745

A novel hydrolytic dehalogenase for the chlorinated aromatic compound chlorothalonil

Author keywords

[No Author keywords available]

Indexed keywords

1,10 PHENANTHROLINE; ADENOSINE TRIPHOSPHATE; AROMATIC COMPOUND; ASPARTIC ACID; BETA LACTAMASE; CHLOROTHALONIL; COENZYME A; DIETHYL PYROCARBONATE; HISTIDINE; MONOMER; TRYPTOPHAN; NITRILE; RECOMBINANT PROTEIN;

EID: 77952574009     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.01547-09     Document Type: Article
Times cited : (68)

References (48)
  • 1
    • 38449091968 scopus 로고    scopus 로고
    • Identification of a chlorobenzene reductive dehalogenase in Dehalococcoides sp. strain CBDB1
    • Adrian, L., J. Rahnenfuhrer, J. Gobom, and T. Holscher. 2007. Identification of a chlorobenzene reductive dehalogenase in Dehalococcoides sp. strain CBDB1. Appl. Environ. Microbiol. 73:7717-7724.
    • (2007) Appl. Environ. Microbiol. , vol.73 , pp. 7717-7724
    • Adrian, L.1    Rahnenfuhrer, J.2    Gobom, J.3    Holscher, T.4
  • 2
    • 0034735782 scopus 로고    scopus 로고
    • Bacterial dehalorespiration with chlorinated benzenes
    • Adrian, L., S. Ulrich, W. Joerg, and G. Helmut. 2000. Bacterial dehalorespiration with chlorinated benzenes. Nature 408:580-583.
    • (2000) Nature , vol.408 , pp. 580-583
    • Adrian, L.1    Ulrich, S.2    Joerg, W.3    Helmut, G.4
  • 3
    • 0017614890 scopus 로고
    • Photochemical reaction of 2,45,6-tetrachloroisophthalonitrile
    • Binkley, R. W., G. L. Kirstner, V. C. Opaskar, and P. Olynyk. 1977. Photochemical reaction of 2,4,5,6-tetrachloroisophthalonitrile. Chemosphere 6:163-166.
    • (1977) Chemosphere , vol.6 , pp. 163-166
    • Binkley, R.W.1    Kirstner, G.L.2    Opaskar, V.C.3    Olynyk, P.4
  • 4
    • 0038343085 scopus 로고    scopus 로고
    • Purification, cloning and sequencing of an enzyme mediating the reductive dechlorination of 2,46-trichlorophenol from Desulfitobacterium frappieri PCP-1
    • Boyer, A., R. Page-BeLanger, M. Saucie, R. Villemur, F. Lepine, P. Juteau, and R. Beaudet. 2003. Purification, cloning and sequencing of an enzyme mediating the reductive dechlorination of 2,4,6-trichlorophenol from Desulfitobacterium frappieri PCP-1. Biochem. J. 373:297-303.
    • (2003) Biochem. J. , vol.373 , pp. 297-303
    • Boyer, A.1    Page-BeLanger, R.2    Saucie, M.3    Villemur, R.4    Lepine, F.5    Juteau, P.6    Beaudet, R.7
  • 5
    • 0346319020 scopus 로고    scopus 로고
    • Reductive dehalogenation of chlorinated dioxins by an anaerobic bacterium
    • DOI 10.1038/nature01237
    • Bunge, M., L. Adrian, A. Kraus, M. Opel, W. G. Lorenz, J. R. Andreesen, H. Gorisch, and U. Lechner. 2003. Reductive dehalogenation of chlorinated dioxins by an anaerobic bacterium. Nature 421:357-360. (Pubitemid 36157930)
    • (2003) Nature , vol.421 , Issue.6921 , pp. 357-360
    • Bunge, M.1    Adrian, L.2    Kraus, A.3    Opel, M.4    Lorenz, W.G.5    Andreesen, J.R.6    Gorisch, H.7    Lechner, U.8
  • 7
    • 0032475852 scopus 로고    scopus 로고
    • Purification and characterization of the 3-chloro-4- Hydroxy- phenylacetate reductive dehalogenase of Desulfitobacterium hafniense
    • Christiansen, N., B. K. Ahring, G. Wohlfarth, and G. Diekert. 1998. Purification and characterization of the 3-chloro-4- hydroxy-phenylacetate reductive dehalogenase of Desulfitobacterium hafniense. FEBS Lett. 436:159-162.
    • (1998) FEBS Lett. , vol.436 , pp. 159-162
    • Christiansen, N.1    Ahring, B.K.2    Wohlfarth, G.3    Diekert, G.4
  • 8
    • 0032175395 scopus 로고    scopus 로고
    • Microbial dehalogenases: Enzymes recruited to convert xenobiotic substrates
    • Copley, S. D. 1998. Microbial dehalogenases: enzymes recruited to convert xenobiotic substrates. Curr. Opin. Chem. Biol. 2:613-617.
    • (1998) Curr. Opin. Chem. Biol. , vol.2 , pp. 613-617
    • Copley, S.D.1
  • 9
    • 0003082320 scopus 로고    scopus 로고
    • Chlorothalonil
    • Cox, C. 1997. Chlorothalonil. J. Pest. Reform. 17:14-20.
    • (1997) J. Pest. Reform. , vol.17 , pp. 14-20
    • Cox, C.1
  • 10
    • 0032420333 scopus 로고    scopus 로고
    • JPred: A consensus secondary structure prediction server
    • DOI 10.1093/bioinformatics/14.10.892
    • Cuff, J. A., M. E. Clamp, A. S. Siddigni, M. Finlay, and G. J. Barton. 1998. JPred: a consensus secondary structure prediction server. Bioinformatics 14:892-893. (Pubitemid 29041548)
    • (1998) Bioinformatics , vol.14 , Issue.10 , pp. 892-893
    • Cuff, J.A.1    Clamp, M.E.2    Siddiqui, A.S.3    Finlay, M.4    Barton, G.J.5
  • 11
    • 0346220394 scopus 로고    scopus 로고
    • Structure and mechanism of bacterial dehalogenases: Different ways to cleave a carbon-halogen bond
    • de Jong, R. M., and B. W. Dijkstra. 2003. Structure and mechanism of bacterial dehalogenases: different ways to cleave a carbon-halogen bond. Curr. Opin. Struct. Biol. 13:722-730.
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 722-730
    • De Jong, R.M.1    Dijkstra, B.W.2
  • 12
    • 0000650644 scopus 로고
    • MNDO study of nucleophilic aromatic substitution
    • Dotterer, S. K., and R. L. Harris. 1988. MNDO study of nucleophilic aromatic substitution. J. Org. Chem. 53:777-779.
    • (1988) J. Org. Chem. , vol.53 , pp. 777-779
    • Dotterer, S.K.1    Harris, R.L.2
  • 13
    • 0035286629 scopus 로고    scopus 로고
    • Reductive coenzyme A-mediated pathway for 3-chlorobenzoate degradation in the phototrophic bacterium Rhodopseudomonas palustris
    • Egland, P. G., J. Gibson, and C. S. Harwood. 2001. Reductive, coenzyme A-mediated pathway for 3-chlorobenzoate degradation in the phototrophic bacterium Rhodopseudomonas palustris. Appl. Environ. Microbiol. 67:1396-1399.
    • (2001) Appl. Environ. Microbiol. , vol.67 , pp. 1396-1399
    • Egland, P.G.1    Gibson, J.2    Harwood, C.S.3
  • 14
    • 3142609729 scopus 로고    scopus 로고
    • Expression, purification, and characterization of a novel methyl parathion hydrolase
    • Fu, G., Z. Cui, T. Huang, and S. Li. 2004. Expression, purification, and characterization of a novel methyl parathion hydrolase. Protein Express. Purif. 36:170-176.
    • (2004) Protein Express. Purif. , vol.36 , pp. 170-176
    • Fu, G.1    Cui, Z.2    Huang, T.3    Li, S.4
  • 15
    • 0032450045 scopus 로고    scopus 로고
    • Reductive dechlorination in the energy metabolism of anaerobic bacteria
    • Holliger, C., G. Wohlfarth, and G. Diekert. 1999. Reductive dechlorination in the energy metabolism of anaerobic bacteria. FEMS Microbiol. Rev. 22:383-398.
    • (1999) FEMS Microbiol. Rev. , vol.22 , pp. 383-398
    • Holliger, C.1    Wohlfarth, G.2    Diekert, G.3
  • 16
    • 0001606804 scopus 로고
    • New colorimetric determination of chloride using mercuric thiocyanate and ferric ion
    • Iwasaki, I., S. Utsumi, and T. Ozawa. 1952. New colorimetric determination of chloride using mercuric thiocyanate and ferric ion. Bull. Chem. Soc. Jpn. 25:226.
    • (1952) Bull. Chem. Soc. Jpn. , vol.25 , pp. 226
    • Iwasaki, I.1    Utsumi, S.2    Ozawa, T.3
  • 18
    • 47149093338 scopus 로고    scopus 로고
    • Simultaneous determination of chlorothalonil and its metabolite 4-hydroxychlorothalonil in greenhouse air: Dissipation process of chlorothalonil
    • Kazos, E. A., C. G. Nanos, C. D. Stalikas, and C. N. Konidari. 2008. Simultaneous determination of chlorothalonil and its metabolite 4-hydroxychlorothalonil in greenhouse air: dissipation process of chlorothalonil. Chemosphere 72:1413-1419.
    • (2008) Chemosphere , vol.72 , pp. 1413-1419
    • Kazos, E.A.1    Nanos, C.G.2    Stalikas, C.D.3    Konidari, C.N.4
  • 19
    • 3042609853 scopus 로고    scopus 로고
    • Glutathione-dependent biotransformation of the fungicide chlorothalonil
    • Kim, Y. M., K. Park, G. J. Joo, E. M. Jeong, J. E. Kim, and I. K. Rhee. 2004. Glutathione-dependent biotransformation of the fungicide chlorothalonil. J. Agric. Food Chem. 52:4192-4196.
    • (2004) J. Agric. Food Chem. , vol.52 , pp. 4192-4196
    • Kim, Y.M.1    Park, K.2    Joo, G.J.3    Jeong, E.M.4    Kim, J.E.5    Rhee, I.K.6
  • 20
    • 0035798656 scopus 로고    scopus 로고
    • 12- And iron-sulfur-containing reductive dehalogenase from Desulfitobacterium chlororespirans
    • 12- and iron-sulfur-containing reductive dehalogenase from Desulfitobacterium chlororespirans. J. Biol. Chem. 276:40991-40997.
    • (2001) J. Biol. Chem. , vol.276 , pp. 40991-40997
    • Krasotkina, J.1    Walters, T.2    Maruya, K.A.3    Ragsdale, S.W.4
  • 21
    • 3242810318 scopus 로고    scopus 로고
    • MEGA3: Integrated software for molecular evolutionary genetics analysis and sequence alignment. Brief
    • Kumar, S., K. Tamura, and M. Nei. 2004. MEGA3: integrated software for molecular evolutionary genetics analysis and sequence alignment. Brief. Bioinform. 5:150-163.
    • (2004) Bioinform , vol.5 , pp. 150-163
    • Kumar, S.1    Tamura, K.2    Nei, M.3
  • 22
    • 0035859887 scopus 로고    scopus 로고
    • The active site dynamics of 4-chlorobenzoyl-CoA dehalogenase
    • Lau, E. Y., and T. C. Bruice. 2001. The active site dynamics of 4-chlorobenzoyl-CoA dehalogenase. Proc. Natl. Acad. Sci. U. S. A. 98:9527-9532.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 9527-9532
    • Lau, E.Y.1    Bruice, T.C.2
  • 24
    • 0024284028 scopus 로고
    • A simple salting out procedure for extracting DNA from human nucleated cells
    • Miller, S. A., D. D. Dykes, and H. F. Polesky. 1988. A simple salting out procedure for extracting DNA from human nucleated cells. Nucleic Acids Res. 16:1215.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 1215
    • Miller, S.A.1    Dykes, D.D.2    Polesky, H.F.3
  • 25
    • 0031895255 scopus 로고    scopus 로고
    • Cloning and sequencing of a 25-dichlorohydroquinone reductive dehalogenase gene whose product is involved in degradation of γ-hexachlorocyclohexane by Sphingomonas paucimobilis
    • Miyachi, K., S. K. Suh, T. Nagata, and M. Takagi. 1998. Cloning and sequencing of a 2,5-dichlorohydroquinone reductive dehalogenase gene whose product is involved in degradation of γ-hexachlorocyclohexane by Sphingomonas paucimobilis. J. Bacteriol. 180:1354-1359.
    • (1998) J. Bacteriol. , vol.180 , pp. 1354-1359
    • Miyachi, K.1    Suh, S.K.2    Nagata, T.3    Takagi, M.4
  • 26
    • 85047677661 scopus 로고    scopus 로고
    • Biodegradation of chlorothalonil in soil after suppression of degradation
    • Motonaga, K., K. Takagi, and S. Matumoto. 1996. Biodegradation of chlorothalonil in soil after suppression of degradation. Biol. Fertil. Soils 23:340-345.
    • (1996) Biol. Fertil. Soils , vol.23 , pp. 340-345
    • Motonaga, K.1    Takagi, K.2    Matumoto, S.3
  • 28
    • 0029129063 scopus 로고
    • Purification and characterization of a novel 3-chlorobenzoate-reductive dehalogenase from the cytoplasmic membrane of Desulfomonile tiedjei DCB-1
    • Ni, S., J. K. Fredrickson, and L. Xun. 1995. Purification and characterization of a novel 3-chlorobenzoate-reductive dehalogenase from the cytoplasmic membrane of Desulfomonile tiedjei DCB-1. J. Bacteriol. 177:5135-5139.
    • (1995) J. Bacteriol. , vol.177 , pp. 5135-5139
    • Ni, S.1    Fredrickson, J.K.2    Xun, L.3
  • 29
    • 0027476196 scopus 로고
    • Cloning, sequence analysis, and expression of the Flavobacterium pentachlorophenol-4-monooxygenase gene in Escherichia coli
    • Orser, C. S., C. C. Lange, L. Xun, T. C. Zahrt, and B. J. Schneider. 1993. Cloning, sequence analysis, and expression of the Flavobacterium pentachlorophenol-4-monooxygenase gene in Escherichia coli. J. Bacteriol. 175:411-416. (Pubitemid 23032002)
    • (1993) Journal of Bacteriology , vol.175 , Issue.2 , pp. 411-416
    • Orser, C.S.1    Lange, C.C.2    Xun, L.3    Zahrt, T.C.4    Schneider, B.J.5
  • 30
    • 0033974553 scopus 로고    scopus 로고
    • Degradation of pentachlorophenol by Phanerochaete chrysosporium: Intermediates and reactions involved
    • Reddy, G. V. B., and M. H. Gold. 2000. Degradation of pentachlorophenol by Phanerochaete chrysosporium: intermediates and reactions involved. Microbiology 146:405-413.
    • (2000) Microbiology , vol.146 , pp. 405-413
    • Reddy, G.V.B.1    Gold, M.H.2
  • 31
    • 0029913853 scopus 로고    scopus 로고
    • NADPH-dependent reductive ortho dehalogenation of 24-dichlorobenzoic acid in Corynebacterium sepedonicum KZ-4 and coryneform bacterium strain NTB-1 via 2,4-dichlorobenzoyl coenzyme a
    • Romanov, V., and R. P. Hausinger. 1996. NADPH-dependent reductive ortho dehalogenation of 2,4-dichlorobenzoic acid in Corynebacterium sepedonicum KZ-4 and coryneform bacterium strain NTB-1 via 2,4-dichlorobenzoyl coenzyme A. J. Bacteriol. 178:2656-2661.
    • (1996) J. Bacteriol. , vol.178 , pp. 2656-2661
    • Romanov, V.1    Hausinger, R.P.2
  • 32
    • 0026446053 scopus 로고
    • Cloning and sequence analysis of genes for dehalogenation of 4-chlorobenzoate from Arthrobacter sp. strain SU
    • Schmitz, A., K. Gartemann, J. Fiedler, E. Grundt, and R. Eichenlaub. 1992. Cloning and sequence analysis of genes for dehalogenation of 4-chlorobenzoate from Arthrobacter sp. strain SU. Appl. Environ. Microbiol. 58:4068-4071.
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 4068-4071
    • Schmitz, A.1    Gartemann, K.2    Fiedler, J.3    Grundt, E.4    Eichenlaub, R.5
  • 34
    • 0023645142 scopus 로고
    • Purification and some properties of component B of the 4-chlorophenylacetate 3,4-dioxygenase from Pseudomonas species strain CBS3
    • Schweizer, D., A. Markus, M. Seez, H. H. Ruf, and F. Lingens. 1987. Purification and some properties of component B of the 4-chlorophenylacetate 3,4-dioxygenase from Pseudomonas species strain CBS3. J. Biol. Chem. 262:9340-9346.
    • (1987) J. Biol. Chem. , vol.262 , pp. 9340-9346
    • Schweizer, D.1    Markus, A.2    Seez, M.3    Ruf, H.H.4    Lingens, F.5
  • 36
    • 9244251590 scopus 로고    scopus 로고
    • Anaerobic microbial dehalogenation
    • Smidt, H., and W. M. de Vos. 2004. Anaerobic microbial dehalogenation. Annu. Rev. Microbiol. 58:43-73.
    • (2004) Annu. Rev. Microbiol. , vol.58 , pp. 43-73
    • Smidt, H.1    De Vos, W.M.2
  • 37
    • 85087234904 scopus 로고    scopus 로고
    • Identification of chlorobenzene dioxygenase sequence elements involved in dechlorination of 1,2,4,5-tetrachlorobenzene
    • Stefan, B., R. M. Jeremy, N. T. Kenneth, and H. P. Dietmar. 1998. Identification of chlorobenzene dioxygenase sequence elements involved in dechlorination of 1,2,4,5-tetrachlorobenzene. J. Bacteriol. 180:520-5528.
    • (1998) J. Bacteriol. , vol.180 , pp. 520-5528
    • Stefan, B.1    Jeremy, R.M.2    Kenneth, N.T.3    Dietmar, H.P.4
  • 38
    • 4143110165 scopus 로고    scopus 로고
    • Purification, cloning, and sequencing of a 35-dichlorophenol reductive dehalogenase from Desulfitobacterium frappieri PCP-1
    • Thibodeau, J., A. Gauthier, M. Duguay, R. Villemur, F. Lepine, P. Juteau, and R. Beaudet. 2004. Purification, cloning, and sequencing of a 3,5-dichlorophenol reductive dehalogenase from Desulfitobacterium frappieri PCP-1. Appl. Environ. Microbiol. 70:4532-4537.
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 4532-4537
    • Thibodeau, J.1    Gauthier, A.2    Duguay, M.3    Villemur, R.4    Lepine, F.5    Juteau, P.6    Beaudet, R.7
  • 39
    • 0032902395 scopus 로고    scopus 로고
    • Cloning, expression, and nucleotide sequence of the Pseudomonas aeruginosa 142 ohb genes coding for oxygenolytic ortho dehalogenation of halobenzoates
    • Tsoi, T. V., E. G. Plotnikova, J. R. Cole, W. F. Guerin, M. Bagdasarian, and J. M. Tiedje. 1999. Cloning, expression, and nucleotide sequence of the Pseudomonas aeruginosa 142 ohb genes coding for oxygenolytic ortho dehalogenation of halobenzoates. Appl. Environ. Microbiol. 65:2151-2162.
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 2151-2162
    • Tsoi, T.V.1    Plotnikova, E.G.2    Cole, J.R.3    Guerin, W.F.4    Bagdasarian, M.5    Tiedje, J.M.6
  • 40
    • 0033575218 scopus 로고    scopus 로고
    • Purification and molecular characterization of ortho-chlorophenol reductive dehalogenase a key enzyme of halorespiration in Desulfitobacterium dehalogenans
    • Van de Pas, B. A., H. Smidt, W. R. Hagen, J. van der Oost, G. Schraa, A. J. M. Stams, and W. M. de Vos. 1999. Purification and molecular characterization of ortho-chlorophenol reductive dehalogenase, a key enzyme of halorespiration in Desulfitobacterium dehalogenans. J. Biol. Chem. 274:20287-20292.
    • (1999) J. Biol. Chem. , vol.274 , pp. 20287-20292
    • Van De Pas, B.A.1    Smidt, H.2    Hagen, W.R.3    Van Der Oost, J.4    Schraa, G.5    Stams, A.J.M.6    De Vos, W.M.7
  • 41
    • 0037908831 scopus 로고    scopus 로고
    • Biological dehalogenation and halogenation reactions
    • van Pee, K., and S. Unversucht. 2003. Biological dehalogenation and halogenation reactions. Chemosphere 52:299-312.
    • (2003) Chemosphere , vol.52 , pp. 299-312
    • Van Pee, K.1    Unversucht, S.2
  • 42
    • 0027337615 scopus 로고
    • Crystallographic analysis of the catalytic mechanism of haloalkane dehalogenase
    • DOI 10.1038/363693a0
    • Verschueren, K. H. G., F. Seljee, H. J. Rozeboom, K. H. Kalk, and B. W. Dijkstra. 1993. Crystallographic analysis of the catalytic mechanism of haloalkane dehalogenase. Nature 363:693-698. (Pubitemid 23227646)
    • (1993) Nature , vol.363 , Issue.6431 , pp. 693-698
    • Verschueren, K.H.G.1    Seljee, F.2    Rozeboom, H.J.3    Kalk, K.H.4    Dijkstra, B.W.5
  • 43
    • 0028263070 scopus 로고
    • Structure and function of glutathione S-transferases
    • Wilce, M. C., and M. W. Parker. 1994. Structure and function of glutathione S-transferases. Biochim. Biophys. Acta 1205:1-18.
    • (1994) Biochim. Biophys. Acta , vol.1205 , pp. 1-18
    • Wilce, M.C.1    Parker, M.W.2
  • 45
    • 0033590113 scopus 로고    scopus 로고
    • Characterization of 2,6-dichlorop-hydroquinone 1,2-dioxygenase (PcpA) of Sphingomonas chlorophenolica ATCC 39723
    • Xun, L., J. Bohuslavek, and M. Cai. 1999. Characterization of 2,6-dichlorop-hydroquinone 1,2-dioxygenase (PcpA) of Sphingomonas chlorophenolica ATCC 39723. Biochem. Biophys. Res. Commun. 266:322-325.
    • (1999) Biochem. Biophys. Res. Commun. , vol.266 , pp. 322-325
    • Xun, L.1    Bohuslavek, J.2    Cai, M.3
  • 46
    • 0026743357 scopus 로고
    • Purification and characterization of a tetrachloro-p-hydroquinone reductive dehalogenase from a Flavobacterium sp
    • Xun, L., T. Edward, and S. O. Cindy. 1992. Purification and characterization of a tetrachloro-p-hydroquinone reductive dehalogenase from a Flavobacterium sp. J. Bacteriol. 174:8003-8007.
    • (1992) J. Bacteriol. , vol.174 , pp. 803-8007
    • Xun, L.1    Edward, T.2    Cindy, S.O.3
  • 47
    • 0029765125 scopus 로고    scopus 로고
    • Identification of active site residues essential to 4-chlorobenzoyl- Coenzyme a dehalogenase catalysis by chemical modification and site directed mutagenesis
    • DOI 10.1021/bi9609533
    • Yang, G., R. Q. Liu, K. L. Taylor, H. Xiang, J. Price, and D. Dunaway- Mariano. 1996. Identification of active site residues essential to 4-chlorobenzoyl-coenzyme A dehalogenase catalysis by chemical modification and site directed mutagenesis. Biochemistry 35:10879-10885. (Pubitemid 26279670)
    • (1996) Biochemistry , vol.35 , Issue.33 , pp. 10879-10885
    • Yang, G.1    Liu, R.-Q.2    Taylor, K.L.3    Xiang, H.4    Price, J.5    Dunaway-Mariano, D.6
  • 48
    • 0031040424 scopus 로고    scopus 로고
    • Mechanism of nucleophilic aromatic substitution of 1-chloro-2,4- dinitrobenzene by glutathione in the gas phase and in solution. Implications for the mode of action of glutathione S-transferases
    • Zheng, Y. J., and R. L. Ornstein. 1997. Mechanism of nucleophilic aromatic substitution of 1-chloro-2,4-dinitrobenzene by glutathione in the gas phase and in solution. Implications for the mode of action of glutathione S-transferases. J. Am. Chem. Soc. 119:648-655.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 648-655
    • Zheng, Y.J.1    Ornstein, R.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.