메뉴 건너뛰기




Volumn 44, Issue 30, 2005, Pages 10360-10368

A mechanistic investigation of the thiol-disulfide exchange step in the reductive dehalogenation catalyzed by tetrachlorohydroquinone dehalogenase

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; CATALYSIS; DEGRADATION; ENZYMES; ISOMERIZATION; REACTION KINETICS;

EID: 23044509966     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi050666b     Document Type: Article
Times cited : (21)

References (35)
  • 1
    • 0026743357 scopus 로고
    • Purification and characterization of a tetrachloro-p-hydroquinone reductive dehalogenase from a Flavobacterium sp
    • Xun, L., Topp, E., and Orser, C. S. (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. 8003-8007
    • Xun, L.1    Topp, E.2    Orser, C.S.3
  • 2
    • 0026555180 scopus 로고
    • Glutathione is the reducing agent for the reductive dehalogenation of tetrachloro-p-hydroquinone by extracts from a Flavobacterium sp
    • Xun, L., Topp, E., and Orser, C. S. (1992) Glutathione is the reducing agent for the reductive dehalogenation of tetrachloro-p-hydroquinone by extracts from a Flavobacterium sp., Biochem. Biophys. Res. Commun. 182, 361-366.
    • (1992) Biochem. Biophys. Res. Commun. , vol.182 , pp. 361-366
    • Xun, L.1    Topp, E.2    Orser, C.S.3
  • 3
    • 0037192150 scopus 로고    scopus 로고
    • Characterization of the initial steps in the reductive dehalogenation catalyzed by tetrachlorohydroquinone dehalogenase
    • Kiefer, P. M., Jr., and Copley, S. D. (2002) Characterization of the initial steps in the reductive dehalogenation catalyzed by tetrachlorohydroquinone dehalogenase, Biochemistry 41, 1315-1322.
    • (2002) Biochemistry , vol.41 , pp. 1315-1322
    • Kiefer Jr., P.M.1    Copley, S.D.2
  • 4
    • 0037192128 scopus 로고    scopus 로고
    • The reaction catalyzed by tetrachlorohydroquinone dehalogenase does not involve nucleophilic aromatic substitution
    • Kiefer, P. M., Jr., McCarthy, D. L., and Copley, S. D. (2002) The reaction catalyzed by tetrachlorohydroquinone dehalogenase does not involve nucleophilic aromatic substitution, Biochemistry 41, 1308-1314.
    • (2002) Biochemistry , vol.41 , pp. 1308-1314
    • Kiefer Jr., P.M.1    McCarthy, D.L.2    Copley, S.D.3
  • 5
    • 0030670259 scopus 로고    scopus 로고
    • Identification of a covalent intermediate between glutathione and cysteine13 during catalysis by tetrachlorohydroquinone dehalogenase
    • McCarthy, D. L., Louie, D. F., and Copley, S. D. (1997) Identification of a covalent intermediate between glutathione and cysteine13 during catalysis by tetrachlorohydroquinone dehalogenase, J. Am. Chem. Soc. 119, 11337-11338.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 11337-11338
    • McCarthy, D.L.1    Louie, D.F.2    Copley, S.D.3
  • 6
    • 0030445133 scopus 로고    scopus 로고
    • Exploration of the relationship between tetrachlorohydroquinone dehalogenase and the glutathione S-transferase superfamily
    • McCarthy, D. L., Navarrete, S., Willett, W. S., Babbitt, P. C., and Copley, S. D. (1996) Exploration of the relationship between tetrachlorohydroquinone dehalogenase and the glutathione S-transferase superfamily, Biochemistry 35, 14634-14642.
    • (1996) Biochemistry , vol.35 , pp. 14634-14642
    • McCarthy, D.L.1    Navarrete, S.2    Willett, W.S.3    Babbitt, P.C.4    Copley, S.D.5
  • 7
    • 0031439569 scopus 로고    scopus 로고
    • Zeta, a novel class of glutathione transferases in a range of species from plants to humans
    • Board, P. G., Baker, R. T., Chelvanayagam, G., and Jermiin, L. S. (1997) Zeta, a novel class of glutathione transferases in a range of species from plants to humans, Biochem. J. 328, 929-935.
    • (1997) Biochem. J. , vol.328 , pp. 929-935
    • Board, P.G.1    Baker, R.T.2    Chelvanayagam, G.3    Jermiin, L.S.4
  • 8
    • 0034625156 scopus 로고    scopus 로고
    • Recruitment of a double bond isomerase to serve as a reductive dehalogenase during biodegradation of pentachlorophenol
    • Anandarajah, K., Kiefer, P. M., and Copley, S. D. (2000) Recruitment of a double bond isomerase to serve as a reductive dehalogenase during biodegradation of pentachlorophenol, Biochemistry 39, 5303-5311.
    • (2000) Biochemistry , vol.39 , pp. 5303-5311
    • Anandarajah, K.1    Kiefer, P.M.2    Copley, S.D.3
  • 9
    • 0015918820 scopus 로고
    • Purification and properties of maleylacetone cis-trans isomerase from Vibrio 01
    • Seltzer, S. (1973) Purification and properties of maleylacetone cis-trans isomerase from Vibrio 01, J. Biol. Chem. 248, 215-222.
    • (1973) J. Biol. Chem. , vol.248 , pp. 215-222
    • Seltzer, S.1
  • 10
    • 0018466476 scopus 로고
    • Maleylacetone cis-trans-isomerase. Mechanism of the interaction of coenzyme glutathione and substrate maleylacetone in the presence and absence of enzyme
    • Seltzer, S., and Lin, M. (1979) Maleylacetone cis-trans-isomerase. Mechanism of the interaction of coenzyme glutathione and substrate maleylacetone in the presence and absence of enzyme, J. Am. Chem. Soc. 101, 3091-3097.
    • (1979) J. Am. Chem. Soc. , vol.101 , pp. 3091-3097
    • Seltzer, S.1    Lin, M.2
  • 11
    • 0025971827 scopus 로고
    • Glutathione S-transferases: Reaction mechanism, structure, and function
    • Armstrong, R. N. (1991) Glutathione S-transferases: reaction mechanism, structure, and function, Chem. Res. Toxicol. 4, 131-140.
    • (1991) Chem. Res. Toxicol. , vol.4 , pp. 131-140
    • Armstrong, R.N.1
  • 12
    • 0035852844 scopus 로고    scopus 로고
    • Crystal structure of maleylacetoacetate isomerase/glutathione transferase zeta reveals the molecular basis for its remarkable catalytic promiscuity
    • Polekhina, G., Board, P. G., Blackburn, A. C., and Parker, M. W. (2001) Crystal structure of maleylacetoacetate isomerase/glutathione transferase zeta reveals the molecular basis for its remarkable catalytic promiscuity. Biochemistry 40, 1567-1576.
    • (2001) Biochemistry , vol.40 , pp. 1567-1576
    • Polekhina, G.1    Board, P.G.2    Blackburn, A.C.3    Parker, M.W.4
  • 13
    • 0035906701 scopus 로고    scopus 로고
    • The structure of a zeta class glutathione S-transferase from Arabidopsis thaliana: Characterisation of a GT with novel active-site architecture and a putative role in tyrosine catabolism
    • Thorn, R., Dixon, D. P., Edwards, R., Cole, D. J., and Lapthorn, A. J. (2001) The structure of a zeta class glutathione S-transferase from Arabidopsis thaliana: Characterisation of a GT with novel active-site architecture and a putative role in tyrosine catabolism, J. Mol. Biol. 308, 949-962.
    • (2001) J. Mol. Biol. , vol.308 , pp. 949-962
    • Thorn, R.1    Dixon, D.P.2    Edwards, R.3    Cole, D.J.4    Lapthorn, A.J.5
  • 14
    • 0016391111 scopus 로고
    • Preparation of adsorbents for biospecific affinity chromatography
    • Sundberg, L., and Porath, J. (1974) Preparation of adsorbents for biospecific affinity chromatography, J. Chromatogr. 90, 87-98.
    • (1974) J. Chromatogr. , vol.90 , pp. 87-98
    • Sundberg, L.1    Porath, J.2
  • 15
    • 3042934967 scopus 로고
    • A colorimetric method for determining low concentrations of mercaptans
    • Ellman, G. (1959) A colorimetric method for determining low concentrations of mercaptans, Arch. Biochem. Biophys. 82, 70-77.
    • (1959) Arch. Biochem. Biophys. , vol.82 , pp. 70-77
    • Ellman, G.1
  • 16
    • 77957001732 scopus 로고
    • Reaction of protein sulfhydryl groups with Ellman's reagent
    • Habeeb, A. F. S. A. (1972) Reaction of protein sulfhydryl groups with Ellman's reagent, Methods Enzymol. 25, 457-464.
    • (1972) Methods Enzymol. , vol.25 , pp. 457-464
    • Habeeb, A.F.S.A.1
  • 18
    • 0014258846 scopus 로고
    • Sulfenyl halides as modifying reagents for polypeptides and proteins
    • Fontana, A., Scoffone, E., and Benassi, C. A. (1968) Sulfenyl halides as modifying reagents for polypeptides and proteins, Biochemistry 7, 980-986.
    • (1968) Biochemistry , vol.7 , pp. 980-986
    • Fontana, A.1    Scoffone, E.2    Benassi, C.A.3
  • 19
    • 0017088968 scopus 로고
    • Reduction of disulfide-containing amines, amino acids, and small peptides
    • Butler, J., Spielberg, S. P., and Schulman, J. D. (1976) Reduction of disulfide-containing amines, amino acids, and small peptides, Anal. Biochem. 75, 674-675.
    • (1976) Anal. Biochem. , vol.75 , pp. 674-675
    • Butler, J.1    Spielberg, S.P.2    Schulman, J.D.3
  • 20
    • 0020345697 scopus 로고
    • Buffers of constant ionic strength for studying pH-dependent processes
    • (Purich, D. L., Ed.), Academic Press, New York
    • Ellis, K. J., and Morrison, J. F. (1982) Buffers of constant ionic strength for studying pH-dependent processes, in Enzyme Kinetics and Mechanism (Purich, D. L., Ed.) pp 405-427, Academic Press, New York.
    • (1982) Enzyme Kinetics and Mechanism
    • Ellis, K.J.1    Morrison, J.F.2
  • 21
    • 0342862068 scopus 로고
    • Solvent deuterium isotope effects on acid-base equilibria
    • Salomaa, P., Schaleger, L. L., and Long, F. A. (1964) Solvent deuterium isotope effects on acid-base equilibria, J. Am. Chem. Soc. 86, 1-7.
    • (1964) J. Am. Chem. Soc. , vol.86 , pp. 1-7
    • Salomaa, P.1    Schaleger, L.L.2    Long, F.A.3
  • 22
    • 0020346954 scopus 로고
    • Solvent isotope effects on enzyme systems
    • Schowen, B. K., and Schowen, R. L. (1982) Solvent isotope effects on enzyme systems, Methods Enzymol. 87, 551-606.
    • (1982) Methods Enzymol. , vol.87 , pp. 551-606
    • Schowen, B.K.1    Schowen, R.L.2
  • 23
    • 0023084955 scopus 로고
    • Determination of low-molecular-weight thiols using monobromobimane fluorescent labeling and high-performance liquid chromatography
    • Fahey, R. C., and Newton, G. L. (1987) Determination of low-molecular-weight thiols using monobromobimane fluorescent labeling and high-performance liquid chromatography, Methods Enzymol. 143, 85-96.
    • (1987) Methods Enzymol. , vol.143 , pp. 85-96
    • Fahey, R.C.1    Newton, G.L.2
  • 24
    • 0022272493 scopus 로고
    • Determination of glutathione and glutathione disulfide in biological samples
    • Anderson, M. E. (1985) Determination of glutathione and glutathione disulfide in biological samples, Methods Enzymol. 113, 548-555.
    • (1985) Methods Enzymol. , vol.113 , pp. 548-555
    • Anderson, M.E.1
  • 26
    • 0344914133 scopus 로고
    • Permeability and transport
    • (Gerhardt, P., Murray, R. G. E., Costilow, R. N., Nester, E. W., Wood, W. A., Krieg, N. R., and Phillips, G. B., Eds.), American Society for Microbiology, Washington, DC
    • Marquis, R. E. (1981) Permeability and transport, in Manual of Methods for General Bacteriology (Gerhardt, P., Murray, R. G. E., Costilow, R. N., Nester, E. W., Wood, W. A., Krieg, N. R., and Phillips, G. B., Eds.) pp 393-404, American Society for Microbiology, Washington, DC.
    • (1981) Manual of Methods for General Bacteriology , pp. 393-404
    • Marquis, R.E.1
  • 27
    • 0343567762 scopus 로고
    • Diluents and biomass measurement
    • (Gerhardt, P., Murray, R. G. E., Costilow, R. N., Nester, E. W., Wood, W. A., Krieg, N. R., and Phillips, G. B., Eds.), American Society for Microbiology, Washington, DC
    • Gerhardt, P. (1981) Diluents and biomass measurement, in Manual of Methods for General Bacteriology (Gerhardt, P., Murray, R. G. E., Costilow, R. N., Nester, E. W., Wood, W. A., Krieg, N. R., and Phillips, G. B., Eds.) pp 504-507, American Society for Microbiology, Washington, DC.
    • (1981) Manual of Methods for General Bacteriology , pp. 504-507
    • Gerhardt, P.1
  • 28
    • 33847087446 scopus 로고
    • Rate constants and equilibrium constants for thiol-disulfide interchange reactions involving oxidized glutathione
    • Szajewski, R. P., and Whitesides, G. M. (1980) Rate constants and equilibrium constants for thiol-disulfide interchange reactions involving oxidized glutathione, J. Am. Chem. Soc. 102, 2011-2026.
    • (1980) J. Am. Chem. Soc. , vol.102 , pp. 2011-2026
    • Szajewski, R.P.1    Whitesides, G.M.2
  • 30
    • 0000444748 scopus 로고
    • Equilibrium deuterium isotope effects on the ionization of thiol acids
    • Jencks, W. P., and Salveson, K. (1971) Equilibrium deuterium isotope effects on the ionization of thiol acids, J. Am. Chem. Soc. 95, 4433-4436.
    • (1971) J. Am. Chem. Soc. , vol.95 , pp. 4433-4436
    • Jencks, W.P.1    Salveson, K.2
  • 31
    • 0003192373 scopus 로고
    • Kinetics of thiol-disulfide exchange
    • Fava, A., Iliceto, A., and Camera, E. (1957) Kinetics of thiol-disulfide exchange, J. Am. Chem. Soc. 79, 833-838.
    • (1957) J. Am. Chem. Soc. , vol.79 , pp. 833-838
    • Fava, A.1    Iliceto, A.2    Camera, E.3
  • 32
    • 0031021397 scopus 로고    scopus 로고
    • Structure, catalytic mechanism, and evolution of the glutathione transferases
    • Armstrong, R. N. (1997) Structure, catalytic mechanism, and evolution of the glutathione transferases, Chem. Res. Toxicol. 10, 2-18.
    • (1997) Chem. Res. Toxicol. , vol.10 , pp. 2-18
    • Armstrong, R.N.1
  • 33
    • 0000541891 scopus 로고
    • Contributions of thiolate "desolvation" to catalysis by glutathione S-transferase isozymes 1-1 and 2-2: Evidence from kinetic solvent isotope effects
    • Huskey, S. W., Huskey, W. P., and Lu, A. Y. H. (1991) Contributions of thiolate "desolvation" to catalysis by glutathione S-transferase isozymes 1-1 and 2-2: evidence from kinetic solvent isotope effects, J. Am. Chem. Soc. 113, 2283-2290.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 2283-2290
    • Huskey, S.W.1    Huskey, W.P.2    Lu, A.Y.H.3
  • 34
    • 0002018792 scopus 로고
    • Solvent isotope effects on enzymic reactions
    • (Cleland, W. W., O'Leary, M. H., and Northrop, D., Eds.), University Park Press, Baltimore, MD
    • Schowen, R. L. (1977) Solvent isotope effects on enzymic reactions, in Isotope effects on enzyme-catalyzed reactions (Cleland, W. W., O'Leary, M. H., and Northrop, D., Eds.) pp 64-99, University Park Press, Baltimore, MD.
    • (1977) Isotope Effects on Enzyme-catalyzed Reactions , pp. 64-99
    • Schowen, R.L.1
  • 35
    • 0001494424 scopus 로고
    • Structure-reactivity correlations for the thiol-disulfide interchange reaction
    • Wilson, J. M., Bayer, R. J., and Hupe, D. J. (1977) Structure-reactivity correlations for the thiol-disulfide interchange reaction. J. Am. Chem. Soc. 99, 7922-7926.
    • (1977) J. Am. Chem. Soc. , vol.99 , pp. 7922-7926
    • Wilson, J.M.1    Bayer, R.J.2    Hupe, D.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.