메뉴 건너뛰기




Volumn 115, Issue 3, 1998, Pages 201-213

Redox cycling of polycyclic aromatic hydrocarbon o-quinones: Metal ion-catalyzed oxidation of catechols bypasses inhibition by superoxide dismutase

Author keywords

[No Author keywords available]

Indexed keywords

BENZO[A]PYRENE DERIVATIVE; CARBONYL REDUCTASE; CATECHOL DERIVATIVE; CHRYSENE DERIVATIVE; COPPER ION; CYTOCHROME C; FERRIC ION; METAL ION; OXIDOREDUCTASE; PHENANTHRENE DERIVATIVE; POLYCYCLIC AROMATIC HYDROCARBON; QUINONE DERIVATIVE; SUPEROXIDE DISMUTASE;

EID: 0032476142     PISSN: 00092797     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0009-2797(98)00070-2     Document Type: Article
Times cited : (26)

References (38)
  • 1
    • 0024465355 scopus 로고
    • Redox and addition chemistry of quinoid compounds and its biological implications
    • Brunmark A., Cadenas E. Redox and addition chemistry of quinoid compounds and its biological implications. Free Radic. Biol. Med. 7:1989;435-477.
    • (1989) Free Radic. Biol. Med. , vol.7 , pp. 435-477
    • Brunmark, A.1    Cadenas, E.2
  • 2
    • 0026040838 scopus 로고
    • Molecular mechanisms of quinone cytotoxicity
    • O'Brien P.J. Molecular mechanisms of quinone cytotoxicity. Chem.-Biol. Interact. 80:1991;1-41.
    • (1991) Chem.-Biol. Interact. , vol.80 , pp. 1-41
    • O'Brien, P.J.1
  • 4
    • 0025070274 scopus 로고
    • Dual effects of superoxide dismutase on the autoxidation of 1,4-naphthohydroquinone
    • Ishii T., Fridovich I. Dual effects of superoxide dismutase on the autoxidation of 1,4-naphthohydroquinone. Free Radic. Biol. Med. 8:1990;21-24.
    • (1990) Free Radic. Biol. Med. , vol.8 , pp. 21-24
    • Ishii, T.1    Fridovich, I.2
  • 5
    • 0014410114 scopus 로고
    • The reduction of cytochrome c by milk xanthine oxidase
    • McCord J.M., Fridovich I. The reduction of cytochrome c by milk xanthine oxidase. J. Biol. Chem. 243:1968;5753-5760.
    • (1968) J. Biol. Chem. , vol.243 , pp. 5753-5760
    • McCord, J.M.1    Fridovich, I.2
  • 6
    • 0025101590 scopus 로고
    • Effect of superoxide dismutase on the autoxidation of substituted hydro- and semi-naphthoquinones
    • Ollinger K., Buffinton G.D., Ernster L., Cadenas E. Effect of superoxide dismutase on the autoxidation of substituted hydro- and semi-naphthoquinones. Chem.-Biol. Interact. 73:1990;53-76.
    • (1990) Chem.-Biol. Interact. , vol.73 , pp. 53-76
    • Ollinger, K.1    Buffinton, G.D.2    Ernster, L.3    Cadenas, E.4
  • 7
    • 0024854643 scopus 로고
    • 3+-induced neurotoxicity of dopamine: Prevention of quinone-derived oxygen toxicity by DT diaphorase and superoxide dismutase
    • 3+-induced neurotoxicity of dopamine: prevention of quinone-derived oxygen toxicity by DT diaphorase and superoxide dismutase. Chem.-Biol. Interact. 72:1989;309-324.
    • (1989) Chem.-Biol. Interact. , vol.72 , pp. 309-324
    • Segura-Aguilar, J.1    Lind, C.2
  • 8
    • 0028016068 scopus 로고
    • Superoxide dismutase and catalase prevent the formation of reactive oxygen species during reduction of cyclized dopa ortho-quinone by DT-diaphorase
    • Baez S., Linderson Y., Segura-Aguilar J. Superoxide dismutase and catalase prevent the formation of reactive oxygen species during reduction of cyclized dopa ortho-quinone by DT-diaphorase. Chem.-Biol. Interact. 93:1994;103-116.
    • (1994) Chem.-Biol. Interact. , vol.93 , pp. 103-116
    • Baez, S.1    Linderson, Y.2    Segura-Aguilar, J.3
  • 9
    • 0026331348 scopus 로고
    • Polycyclic aromatic hydrocarbon quinone-mediated oxidation reduction cycling catalyzed by a human placental NADPH-linked carbonyl reductase
    • Jarabak J. Polycyclic aromatic hydrocarbon quinone-mediated oxidation reduction cycling catalyzed by a human placental NADPH-linked carbonyl reductase. Arch. Biochem. Biophys. 291:1991;334-338.
    • (1991) Arch. Biochem. Biophys. , vol.291 , pp. 334-338
    • Jarabak, J.1
  • 10
    • 0026623207 scopus 로고
    • Quinone reduction and redox cycling catalyzed by purified rat liver dihydrodiol/3α-hydroxysteroid dehydrogenase
    • Klein J., Post K., Seidel A., Frank H., Oesch F., Platt K.L. Quinone reduction and redox cycling catalyzed by purified rat liver dihydrodiol/3α-hydroxysteroid dehydrogenase. Biochem. Pharmacol. 44:1992;341-349.
    • (1992) Biochem. Pharmacol. , vol.44 , pp. 341-349
    • Klein, J.1    Post, K.2    Seidel, A.3    Frank, H.4    Oesch, F.5    Platt, K.L.6
  • 11
    • 0027207716 scopus 로고
    • Studies on three reductases which have polycyclic aromatic hydrocarbon quinones as substrates
    • Jarabak J., Harvey R.G. Studies on three reductases which have polycyclic aromatic hydrocarbon quinones as substrates. Arch. Biochem. Biophys. 303:1993;394-401.
    • (1993) Arch. Biochem. Biophys. , vol.303 , pp. 394-401
    • Jarabak, J.1    Harvey, R.G.2
  • 12
    • 0030039912 scopus 로고    scopus 로고
    • Polycyclic aromatic hydrocarbon quinone-mediated oxidation reduction cycling catalyzed by a human placental 17β-hydroxysteroid dehydrogenase
    • Jarabak R., Harvey R.G., Jarabak J. Polycyclic aromatic hydrocarbon quinone-mediated oxidation reduction cycling catalyzed by a human placental 17β-hydroxysteroid dehydrogenase. Arch. Biochem. Biophys. 327:1996;174-180.
    • (1996) Arch. Biochem. Biophys. , vol.327 , pp. 174-180
    • Jarabak, R.1    Harvey, R.G.2    Jarabak, J.3
  • 13
    • 0031105666 scopus 로고    scopus 로고
    • Redox cycling of polycyclic aromatic hydrocarbon o-quinones: Reversal of superoxide dismutase inhibition by ascorbate
    • Jarabak R., Harvey R.G., Jarabak J. Redox cycling of polycyclic aromatic hydrocarbon o-quinones: reversal of superoxide dismutase inhibition by ascorbate. Arch. Biochem. Biophys. 339:1997;92-98.
    • (1997) Arch. Biochem. Biophys. , vol.339 , pp. 92-98
    • Jarabak, R.1    Harvey, R.G.2    Jarabak, J.3
  • 14
    • 0000894531 scopus 로고
    • Metal-catalyzed oxidation of 3,5-di-t-butyl pyrocatechol, and its significance in the mechanism of pyrocatechase action
    • Grinstead R.R. Metal-catalyzed oxidation of 3,5-di-t-butyl pyrocatechol, and its significance in the mechanism of pyrocatechase action. Biochemistry. 3:1964;1308-1314.
    • (1964) Biochemistry , vol.3 , pp. 1308-1314
    • Grinstead, R.R.1
  • 15
    • 0023514631 scopus 로고
    • Interactions between metals, ligands, and oxygen in the autoxidation of 6-hydroxydopamine: Mechanisms by which metal chelation enhances inhibition by superoxide dismutase
    • Bandy B., Davison A.J. Interactions between metals, ligands, and oxygen in the autoxidation of 6-hydroxydopamine: mechanisms by which metal chelation enhances inhibition by superoxide dismutase. Arch. Biochem. Biophys. 259:1987;305-315.
    • (1987) Arch. Biochem. Biophys. , vol.259 , pp. 305-315
    • Bandy, B.1    Davison, A.J.2
  • 16
    • 0027259457 scopus 로고
    • Oxidation of hydroquinone by copper: Chemical mechanism and biological effects
    • Li Y., Trush M.A. Oxidation of hydroquinone by copper: chemical mechanism and biological effects. Arch. Biochem. Biophys. 300:1993;346-355.
    • (1993) Arch. Biochem. Biophys. , vol.300 , pp. 346-355
    • Li, Y.1    Trush, M.A.2
  • 17
    • 0029913018 scopus 로고    scopus 로고
    • Effects of metals, ligands, and antioxidants on the reaction of oxygen with 1,2,4-benzenetriol
    • Zhang L., Bandy B., Davison A.J. Effects of metals, ligands, and antioxidants on the reaction of oxygen with 1,2,4-benzenetriol. Free Radic. Biol. Med. 20:1996;495-505.
    • (1996) Free Radic. Biol. Med. , vol.20 , pp. 495-505
    • Zhang, L.1    Bandy, B.2    Davison, A.J.3
  • 18
    • 0016849209 scopus 로고
    • 'K-Region' oxides and related metabolites of carcinogenic aromatic hydrocarbons
    • Harvey R.G., Goh S.H., Cortez C. 'K-Region' oxides and related metabolites of carcinogenic aromatic hydrocarbons. J. Am. Chem. Soc. 97:1975;3468-3479.
    • (1975) J. Am. Chem. Soc. , vol.97 , pp. 3468-3479
    • Harvey, R.G.1    Goh, S.H.2    Cortez, C.3
  • 19
    • 0016905198 scopus 로고
    • Synthesis of hydroquinone diacetates from polycyclic aromatic quinones
    • H. Cho, R.G. Harvey, Synthesis of hydroquinone diacetates from polycyclic aromatic quinones, J. Chem. Soc. Perkin Trans., I (1976) 836-839.
    • (1976) J. Chem. Soc. Perkin Trans. , vol.1 , pp. 836-839
    • Cho, H.1    Harvey, R.G.2
  • 20
    • 0023899965 scopus 로고
    • In the absence of catalytic metals ascorbate does not autoxidize at pH 7: Ascorbate as a test for catalytic metals
    • Buettner G.R. In the absence of catalytic metals ascorbate does not autoxidize at pH 7: Ascorbate as a test for catalytic metals. J. Biochem. Biophys. Methods. 16:1988;27-40.
    • (1988) J. Biochem. Biophys. Methods , vol.16 , pp. 27-40
    • Buettner, G.R.1
  • 21
    • 0017857353 scopus 로고
    • Isolation of two proteins with 9-ketoprostaglandin reductase and NADP-linked 15-hydroxyprostaglandin dehydrogenase activities and study of their inhibition
    • Lin Y.-M., Jarabak J. Isolation of two proteins with 9-ketoprostaglandin reductase and NADP-linked 15-hydroxyprostaglandin dehydrogenase activities and study of their inhibition. Biochem. Biophys. Res. Commun. 81:1978;1227-1234.
    • (1978) Biochem. Biophys. Res. Commun. , vol.81 , pp. 1227-1234
    • Lin, Y.-M.1    Jarabak, J.2
  • 22
    • 0000797162 scopus 로고
    • Soluble 17β-hydroxysteroid dehydrogenase of human placenta
    • Jarabak J. Soluble 17β-hydroxysteroid dehydrogenase of human placenta. Methods Enzymol. 15:1969;746-752.
    • (1969) Methods Enzymol. , vol.15 , pp. 746-752
    • Jarabak, J.1
  • 23
    • 0014691242 scopus 로고
    • Superoxide dismutase: An enzymatic function for erythrocuprein (hemocuprein)
    • McCord J.M., Fridovich I. Superoxide dismutase: an enzymatic function for erythrocuprein (hemocuprein). J. Biol. Chem. 244:1969;6049-6055.
    • (1969) J. Biol. Chem. , vol.244 , pp. 6049-6055
    • McCord, J.M.1    Fridovich, I.2
  • 24
    • 29744466425 scopus 로고
    • Determination of serum proteins by means of the biuret reaction
    • Gornall A.G., Bardawill C.J., David M.M. Determination of serum proteins by means of the biuret reaction. J. Biol. Chem. 177:1949;751-756.
    • (1949) J. Biol. Chem. , vol.177 , pp. 751-756
    • Gornall, A.G.1    Bardawill, C.J.2    David, M.M.3
  • 25
    • 4243457224 scopus 로고
    • Spectrophotometric determination of hydrogen peroxide and organic hydroperoxides at low concentrations in aqueous solution
    • Frew J.E., Jones P., Scholes G. Spectrophotometric determination of hydrogen peroxide and organic hydroperoxides at low concentrations in aqueous solution. Anal. Chim. Acta. 155:1983;139-150.
    • (1983) Anal. Chim. Acta , vol.155 , pp. 139-150
    • Frew, J.E.1    Jones, P.2    Scholes, G.3
  • 26
    • 0010401657 scopus 로고
    • The chromatographic behavior of cytochrome c on cation exchangers
    • Margoliash E. The chromatographic behavior of cytochrome c on cation exchangers. Biochem. J. 56:1954;535-543.
    • (1954) Biochem. J. , vol.56 , pp. 535-543
    • Margoliash, E.1
  • 27
    • 0025095542 scopus 로고
    • Transition metals as catalysts of 'autoxidation' reactions
    • Miller D.M., Buettner G.R., Aust S.D. Transition metals as catalysts of 'autoxidation' reactions. Free Radic. Biol. Med. 8:1990;95-108.
    • (1990) Free Radic. Biol. Med. , vol.8 , pp. 95-108
    • Miller, D.M.1    Buettner, G.R.2    Aust, S.D.3
  • 28
    • 0028214731 scopus 로고
    • Reactive oxygen-dependent DNA damage resulting from the oxidation of phenolic compounds by a copper-redox cycle mechanism
    • Li Y., Trush M.A. Reactive oxygen-dependent DNA damage resulting from the oxidation of phenolic compounds by a copper-redox cycle mechanism. Cancer Res. (Suppl.). 54:1994;1895s-1898s.
    • (1994) Cancer Res. (Suppl.) , vol.54
    • Li, Y.1    Trush, M.A.2
  • 29
    • 0014369841 scopus 로고
    • Catalytic effects of metal chelate compounds
    • Martell A.E. Catalytic effects of metal chelate compounds. Pure Appl. Chem. 17:1968;129-178.
    • (1968) Pure Appl. Chem. , vol.17 , pp. 129-178
    • Martell, A.E.1
  • 30
    • 0002810701 scopus 로고
    • Copper (II)-catalyzed oxidation of catechol by oxygen in aqueous solution
    • Balla J., Kiss T., Jameson R.F. Copper (II)-catalyzed oxidation of catechol by oxygen in aqueous solution. Inorg. Chem. 31:1992;58-62.
    • (1992) Inorg. Chem. , vol.31 , pp. 58-62
    • Balla, J.1    Kiss, T.2    Jameson, R.F.3
  • 31
    • 50549169947 scopus 로고
    • DT diaphorase: I. Purification from the soluble fraction of rat-liver cytosol, and properties
    • Ernster L., Danielson L., Ljunggren M. DT diaphorase: I. Purification from the soluble fraction of rat-liver cytosol, and properties. Biochem. Biophys. Acta. 58:1962;171-188.
    • (1962) Biochem. Biophys. Acta , vol.58 , pp. 171-188
    • Ernster, L.1    Danielson, L.2    Ljunggren, M.3
  • 32
    • 0014014281 scopus 로고
    • One-electron-transfer reactions in biochemical systems: I. Kinetic analysis of the oxidation-reduction equilibrium between quinol-quinone and ferro-ferricytochrome c
    • Yamazaki I., Ohnishi T. One-electron-transfer reactions in biochemical systems: I. Kinetic analysis of the oxidation-reduction equilibrium between quinol-quinone and ferro-ferricytochrome c. Biochem. Biophys. Acta. 112:1966;469-481.
    • (1966) Biochem. Biophys. Acta , vol.112 , pp. 469-481
    • Yamazaki, I.1    Ohnishi, T.2
  • 33
    • 0017313950 scopus 로고
    • Kinetics of reduction of horse-heart ferricytochrome c by catechol
    • Toppen D.L. Kinetics of reduction of horse-heart ferricytochrome c by catechol. J. Am. Chem. Soc. 98:1976;4023-4024.
    • (1976) J. Am. Chem. Soc. , vol.98 , pp. 4023-4024
    • Toppen, D.L.1
  • 34
    • 0018792314 scopus 로고
    • A mechanism for the reduction of cytochromes by quinols in solution and its relevance to biological electron transfer reactions
    • Rich P.R., Bendall D.S. A mechanism for the reduction of cytochromes by quinols in solution and its relevance to biological electron transfer reactions. FEBS Lett. 105:1979;189-194.
    • (1979) FEBS Lett. , vol.105 , pp. 189-194
    • Rich, P.R.1    Bendall, D.S.2
  • 35
    • 0019316012 scopus 로고
    • The kinetics and thermodynamics of the reduction of cytochrome c by substituted p-benzoquinols in solution
    • Rich P.R., Bendall D.S. The kinetics and thermodynamics of the reduction of cytochrome c by substituted p-benzoquinols in solution. Biochem. Biophys. Acta. 592:1980;506-518.
    • (1980) Biochem. Biophys. Acta , vol.592 , pp. 506-518
    • Rich, P.R.1    Bendall, D.S.2
  • 36
    • 0020110270 scopus 로고
    • Kinetic studies on the reduction of cytochrome c: Reaction with dihydroxy conjugated compounds (catechols and quinols)
    • Saleem M.M.M., Wilson M.T. Kinetic studies on the reduction of cytochrome c: reaction with dihydroxy conjugated compounds (catechols and quinols). Biochem. J. 201:1982;433-444.
    • (1982) Biochem. J. , vol.201 , pp. 433-444
    • Saleem, M.M.M.1    Wilson, M.T.2
  • 37
    • 0027296545 scopus 로고
    • DNA damage resulting from the oxidation of hydroquinone by copper: Role for a Cu (II)/Cu (I) redox cycle and reactive oxygen generation
    • Li Y., Trush M.A. DNA damage resulting from the oxidation of hydroquinone by copper: role for a Cu (II)/Cu (I) redox cycle and reactive oxygen generation. Carcinogenesis. 14:1993;1303-1311.
    • (1993) Carcinogenesis , vol.14 , pp. 1303-1311
    • Li, Y.1    Trush, M.A.2
  • 38
    • 0027310474 scopus 로고
    • Benzene metabolite, 1,2,4-benzenetriol, induces micronuclei and oxidative damage in human lymphocytes and HL60 cells
    • Zhang L., Robertson M.L., Kolachana P., Davison A.J., Smith M.T. Benzene metabolite, 1,2,4-benzenetriol, induces micronuclei and oxidative damage in human lymphocytes and HL60 cells. Environ. Mol. Mutagen. 21:1993;339-348.
    • (1993) Environ. Mol. Mutagen. , vol.21 , pp. 339-348
    • Zhang, L.1    Robertson, M.L.2    Kolachana, P.3    Davison, A.J.4    Smith, M.T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.