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Volumn 16, Issue 8, 1997, Pages 441-448

Primary aromatic amines: Their N-oxidative bioactivation

Author keywords

Enzymology; N oxygenation; Primary arylamines; Toxicity

Indexed keywords

AROMATIC AMINE; CHLORIDE PEROXIDASE; CYTOCHROME P450; FREE RADICAL; HEMOGLOBIN; HORSERADISH PEROXIDASE; LACTOPEROXIDASE; MYELOPEROXIDASE; NITROGEN DERIVATIVE; PEROXIDASE; PROSTAGLANDIN SYNTHASE; QUERCETIN; UNSPECIFIC MONOOXYGENASE;

EID: 0030854339     PISSN: 09603271     EISSN: None     Source Type: Journal    
DOI: 10.1177/096032719701600805     Document Type: Article
Times cited : (26)

References (81)
  • 1
    • 0020018460 scopus 로고
    • Biological oxidation of nitrogen in organic compounds and disposition of N-oxidized products
    • Hlavica P. Biological oxidation of nitrogen in organic compounds and disposition of N-oxidized products. CRC Crit Rev Biochem 1982; 12: 39-101.
    • (1982) CRC Crit Rev Biochem , vol.12 , pp. 39-101
    • Hlavica, P.1
  • 3
    • 0005377890 scopus 로고
    • The role of N-oxidation by leucocytes in drug-induced agranulocytosis and other drug hypersensitivity reactions
    • Hlavica P and Damani LA (eds.). Chapman and Hall, London
    • Uetrecht J. The role of N-oxidation by leucocytes in drug-induced agranulocytosis and other drug hypersensitivity reactions. In: Hlavica P and Damani LA (eds.). N-Oxidation of Drugs. Biochemistry, Pharmacology, Toxicology, Chapman and Hall, London, 1991, pp435-453.
    • (1991) N-Oxidation of Drugs. Biochemistry, Pharmacology, Toxicology , pp. 435-453
    • Uetrecht, J.1
  • 4
    • 0016287157 scopus 로고
    • Carcinogenesis by aromatic amines
    • Kriek E. Carcinogenesis by aromatic amines. Biochim Biophys Acta 1974; 355: 177-203.
    • (1974) Biochim Biophys Acta , vol.355 , pp. 177-203
    • Kriek, E.1
  • 5
    • 0027446505 scopus 로고
    • The P-450 superfamily: Update of new sequences, gene mapping, accession numbers, early trivial names of enzymes, and nomenclature
    • Nelson DR et al. The P-450 superfamily: update of new sequences, gene mapping, accession numbers, early trivial names of enzymes, and nomenclature. DNA Cell Biol 1993; 12: 1-51.
    • (1993) DNA Cell Biol , vol.12 , pp. 1-51
    • Nelson, D.R.1
  • 6
    • 0014429295 scopus 로고
    • Role of hemoprotein P-450 in fatty acid ω-hydroxylation in a soluble enzyme system from liver microsomes
    • Lu AYH, Coon MJ. Role of hemoprotein P-450 in fatty acid ω-hydroxylation in a soluble enzyme system from liver microsomes. J Biol Chem 1968; 243; 1331-1332.
    • (1968) J Biol Chem , vol.243 , pp. 1331-1332
    • Lu, A.Y.H.1    Coon, M.J.2
  • 7
    • 0021647933 scopus 로고
    • 5 on cytochrome P-450-catalyzed reactions
    • 5 on cytochrome P-450-catalyzed reactions. Drug Metab Dispos 1984; 12: 358-364.
    • (1984) Drug Metab Dispos , vol.12 , pp. 358-364
    • Morgan, E.T.1    Coon, M.J.2
  • 8
    • 0014751753 scopus 로고
    • N-Oxygenation of arylamines in microsomes prepared from corpora lutea of the cycle and other tissues of the pig
    • Heinze E, Hlavica P, Kiese M, Lipowsky G. N-Oxygenation of arylamines in microsomes prepared from corpora lutea of the cycle and other tissues of the pig. Biochem Pharmacol 1970; 19: 641-649.
    • (1970) Biochem Pharmacol , vol.19 , pp. 641-649
    • Heinze, E.1    Hlavica, P.2    Kiese, M.3    Lipowsky, G.4
  • 9
    • 0016218171 scopus 로고
    • Studies on the mechanism of hepatic microsomal N-oxide formation
    • Hlavica P, Kehl M. Studies on the mechanism of hepatic microsomal N-oxide formation. Hoppe-Seyler's Z Physiol Chem 1974; 355: 1508-1514.
    • (1974) Hoppe-Seyler's Z Physiol Chem , vol.355 , pp. 1508-1514
    • Hlavica, P.1    Kehl, M.2
  • 10
    • 0015090320 scopus 로고
    • N-Hydroxylation
    • Uehleke H. N-Hydroxylation. Xenobiotica 1971; 1: 327-338.
    • (1971) Xenobiotica , vol.1 , pp. 327-338
    • Uehleke, H.1
  • 11
    • 0021104211 scopus 로고
    • Comparative studies on the cumene hydroperoxide- and NADPH-supported N-oxidation of 4-chloroaniline by cytochrome P-450
    • Hlavica P, Golly I, Mietaschk J. Comparative studies on the cumene hydroperoxide- and NADPH-supported N-oxidation of 4-chloroaniline by cytochrome P-450. Biochem J 1983; 212: 539-547.
    • (1983) Biochem J , vol.212 , pp. 539-547
    • Hlavica, P.1    Golly, I.2    Mietaschk, J.3
  • 12
    • 0014532075 scopus 로고
    • N-Oxygenation of N-alkyl- and N,N-dialkylanilines by rabbit liver microsomes
    • Hlavica P, Kiese M. N-Oxygenation of N-alkyl- and N,N-dialkylanilines by rabbit liver microsomes. Biochem Pharmacol 1969; 18: 1501-1509.
    • (1969) Biochem Pharmacol , vol.18 , pp. 1501-1509
    • Hlavica, P.1    Kiese, M.2
  • 13
    • 0027273411 scopus 로고
    • Qualitative and quantitative influences of ortho chlorine substituents on the microsomal metabolism of 4-toludines
    • Tyrakowska B, Boeren S, Geurtsen B, Rietjens IMCM. Qualitative and quantitative influences of ortho chlorine substituents on the microsomal metabolism of 4-toludines. Drug Metab Dispos 1993; 21: 508-519.
    • (1993) Drug Metab Dispos , vol.21 , pp. 508-519
    • Tyrakowska, B.1    Boeren, S.2    Geurtsen, B.3    Rietjens, I.M.C.M.4
  • 14
    • 0015350553 scopus 로고
    • Mikrosomale Oxydation am Stickstoffatom aromatischer Amine
    • Schmidt HL, Kexel H, Weber N. Mikrosomale Oxydation am Stickstoffatom aromatischer Amine. Biochem Pharmacol 1972; 21: 1641-1648.
    • (1972) Biochem Pharmacol , vol.21 , pp. 1641-1648
    • Schmidt, H.L.1    Kexel, H.2    Weber, N.3
  • 15
    • 0021361235 scopus 로고
    • Metabolism of procainamide to a hydroxylamine by rat and human hepatic microsomes
    • Uetrecht JP, Sweetman BJ, Woosley RL, Oates JA. Metabolism of procainamide to a hydroxylamine by rat and human hepatic microsomes. Drug Metab Dispos 1984; 12: 77-81.
    • (1984) Drug Metab Dispos , vol.12 , pp. 77-81
    • Uetrecht, J.P.1    Sweetman, B.J.2    Woosley, R.L.3    Oates, J.A.4
  • 16
    • 0023097220 scopus 로고
    • The formation of procainamide hydroxylamine by rat and human liver microsomes
    • Budinsky RA et al. The formation of procainamide hydroxylamine by rat and human liver microsomes. Drug Metab Dispos 1987; 15; 37-43.
    • (1987) Drug Metab Dispos , vol.15 , pp. 37-43
    • Budinsky, R.A.1
  • 17
    • 0015928424 scopus 로고
    • N-Hydroxylation of 4,4′-diaminodiphenylsulphone (dapsone) by liver microsomes, and in dogs and humans
    • Uehleke H, Tabarelli S. N-Hydroxylation of 4,4′-diaminodiphenylsulphone (dapsone) by liver microsomes, and in dogs and humans. NaunynSchmiedeberg's Arch Pharmacol 1973; 278; 55-68.
    • (1973) NaunynSchmiedeberg's Arch Pharmacol , vol.278 , pp. 55-68
    • Uehleke, H.1    Tabarelli, S.2
  • 18
    • 84931117183 scopus 로고
    • Der Einfluß von Metyrapon auf verschiedene Typen von mikrosomalen N-Oxidationen
    • Uehleke H et al. Der Einfluß von Metyrapon auf verschiedene Typen von mikrosomalen N-Oxidationen. Hoppe-Seyler's Z Physiol Chem 1971; 352: 403-411.
    • (1971) Hoppe-Seyler's Z Physiol Chem , vol.352 , pp. 403-411
    • Uehleke, H.1
  • 19
    • 0014184960 scopus 로고
    • Hydroxylamino- und Nitrosobiphenyl: Biologische Oxydationsprodukte von 4-Aminobiphenyl und Zwischenprodukte der Reduktion von 4-Nitrobiphenyl
    • Uehleke H, Nestel K. Hydroxylamino- und Nitrosobiphenyl: Biologische Oxydationsprodukte von 4-Aminobiphenyl und Zwischenprodukte der Reduktion von 4-Nitrobiphenyl. Naunyn-Schmiedeberg's Arch Pharmak exp Path 1967; 257: 151-171.
    • (1967) Naunyn-Schmiedeberg's Arch Pharmak Exp Path , vol.257 , pp. 151-171
    • Uehleke, H.1    Nestel, K.2
  • 20
    • 0022979115 scopus 로고
    • Induction of a high spin form of microsomal cytochrome P-448 in rat liver by 4-aminoazobenzene derivatives
    • Degawa M, Kojima M, Sato Y, Hashimoto Y. Induction of a high spin form of microsomal cytochrome P-448 in rat liver by 4-aminoazobenzene derivatives. Biochem Pharmacol 1986; 35: 3565-3570.
    • (1986) Biochem Pharmacol , vol.35 , pp. 3565-3570
    • Degawa, M.1    Kojima, M.2    Sato, Y.3    Hashimoto, Y.4
  • 21
    • 0028986887 scopus 로고
    • 4-Hydroxylation of sulfamethoxazole by cytochrome P-450 of the cytochrome P-450 2C subfamily and reduction of sulfamethoxazole hydroxylamine in human and rat hepatic microsomes
    • 4-Hydroxylation of sulfamethoxazole by cytochrome P-450 of the cytochrome P-450 2C subfamily and reduction of sulfamethoxazole hydroxylamine in human and rat hepatic microsomes. Drug Metab Dispos 1995; 23: 406-414.
    • (1995) Drug Metab Dispos , vol.23 , pp. 406-414
    • Cribb, A.E.1    Spielberg, S.P.2    Griffin, G.P.3
  • 22
  • 23
    • 0027980609 scopus 로고
    • Evidence that the biotransformation of dapsone and monoacetyldapsone to their respective hydroxylamine metabolites in rat liver microsomes is mediated by cytochrome P-450 2C6/2C11 and 3A1
    • Vage C, Svensson CK. Evidence that the biotransformation of dapsone and monoacetyldapsone to their respective hydroxylamine metabolites in rat liver microsomes is mediated by cytochrome P-450 2C6/2C11 and 3A1. Drug Metab Dispos 1994; 22: 572-577.
    • (1994) Drug Metab Dispos , vol.22 , pp. 572-577
    • Vage, C.1    Svensson, C.K.2
  • 24
    • 0019990422 scopus 로고
    • Cytochrome P-450- and flavin-containing monooxygenase-catalyzed formation of the carcinogen N-hydroxy-2-aminofluorene and its covalent binding to nuclear DNA
    • Frederick CB et al. Cytochrome P-450- and flavin-containing monooxygenase-catalyzed formation of the carcinogen N-hydroxy-2-aminofluorene and its covalent binding to nuclear DNA. Cancer Res 1982; 42: 2671-2677.
    • (1982) Cancer Res , vol.42 , pp. 2671-2677
    • Frederick, C.B.1
  • 25
    • 0020597193 scopus 로고
    • A high-spin form of cytochrome P-450 highly purified from polychlorinated biphenyl-treated rats
    • Kamataki T et al. A high-spin form of cytochrome P-450 highly purified from polychlorinated biphenyl-treated rats. Mol Pharmacol 1983; 24: 146-155.
    • (1983) Mol Pharmacol , vol.24 , pp. 146-155
    • Kamataki, T.1
  • 26
    • 0022006601 scopus 로고
    • Metabolic oxidation of carcinogenic arylamines by rat, dog, and human hepatic microsomes and by purified flavin-containing and cytochrome P-450 monooxygenases
    • Hammons GJ et al. Metabolic oxidation of carcinogenic arylamines by rat, dog, and human hepatic microsomes and by purified flavin-containing and cytochrome P-450 monooxygenases. Cancer Res 1985; 45: 3578-3585.
    • (1985) Cancer Res , vol.45 , pp. 3578-3585
    • Hammons, G.J.1
  • 27
    • 0024343858 scopus 로고
    • PA (P-450 IA2), the phenacetin O-deethylase, is primarily responsible for the hepatic 3-methylation of caffeine and N-oxidation of carcinogenic arylamines
    • PA (P-450 IA2), the phenacetin O-deethylase, is primarily responsible for the hepatic 3-methylation of caffeine and N-oxidation of carcinogenic arylamines. Proc Natl Acad Sci (USA) 1989; 86: 7696-7700.
    • (1989) Proc Natl Acad Sci (USA) , vol.86 , pp. 7696-7700
    • Butler, M.A.1    Iwasaki, M.2    Guengerich, F.P.3    Kadlubar, F.F.4
  • 28
    • 0024568395 scopus 로고
    • Metabolic oxidation of the carcinogens 4-aminobiphenyl and 4,4′-methylene-bis (2-chloraniline) by human hepatic microsomes and by purified rat hepatic cytochrome P-450 monooxygenases
    • Butler MA, Guengerich FP, Kadlubar FF. Metabolic oxidation of the carcinogens 4-aminobiphenyl and 4,4′-methylene-bis (2-chloraniline) by human hepatic microsomes and by purified rat hepatic cytochrome P-450 monooxygenases. Cancer Res 1989; 49: 25-31.
    • (1989) Cancer Res , vol.49 , pp. 25-31
    • Butler, M.A.1    Guengerich, F.P.2    Kadlubar, F.F.3
  • 29
    • 0026540756 scopus 로고
    • Contributions of human liver cytochrome P-450 enzymes to the N-oxidation of 4,4′-methylene-bis (2-chloroaniline)
    • Yun Ch, Shimada T, Guengerich FP. Contributions of human liver cytochrome P-450 enzymes to the N-oxidation of 4,4′-methylene-bis (2-chloroaniline). Carcinogenesis 1992; 13: 217-222.
    • (1992) Carcinogenesis , vol.13 , pp. 217-222
    • Yun, Ch.1    Shimada, T.2    Guengerich, F.P.3
  • 30
    • 0017717638 scopus 로고
    • Inhibition of mixed-function oxidations by substrates forming reduced cytochrome P-450 metabolic-intermediate complexes
    • Franklin MR. Inhibition of mixed-function oxidations by substrates forming reduced cytochrome P-450 metabolic-intermediate complexes. Pharmac Ther A 1977; 2: 227-245.
    • (1977) Pharmac Ther A , vol.2 , pp. 227-245
    • Franklin, M.R.1
  • 31
    • 0026516593 scopus 로고
    • 2 (P-450 IIB4): Influence on heme liganding of arylamines
    • 2 (P-450 IIB4): influence on heme liganding of arylamines, Arch Biochem Biophys 1992; 292: 287-294.
    • (1992) Arch Biochem Biophys , vol.292 , pp. 287-294
    • Golly, I.1    Hlavica, P.2
  • 32
    • 0014943862 scopus 로고
    • Studies on the active site of mixed function oxidases in rabbit liver microsomes
    • Hlavica P. Studies on the active site of mixed function oxidases in rabbit liver microsomes. Biochem Biophys Res Commun 1970; 40: 212-217.
    • (1970) Biochem Biophys Res Commun , vol.40 , pp. 212-217
    • Hlavica, P.1
  • 33
    • 0017167499 scopus 로고
    • Comparative studies on the N-oxidation of aniline and N,N-dimethylaniline by rabbit liver microsomes
    • Hlavica P, Kehl M. Comparative studies on the N-oxidation of aniline and N,N-dimethylaniline by rabbit liver microsomes. Xenobiotica 1976; 6: 679-689.
    • (1976) Xenobiotica , vol.6 , pp. 679-689
    • Hlavica, P.1    Kehl, M.2
  • 34
    • 0022403842 scopus 로고
    • Chemical modification of cytochrome P-450 LM2 with N-acetylimidazole. Evidence for the functional involvement of tyrosyl residues
    • Jänig GR et al. Chemical modification of cytochrome P-450 LM2 with N-acetylimidazole. Evidence for the functional involvement of tyrosyl residues. Biomed Biochim Acta 1985; 44: 1071-1082.
    • (1985) Biomed Biochim Acta , vol.44 , pp. 1071-1082
    • Jänig, G.R.1
  • 35
    • 0026468125 scopus 로고
    • Modification of cytochrome P-450 1A2 enzymes by mechanism-based inactivator 2-ethynylnaphthalene and the photoaffinity label 4-azidobiphenyl
    • Yun CH et al. Modification of cytochrome P-450 1A2 enzymes by mechanism-based inactivator 2-ethynylnaphthalene and the photoaffinity label 4-azidobiphenyl. Biochemistry 1992; 31: 10556-10563.
    • (1992) Biochemistry , vol.31 , pp. 10556-10563
    • Yun, C.H.1
  • 36
    • 0017333194 scopus 로고
    • Nuclear magnetic reasonance studies of substratehemoprotein complexes in solution
    • Novak RF, Kapetanovic IM, Mieyal JJ. Nuclear magnetic reasonance studies of substratehemoprotein complexes in solution. Mol Pharmacol 1977; 13: 15-30.
    • (1977) Mol Pharmacol , vol.13 , pp. 15-30
    • Novak, R.F.1    Kapetanovic, I.M.2    Mieyal, J.J.3
  • 37
    • 0021383308 scopus 로고
    • 5 in the cytochrome P-450-dependent oxygenase system
    • 5 in the cytochrome P-450-dependent oxygenase system. Arch Biochem Biophys 1984; 228: 600-608.
    • (1984) Arch Biochem Biophys , vol.228 , pp. 600-608
    • Hlavica, P.1
  • 38
    • 0023228293 scopus 로고
    • 5-enriched rabbit liver microsomal fractions
    • 5-enriched rabbit liver microsomal fractions. Biochim Biophys Acta 1987; 913: 219-227.
    • (1987) Biochim Biophys Acta , vol.913 , pp. 219-227
    • Golly, I.1    Hlavica, P.2
  • 39
    • 0021343149 scopus 로고
    • The peroxidatic function of liver microsomal cytochrome P-450: Comparison of hydrogen peroxide and NADPH-catalyzed N-demethylation reactions
    • Estabrook RW et al. The peroxidatic function of liver microsomal cytochrome P-450: comparison of hydrogen peroxide and NADPH-catalyzed N-demethylation reactions. Xenobiotica 1984; 14: 87-104.
    • (1984) Xenobiotica , vol.14 , pp. 87-104
    • Estabrook, R.W.1
  • 40
    • 0020614531 scopus 로고
    • Hydroperoxide-dependent activation of p-phenetidine catalyzed by prostaglandin synthase and other peroxidases
    • Andersson B, Larsson R, Rahimtula A, Moldeus P. Hydroperoxide-dependent activation of p-phenetidine catalyzed by prostaglandin synthase and other peroxidases. Biochem Pharmacol 1983; 32: 1045-1050.
    • (1983) Biochem Pharmacol , vol.32 , pp. 1045-1050
    • Andersson, B.1    Larsson, R.2    Rahimtula, A.3    Moldeus, P.4
  • 41
    • 0028302414 scopus 로고
    • A nomenclature for the mammalian flavin-containing monooxygenase gene family based on amino acid sequence identities
    • Lawton MP et al. A nomenclature for the mammalian flavin-containing monooxygenase gene family based on amino acid sequence identities. Arch Biochem Biophys 1994; 308: 254-257.
    • (1994) Arch Biochem Biophys , vol.308 , pp. 254-257
    • Lawton, M.P.1
  • 42
    • 0027462628 scopus 로고
    • Recent studies on the structure and function of multisubstrate flavin-containing monooxygenases
    • Ziegler DM. Recent studies on the structure and function of multisubstrate flavin-containing monooxygenases. Annu Rev Pharmacol Toxicol 1993; 33: 179-199.
    • (1993) Annu Rev Pharmacol Toxicol , vol.33 , pp. 179-199
    • Ziegler, D.M.1
  • 43
    • 0017175198 scopus 로고
    • Mechanism of 2-naphthylamine oxidation catalysed by pig liver microsomes
    • Poulsen LL, Masters BSS, Ziegler DM. Mechanism of 2-naphthylamine oxidation catalysed by pig liver microsomes. Xenobiotica 1976; 6: 481-498.
    • (1976) Xenobiotica , vol.6 , pp. 481-498
    • Poulsen, L.L.1    Masters, B.S.S.2    Ziegler, D.M.3
  • 44
    • 0020579154 scopus 로고
    • The role of haemoglobin in the N-oxidation of 4-chloroaniline
    • Golly I, Hlavica P. The role of haemoglobin in the N-oxidation of 4-chloroaniline. Biochim Biophys Acta 1983; 760: 69-76.
    • (1983) Biochim Biophys Acta , vol.760 , pp. 69-76
    • Golly, I.1    Hlavica, P.2
  • 45
    • 0026619048 scopus 로고
    • Oxidative activation of 2-aminofluorene by human red blood cell cytosol
    • Duverger-van Bogaert M, Wiame D, Stecca C. Oxidative activation of 2-aminofluorene by human red blood cell cytosol. Biochem Pharmacol 1992; 44: 2422-2424.
    • (1992) Biochem Pharmacol , vol.44 , pp. 2422-2424
    • Duverger-van Bogaert, M.1    Wiame, D.2    Stecca, C.3
  • 46
    • 0021144952 scopus 로고
    • Peroxidase activity of oxyhaemoglobin in vitro
    • Lenk W, Sterzl H. Peroxidase activity of oxyhaemoglobin in vitro. Xenobiotica 1984; 14: 581-588.
    • (1984) Xenobiotica , vol.14 , pp. 581-588
    • Lenk, W.1    Sterzl, H.2
  • 47
    • 0343404604 scopus 로고
    • Multiple mechanisms of metabolic activation of aromatic amine carcinogens
    • Pryor WA (ed.). Academic Press, New York
    • O'Brien PJ. Multiple mechanisms of metabolic activation of aromatic amine carcinogens. In: Pryor WA (ed.). Free Radicals in Biology, Vol. VI, Academic Press, New York, 1984, pp 289-322.
    • (1984) Free Radicals in Biology , vol.6 , pp. 289-322
    • O'Brien, P.J.1
  • 48
    • 0002913418 scopus 로고
    • Comparison of the peroxidase activity of hemeproteins and cytochrome P-450
    • Oritz de Montellano PR (ed.). Plenum Press, New York
    • Marnett LJ, Weller P, Battista JR. Comparison of the peroxidase activity of hemeproteins and cytochrome P-450. In: Oritz de Montellano PR (ed.). Cytochrome P-450. Structure, Mechanism, and Biochemistry, Plenum Press, New York, 1986, pp29-76.
    • (1986) Cytochrome P-450. Structure, Mechanism, and Biochemistry , pp. 29-76
    • Marnett, L.J.1    Weller, P.2    Battista, J.R.3
  • 49
    • 0018847714 scopus 로고
    • Mechanisms of reaction of hemoproteins with oxygen and hydroperoxide in the oxidation of organic substrates
    • Castro CE. Mechanisms of reaction of hemoproteins with oxygen and hydroperoxide in the oxidation of organic substrates. Pharmac Ther 1980; 10: 171-189.
    • (1980) Pharmac Ther , vol.10 , pp. 171-189
    • Castro, C.E.1
  • 51
    • 0020632378 scopus 로고
    • Oxidation of p-aminophenol catalyzed by horseradish peroxidase and prostaglandin synthase
    • Josephy PD, Eling TE, Mason RP. Oxidation of p-aminophenol catalyzed by horseradish peroxidase and prostaglandin synthase. Mol Pharmacol 1983; 23: 461-466.
    • (1983) Mol Pharmacol , vol.23 , pp. 461-466
    • Josephy, P.D.1    Eling, T.E.2    Mason, R.P.3
  • 52
    • 0000777820 scopus 로고
    • The kinetics and stoichiometry of the transition from the primary to the secondary peroxidase peroxide complexes
    • Chance B. The kinetics and stoichiometry of the transition from the primary to the secondary peroxidase peroxide complexes. Arch Biochem Biophys 1952; 41: 416-424.
    • (1952) Arch Biochem Biophys , vol.41 , pp. 416-424
    • Chance, B.1
  • 53
    • 0026095346 scopus 로고
    • Reactive intermediates formed during the peroxidative oxidation of anisidine isomers
    • Thompson DC, Eling TE. Reactive intermediates formed during the peroxidative oxidation of anisidine isomers. Chem Res Toxicol 1991; 4: 474-481.
    • (1991) Chem Res Toxicol , vol.4 , pp. 474-481
    • Thompson, D.C.1    Eling, T.E.2
  • 54
    • 0021954154 scopus 로고
    • The oxidation of p-phenetidine by horseradish peroxidase and prostaglandin synthase and the fate of glutathione during such oxidations
    • Ross D et al. The oxidation of p-phenetidine by horseradish peroxidase and prostaglandin synthase and the fate of glutathione during such oxidations. Biochem Pharmacol 1985; 34: 343-351.
    • (1985) Biochem Pharmacol , vol.34 , pp. 343-351
    • Ross, D.1
  • 55
    • 0026672949 scopus 로고
    • The oxidation of 4-aminobiphenyl by horseradish peroxidase
    • Hughes MF, Smith BL, Eling TE. The oxidation of 4-aminobiphenyl by horseradish peroxidase. Chem Res Toxicol 1992; 5; 340-345.
    • (1992) Chem Res Toxicol , vol.5 , pp. 340-345
    • Hughes, M.F.1    Smith, B.L.2    Eling, T.E.3
  • 56
    • 0020640458 scopus 로고
    • An electron spin resonance study of the activation of benzidine by peroxidases
    • Josephy PD, Eling TE, Mason RP. An electron spin resonance study of the activation of benzidine by peroxidases. Mol Pharmacol 1983; 23: 766-770.
    • (1983) Mol Pharmacol , vol.23 , pp. 766-770
    • Josephy, P.D.1    Eling, T.E.2    Mason, R.P.3
  • 57
    • 0020478887 scopus 로고
    • The horseradish peroxidase-catalyzed oxidation of 3,5,3′,5′-tetramethylbenzidine
    • Josephy PD, Eling TE, Mason RP. The horseradish peroxidase-catalyzed oxidation of 3,5,3′,5′-tetramethylbenzidine. J Biol Chem 1982; 257: 3669-3675.
    • (1982) J Biol Chem , vol.257 , pp. 3669-3675
    • Josephy, P.D.1    Eling, T.E.2    Mason, R.P.3
  • 58
    • 0025857138 scopus 로고
    • One-electron oxidative activation of 2-aminofluorene by horseradish peroxidase compounds I and II: Spectral kinetic studies
    • Huang J, Dunford HB. One-electron oxidative activation of 2-aminofluorene by horseradish peroxidase compounds I and II: spectral kinetic studies. Arch Biochem Biophys 1991; 287: 257-262.
    • (1991) Arch Biochem Biophys , vol.287 , pp. 257-262
    • Huang, J.1    Dunford, H.B.2
  • 59
    • 9844263898 scopus 로고
    • Oxydation von Anilin zu Nitrosobenzol durch Peroxydasen
    • Böttcher G, Kiese M. Oxydation von Anilin zu Nitrosobenzol durch Peroxydasen. Naturwissenschaften 1960; 47: 157.
    • (1960) Naturwissenschaften , vol.47 , pp. 157
    • Böttcher, G.1    Kiese, M.2
  • 60
    • 0021741045 scopus 로고
    • Evidence for a one-electron mechanism of 2-aminofluorene oxidation by prostaglandin H synthase and horseradish peroxidase
    • Boyd JA, Eling TE. Evidence for a one-electron mechanism of 2-aminofluorene oxidation by prostaglandin H synthase and horseradish peroxidase. J Biol Chem 1984; 259: 13885-13896.
    • (1984) J Biol Chem , vol.259 , pp. 13885-13896
    • Boyd, J.A.1    Eling, T.E.2
  • 61
    • 9844228063 scopus 로고
    • Procainamide (PA) is N-chlorinated by myeloperoxidase (MPO)-implications for toxicity
    • Uetrecht J, Zahid N. Procainamide (PA) is N-chlorinated by myeloperoxidase (MPO)-implications for toxicity. Pharmacologist 1988; 30: A98.
    • (1988) Pharmacologist , vol.30
    • Uetrecht, J.1    Zahid, N.2
  • 62
    • 0023944956 scopus 로고
    • Metabolism of procainamide to a hydroxylamine by human neutrophiles and mononuclear leukocytes
    • Uetrecht J, Zahid N, Rubin R. Metabolism of procainamide to a hydroxylamine by human neutrophiles and mononuclear leukocytes. Chem Res Toxicol 1988; 1: 74-78.
    • (1988) Chem Res Toxicol , vol.1 , pp. 74-78
    • Uetrecht, J.1    Zahid, N.2    Rubin, R.3
  • 63
    • 0025245841 scopus 로고
    • Peroxidase-dependent oxidation of sulfonamides by monocytes and neutrophiles from humans and dogs
    • Cribb AE, Miller M, Tesoro A, Spielberg SP. Peroxidase-dependent oxidation of sulfonamides by monocytes and neutrophiles from humans and dogs. Mol Pharmacol 1990; 38: 744-751.
    • (1990) Mol Pharmacol , vol.38 , pp. 744-751
    • Cribb, A.E.1    Miller, M.2    Tesoro, A.3    Spielberg, S.P.4
  • 64
    • 0023886192 scopus 로고
    • Metabolism of dapsone to a hydroxylamine by human neutrophiles and mononuclear cells
    • Uetrecht J, Zahid N, Shear NH, Biggar WD. Metabolism of dapsone to a hydroxylamine by human neutrophiles and mononuclear cells. J Pharmacol Exp Ther 1988; 245: 274-279.
    • (1988) J Pharmacol Exp Ther , vol.245 , pp. 274-279
    • Uetrecht, J.1    Zahid, N.2    Shear, N.H.3    Biggar, W.D.4
  • 65
    • 0019021448 scopus 로고
    • The action of chloride peroxidase on 4-chloroaniline
    • Corbett MD, Chipko BR, Batchelor AO. The action of chloride peroxidase on 4-chloroaniline. Biochem J 1980; 187: 893-903.
    • (1980) Biochem J , vol.187 , pp. 893-903
    • Corbett, M.D.1    Chipko, B.R.2    Batchelor, A.O.3
  • 66
    • 0026000596 scopus 로고
    • Peroxygenation mechanism for chloroperoxidase-catalyzed N-oxidation of arylamines
    • Doerge DR, Corbett MD. Peroxygenation mechanism for chloroperoxidase-catalyzed N-oxidation of arylamines. Chem Res Toxicol 1991; 4: 556-560.
    • (1991) Chem Res Toxicol , vol.4 , pp. 556-560
    • Doerge, D.R.1    Corbett, M.D.2
  • 67
    • 0020962346 scopus 로고
    • The oxidation of 2-aminofluorene by prostaglandin endoperoxide synthetase
    • Boyd JA, Harvan DJ, Eling TE. The oxidation of 2-aminofluorene by prostaglandin endoperoxide synthetase. J Biol Chem 1983; 258: 8246-8254.
    • (1983) J Biol Chem , vol.258 , pp. 8246-8254
    • Boyd, J.A.1    Harvan, D.J.2    Eling, T.E.3
  • 68
    • 0345108715 scopus 로고
    • Hydroperoxidase-dependent oxidations during prostaglandin biosynthesis
    • Pryor WA (ed.). Academic Press, New York
    • Marnett LJ. Hydroperoxidase-dependent oxidations during prostaglandin biosynthesis. In: Pryor WA (ed.). Free Radicals in Biology, Vol. VI, Academic Press, New York, 1984, pp 63-94.
    • (1984) Free Radicals in Biology , vol.6 , pp. 63-94
    • Marnett, L.J.1
  • 69
    • 0021360480 scopus 로고
    • Metabolic activation of carcinogenic aromatic amines by dog bladder and kidney prostaglandin H synthase
    • Wise RW, Zenser TV, Kadlubar FF, Davis BB. Metabolic activation of carcinogenic aromatic amines by dog bladder and kidney prostaglandin H synthase. Cancer Res 1984; 44: 1893-1897.
    • (1984) Cancer Res , vol.44 , pp. 1893-1897
    • Wise, R.W.1    Zenser, T.V.2    Kadlubar, F.F.3    Davis, B.B.4
  • 70
    • 0021099472 scopus 로고
    • Co-oxidation of benzidine by prostaglandin synthase and comparison with the action of horseradish peroxidase
    • Josephy PD, Eling TE, Mason RP. Co-oxidation of benzidine by prostaglandin synthase and comparison with the action of horseradish peroxidase. J Biol Chem 1983; 258: 5561-5569.
    • (1983) J Biol Chem , vol.258 , pp. 5561-5569
    • Josephy, P.D.1    Eling, T.E.2    Mason, R.P.3
  • 71
    • 0021040850 scopus 로고
    • Prostaglandin H synthase catalyzed activation of benzidine: A model to assess pharmacologic intervention of the initiation of chemical carcinogenesis
    • Zenser TV et al. Prostaglandin H synthase catalyzed activation of benzidine: a model to assess pharmacologic intervention of the initiation of chemical carcinogenesis. J Pharmacol Exp Ther 1983; 227: 545-550.
    • (1983) J Pharmacol Exp Ther , vol.227 , pp. 545-550
    • Zenser, T.V.1
  • 72
    • 0021943764 scopus 로고
    • N-Oxidation of 4-chloroaniline by prostaglandin synthase
    • Golly I, Hlavica P. N-Oxidation of 4-chloroaniline by prostaglandin synthase. Biochem J 1985; 226: 803-809.
    • (1985) Biochem J , vol.226 , pp. 803-809
    • Golly, I.1    Hlavica, P.2
  • 73
    • 0020379117 scopus 로고
    • Prostaglandin endoperoxide synthetase-mediated metabolism of carcinogenic aromatic amines and their binding to DNA and protein
    • Kadlubar FF, Frederick CB, Weis CC, Zenser TV. Prostaglandin endoperoxide synthetase-mediated metabolism of carcinogenic aromatic amines and their binding to DNA and protein. Biochem Biophys Res Commun 1982; 108: 253-258.
    • (1982) Biochem Biophys Res Commun , vol.108 , pp. 253-258
    • Kadlubar, F.F.1    Frederick, C.B.2    Weis, C.C.3    Zenser, T.V.4
  • 74
    • 0023028620 scopus 로고
    • Generation of superoxide radical and hydrogen peroxide by 1,2,4-triaminobenzene, a mutagenic and myotoxic aromatic amine
    • Munday R. Generation of superoxide radical and hydrogen peroxide by 1,2,4-triaminobenzene, a mutagenic and myotoxic aromatic amine. Chem-Biol Interact 1986; 60: 171-181.
    • (1986) Chem-Biol Interact , vol.60 , pp. 171-181
    • Munday, R.1
  • 75
    • 0019155988 scopus 로고
    • Spectroscopic studies of cutaneous photosensitizing agents - I. Spin trapping of photolysis products from sulfanilamide, 4-aminobenzoic acid and related compounds
    • Chignell CF, Kalyanaraman B, Mason RP, Sik RH. Spectroscopic studies of cutaneous photosensitizing agents - I. Spin trapping of photolysis products from sulfanilamide, 4-aminobenzoic acid and related compounds. Photochem Photobiol 1980; 32: 563-571.
    • (1980) Photochem Photobiol , vol.32 , pp. 563-571
    • Chignell, C.F.1    Kalyanaraman, B.2    Mason, R.P.3    Sik, R.H.4
  • 76
    • 0018905144 scopus 로고
    • Photodecomposition of sulfonamides and tetracyclines
    • Sanniez WHK, Pilpel N. Photodecomposition of sulfonamides and tetracyclines. J Pharm Sci 1980; 69: 5-8.
    • (1980) J Pharm Sci , vol.69 , pp. 5-8
    • Sanniez, W.H.K.1    Pilpel, N.2
  • 77
    • 0015298915 scopus 로고
    • Photo- and radiation chemical studies. XIV. Photochemical studies of sulfanilamide, sulfacetamide and ethyl-4-aminobenzoate
    • Reisch J, Niemeyer DH. Photo- and radiation chemical studies. XIV. Photochemical studies of sulfanilamide, sulfacetamide and ethyl-4-aminobenzoate. Arch Pharm 1972; 305: 135-140.
    • (1972) Arch Pharm , vol.305 , pp. 135-140
    • Reisch, J.1    Niemeyer, D.H.2
  • 79
    • 0021700537 scopus 로고
    • The role of lipid perodixation in the N-oxidation of 4-chloroaniline
    • Golly I, Hlavica P, Wolf J. The role of lipid perodixation in the N-oxidation of 4-chloroaniline. Biochem J 1984; 224: 415-421.
    • (1984) Biochem J , vol.224 , pp. 415-421
    • Golly, I.1    Hlavica, P.2    Wolf, J.3
  • 80
    • 0023684489 scopus 로고
    • Distribution of microsomal monooxygenases in the rabbit respiratory tract
    • Sabourin P et al. Distribution of microsomal monooxygenases in the rabbit respiratory tract. Drug Metab Dispos 1988; 16: 557-562.
    • (1988) Drug Metab Dispos , vol.16 , pp. 557-562
    • Sabourin, P.1
  • 81
    • 0014682760 scopus 로고
    • α-Naphthylamine and β-naphthylamine in cigarette smoke
    • Hoffman D, Masuda X, Wynder EL. α-Naphthylamine and β-naphthylamine in cigarette smoke. Nature 1969; 221: 254-256.
    • (1969) Nature , vol.221 , pp. 254-256
    • Hoffman, D.1    Masuda, X.2    Wynder, E.L.3


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