Oxygen and Xenobiotic Reductase Activities of Cytochrome P450

References

• Omura T., Sato R. The carbon monoxide-binding pigment of liver microsomes. J. Biol. Chem. 1964; 239: 2370
   PubMed Web of Science ®Google Scholar
• Guengerich F. P. Cytochrome P450: advances and prospects. FASEB J. 1992; 6: 667
   PubMed Web of Science ®Google Scholar
• Wickramasingh R. H., Villee C. A. Early role during chemical evolution for cytochrome P450 in oxygen detoxification. Nature (London) 1975; 256: 509
   PubMed Web of Science ®Google Scholar
• Oxygen is poisonous — an introduction to oxygen toxicity and free radicals. Free Radicals in Biology and Medicine, B. Halliwell, J. M. C. Gutteridge. Clarendon Press, Oxford 1989; 1
   Google Scholar
• Bast A. Is formation of reactive oxygen by cytochrome P450 perilous and predictable. TIPS 1986; 7: 266
   Web of Science ®Google Scholar
• McCord J. M., Fridovich I. Superoxide dismutase: the first twenty years (1968–1988). Free Rad. Biol. Med. 1988; 5: 363
   PubMed Web of Science ®Google Scholar
• Gonzales F. J., Nebert D. W. Evolution of the P450 superfamily: animal-plant “warfare”, molecular drive and human genetic differences in drug oxidation. Trends Genet. 1990; 6: 182
   PubMed Web of Science ®Google Scholar
• Soucek P., Gut I. Cytochrome P450 in rats: structures, functions, properties and relevant human forms. Xenobiotica 1992; 22: 83
   PubMed Web of Science ®Google Scholar
• Garfinkel D. Studies on pig liver microsomes. I. Enzymatic and pigment composition of different microsomal preparations. Arch. Biochem. Biophys. 1958; 77: 376
   Web of Science ®Google Scholar
• Klingenberg M. Pigments of rat liver microsomes. Arch. Biochem. Biophys. 1958; 75: 376
   PubMed Web of Science ®Google Scholar
• Alvares A. P., Schilling G., Levin W., Kuntzman R. Studies on the induction of CO-binding pigment in liver microsomes by phenobarbital and 3-methylcholanthrene. Biochem. Biophys. Res. Commun. 1967; 29: 521
   PubMed Web of Science ®Google Scholar
• Nebert D. W., Nelson D. R., Adesnik M., Coon M. J., Estabrook R. W., Gonzales F. J., Guengerich F. P., Gunsalus I. C., Johnson E. F., Kemper B., Levin W., Phillips I. R., Sato R., Waterman M. R. The P450 superfamily: updated listing of all genes and recommended nomenclature for the chromosomal loci. DNA 1989; 8: 1
   PubMedGoogle Scholar
• Nebert D. W., Nelson D. R., Coon M. J., Estabrook R. W., Feyereisen R., Fujii-Kuriyama Y., Gonzales F. J., Guengerich F. P., Gunsalus I. C., Johnson E. F., Loper J. C., Sato R., Waterman M. R., Waxman D. J. The P450 superfamily: update on new sequences, gene mapping and recommended nomenclature. DNA Cell. Biol. 1991; 10: 1
   PubMed Web of Science ®Google Scholar
• Brown C. A., Black S. D. Membrane topology of mammalian cytochrome P450 from liver endoplasmic reticulum: determination by trypsinolysis of phenobarbital-treated microsomes. J. Biol. Chem. 1989; 264: 4442
   PubMed Web of Science ®Google Scholar
• Black S. D. Membrane topology of the mammalian P450 cytochromes. FASEB J. 1992; 6: 680
   PubMed Web of Science ®Google Scholar
• Guengerich F. P., Martin M. V. Purification of cytochrome P-450, NADPH-cytochrome P-450 reductase and epoxide hydratase from a single preparation of rat liver microsomes. Arch. Biochem. Biophys. 1980; 205: 365
   PubMed Web of Science ®Google Scholar
• Schenkman J. B., Sligar S. G., Cinti D. L. Substrate interaction with cytochrome P450. Hepatic Cytochrome P450 Monooxygenase System, J. B. Schenkman, D. Kupfer. Pergamon Press, Oxford 1982; 587
   Google Scholar
• Backes W. L., Turner J. L., Heinemann T. G., Canady W. J. Association of hydrophobic substances with hemin: Characterization of the reverse type I binding spectrum and its relationship to cytochrome P450. Biochem. Pharmacol. 1986; 35: 4443
   PubMed Web of Science ®Google Scholar
• Lewis D. F. V., Ionnides C., Parke D. V. Molecular orbital studies of oxygen activation and mechanisms of cytochrome P450-mediated oxidative metabolism of xenobiotics. Chem. Biol. Interact. 1989; 70: 263
   PubMed Web of Science ®Google Scholar
• Williams R. J. P. Haem-proteins and oxygen. Iron in Biochemistry and Medicine, A. Jacobs, M. Worwood. Academic Press, New York 1974; 183
   Google Scholar
• Poulos T. L., Raag R. Cytochrome P450cam: crystallography, oxygen activation and electron transfer. FASEB J. 1992; 6: 674
   PubMed Web of Science ®Google Scholar
• Sligar S. G., Murray R. I. Cytochrome P-450cam and other bacterial P- 450 enzymes. Cytochrome P-450: Structure, Mechanism, and Biochemistry, P. R. Ortiz de Montellano. Plenum Press, New York 1986; 429
   Google Scholar
• Poulos T. L. Cytochrome P450: molecular architecture, mechanism and prospects for rational inhibitor design. Pharmaceut. Res. 1988; 5: 67
   PubMed Web of Science ®Google Scholar
• Miwa G. T., Lu A. Y. H. The topology of the mammalian cytochrome P-450 active site. Cytochrome P-450, Structure, Mechanism, and Biochemistry, P. R. Ortiz de Montellano. Plenum Press, New York 1986; 77
   Google Scholar
• Guengerich F. P., Wang P., Davidson N. K. Estimation of isoenzymes of microsomal cytochrome P450 in rats, rabbits and humans using immunochemical staining coupled with sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Biochemistry 1982; 21: 1698
   PubMed Web of Science ®Google Scholar
• Pickett C. B., Jeter R. L., Morin J., Lu A. Y. H. Electroimmunochemical quantitation of cytochrome P450, cytochrome P448 and epoxide hydrolase in rat liver microsomes. J. Biol. Chem. 1981; 256: 8815
   PubMed Web of Science ®Google Scholar
• Armstrong R. N., Levin W., Ryan D. E., Thomas P. E., Mah H. D., Jerina D. M. Stereoselectivity of rat liver cytochrome P450c in formation of benzo[a]pyrene 4,5-oxide. Biochem. Biophys. Res. Commun. 1981; 100: 1077
   PubMed Web of Science ®Google Scholar
• Boyd D. R., Gadaginamath G. S., Kher A., Malone J. F., Yagi H., Jerina D. M. (+)- and (-)-benzo[a]pyrene 7,8-oxide: synthesis, absolute stereochemistry, and stereochemical correlation with other mammalian metabolites of benzo[a]pyrene. J. Chem. Soc. Perkin Trans. 1980; 1: 2112
   Google Scholar
• Van Bladeren P. J., Armstrong R. N., Cobb D., Thakker D. R., Ryan D. E., Thomas P. E., Sharma N. D., Boyd D. R., Levin W., Jerina D. M. Stereoselective formation of benzo[a]anthracene (+)-(5S, 6R)-oxide and (+)-(8R, 9S)-oxide by a highly purified and reconstituted system containing P450c. Biochem. Biophys. Res. Commun. 1982; 106: 602
   PubMed Web of Science ®Google Scholar
• Nordqvist M., Thakker D. R., Vyas K. P., Yagi H., Levin W., Ryan D. E., Thomas P. E., Conney A. H., Jerina D. M. Metabolism of chrysene and phenanthrene to bay-region diol epoxides by rat liver enzymes. Mol. Pharmacol. 1981; 19: 168
   PubMed Web of Science ®Google Scholar
• Yagi H., Jerina D. M. Absolute configuration of the trans-9,10-dihydrodiol metabolite of the carcinogen benzo[a]pyrene. J. Am. Chem. Soc. 1982; 104: 4026
   Web of Science ®Google Scholar
• Ortiz de Montellano P. R. Prosthetic heme alkylation and the catalytic mechanism of cytochrome P450. Rev. Biochem. Toxicol. 1984; 6: 1
   Google Scholar
• Koymans L., Vermeulen N. P. E., Van Acker S. A. B. E., Koppele J. M., Heykants J. J. P., Lavrijsen K., Meuldermans W., Donné-Opden Kelder G. M. A predictive model for substrates of cytochrome P450-debrisoquine (2D6). Chem. Res. Toxicol. 1992; 5: 211
   PubMed Web of Science ®Google Scholar
• Koymans L., Vermeulen N. P. E., Baarslag A., Donné-Op den Kelder G. M. A preliminary 3D model for cytochrome P450 2D6 constructed by homology model building. J. Comp. vt. Aided Mol. Design 1993; 7: 281
   PubMed Web of Science ®Google Scholar
• Taniguchi H., Imai Y., Sato R. Role of electron transfer system in microsomal drug monooxygenase reaction catalyzed by cytochrome P450. Arch. Biochem. Biophys. 1984; 232: 585
   PubMed Web of Science ®Google Scholar
• Gum J. R., Strobel H. W. Isolation of the membrane-binding peptide of NADPH-cytochrome P450 reductase: characterization of the peptide and its role in the interaction of reductase with P450. J. Biol. Chem. 1979; 254: 4177
   PubMedGoogle Scholar
• Potter D. W., Reed D. J. Involvement of FMN and phenobarbital cytochrome P450 in stimulating a one-electron reductive denitrosation of 1-(2-chloroethyl)-3-(cyclohexyl)-1-nitrosourea catalyzed by NADPH-cytochrome P450 reductase. J. Biol. Chem. 1983; 258: 6906
   PubMed Web of Science ®Google Scholar
• Vermilion J. L., Coon M. J. Identification of the high and low potential flavins of liver microsomal NADPH-cytochrome P450 reductase. J. Biol. Chem. 1978; 253: 8812
   PubMed Web of Science ®Google Scholar
• Strobel H. W., Fang W.-F., Takazawa R. S., Stralka D. J., Newaz S. N., Kurzban G. P., Nelson D. R., Beyer R. S. Cytochrome P450 and the activation and inactivation of mutagens and carcinogens. Basic Life Sci. 1986; 39: 61
   PubMedGoogle Scholar
• Gum J. R., Strobel H. W. Isolation of the membrane-binding peptide of NADPH-cytochrome P450 reductase. Characterization of the peptide and its role in the interaction of reductase with cytochrome P450. J. Biol. Chem. 1981; 256: 7478
   PubMed Web of Science ®Google Scholar
• Black S. D., French J. S., Williams C. H., Jr., Coon M. J. Role of a hydrophobic polypeptide in the N-terminal region of NADPH-cytochrome P450 reductase complex formation with P450LM. Biophys. Res. Commun. 1979; 91: 1528
   PubMed Web of Science ®Google Scholar
• Black S. D., Coon M. J. Structural features of liver microsomal NADPH-cytochrome P-450 reductase. Hydrophobic domain, hydrophilic domain, and connecting region. J. Biol. Chem. 1982; 257: 5929
   PubMed Web of Science ®Google Scholar
• Nadler S. G., Strobel H. W. Identification and characterization of an NADPH-cytochrome P450 reductase derived peptide involved in binding to cytochrome P450. Arch. Biochem. Biophys. 1991; 2: 277
   Google Scholar
• Voznesensky A. I., Schenkman J. B. The cytochrome P4502B4-NADPH-cytochrome P450 reductase electron transfer is not formed by charge-pairing. J. Biol. Chem. 1992; 267: 14669
   PubMed Web of Science ®Google Scholar
• Miwa G. T., West S. B., Huang M.-T., Lu A. Y. H. Studies on the association of cytochrome P450 and NADPH-cytochrome C reductase during catalysis in a reconstituted hydroxylating system. J. Biol. Chem. 1979; 254: 5695
   PubMed Web of Science ®Google Scholar
• Shepard E. A., Phillips I. R., Bayney R. M., Pike S. F., Rabin B. R. Quantification of NADPH-cytochrome P450 reductase in liver. Biochem. J. 1983; 211: 333
   PubMed Web of Science ®Google Scholar
• Backes W. L., Tamburini P. P., Jansson I., Gibson G. G., Sligar S. G., Schenkman J. B. Kinetics of cytochrome P450 reduction: evidence for faster reduction of the high-spin ferric state. Biochemistry 1985; 24: 5130
   PubMed Web of Science ®Google Scholar
• Tamburini P. P., Gibson G. G., Backes W. L., Sligar S. G., Schenkman J. B. Reduction kinetics of purified rat liver cytochrome P450. Evidence for a sequential reaction mechanism dependent on the hemoprotein spin state. Biochemistry 1984; 23: 4526
   PubMed Web of Science ®Google Scholar
• Backes W. L., Sligar S. G., Schenkman J. B. Kinetics of hepatic cytochrome P450 reduction: correlation with spin state of the ferric heme. Biochemistry 1982; 21: 1324
   PubMed Web of Science ®Google Scholar
• Schenkman J. B., Gibson G. G. Status of the cytochrome P450 cycle. TIPS June, 1981; 150
   Web of Science ®Google Scholar
• Sligar S. G., Cinti D. L., Gibson G. G., Schenkman J. B. Spin state control of the hepatic cytochrome P450 redox potential. Biochem. Biophys. Res. Commun. 1979; 90: 925
   PubMed Web of Science ®Google Scholar
• Franklin M. R., Estabrook R. W. On the inhibitory action of mersalyl on drug oxidation: a rigid organization of the electron transport chain. Arch. Biochem. Biophys. 1971; 143: 318
   PubMed Web of Science ®Google Scholar
• Yang C. S. The association between cytochrome P450 and NADPH-cytochrome P450 reductase in microsomal membrane. FEBS Lett. 1975; 54: 61
   PubMed Web of Science ®Google Scholar
• Peterson J. A., Ebel R. E., O'Keeffe D. H., Matsubara T., Estabrook R. W. Temperature dependence of cytochrome P450 reduction. A model for NADPH-cytochrome P450 reductase: cytochrome P450 interaction. J. Biol. Chem. 1976; 251: 4010
   PubMed Web of Science ®Google Scholar
• Tangiguchi H., Imai Y., Iyanagi T., Sato R. Interaction between NADPH-cytochrome P450 reductase and cytochrome P450 in the membrane of phosphatidylcholine vesicles. Biochem. Biophys. Acta 1979; 550: 341
   PubMedGoogle Scholar
• Gut J., Richter C., Cherry R. J., Wintherhalter K. H., Kawato S. Rotation of cytochrome P450. Complex formation of cytochrome P450. Complex formation of cytochrome P450 with NADPH-cytochrome P450 reductase in liposomes demonstrated by combining protein rotation with antibody-induced cross-linking. J. Biol. Chem. 1983; 258: 8588
   PubMed Web of Science ®Google Scholar
• Backes W. L., Eyer C. S. Cytochrome P450LM2 reduction. Substrate effects on the rate of reductase-LM2 association. J. Biol. Chem. 1989; 264: 6252
   PubMed Web of Science ®Google Scholar
• Eyer C. S., Backes W. L. Relationship between the rate of reductase-cytochrome P450 complex formation and the rate of first electron transfer. Arch. Biochem. Biophys. 1992; 293: 231
   PubMed Web of Science ®Google Scholar
• Gunsalus I. C., Pedersen T. C., Sligar S. G. Oxygenase-catalyzed biological hydroxylations. Annu. Rev. Biochem. 1975; 44: 377
   PubMed Web of Science ®Google Scholar
• Sipes G., Gandolfi A. J. Biotransformation of toxicants. Cassarett & Doul's Toxicology: The Basic Science of Poisons, C. D. Klaassen, M. D. Amdur, J. Doul. MacMillan, New York 1986; 64
   Google Scholar
• Groves J. T., Watanabe Y. Reactive iron porphyrin derivatives related to the catalytic cycles of cytochrome P450 and peroxidases. Studies of the mechanism of oxygen activation. J. Am. Chem. Soc. 1988; 110: 8443
   Web of Science ®Google Scholar
• Cytochrome P-450: Structure, Mechanism, and Biochemistry, P. R. Ortiz de Montellano. Plenum Press, New York 1986
   Google Scholar
• Ortiz de Montellano P. R. Cytochrome P450 catalysis: radical intermediates and dehydrogenation reactions. TIPS 1989; 10: 354
   PubMed Web of Science ®Google Scholar
• Koymans L., Van Lenthe J. H., Van de Straat R., Donné-Op den Kelder G. M., Vermeulen N. P. E. A theoretical study on the metabolic activation of paracetamol by cytochrome P450: indications for a uniform oxidation mechanism. Chem. Res. Toxicol. 1989; 2: 60
   PubMed Web of Science ®Google Scholar
• White R. E., Coon M. J. Oxygen activation by cytochrome P450. Annu. Rev. Biochem. 1980; 49: 315
   PubMed Web of Science ®Google Scholar
• Kadlubar F. F., Morton K. C., Ziegler D. M. Microsomal catalyzed hydroperoxide-dependent C-oxidation of amines. Biochem. Biophys. Res. Commun. 1973; 54: 1225
   Web of Science ®Google Scholar
• Rahimtula A. D., O'Brien P. J. Hydroperoxide catalyzed liver microsomal aromatic hydroxylation reactions involving cytochrome P450. Biochem. Biophys. Res. Commun. 1974; 60: 440
   PubMed Web of Science ®Google Scholar
• Hewson W. D., Hager L. P. Peroxidases, catalases and chlorperoxidases. The Porphyrins, D. Dolphin. Academic Press, New York 1979; Vol. 7: 295
   Google Scholar
• Kuthan H., Ullrich V. Oxidase and oxygenase function of the microsomal cytochrome P450 monooxygenase system. Eur. J. Biochem. 1982; 126: 583
   PubMedGoogle Scholar
• Fisher M. T., Sligar S. G. Control of heme redox potential and reduction rate: a linear free energy relation between potential and ferric spin state equilibrium. J. Am. Chem. Soc. 1983; 107: 5018
   Web of Science ®Google Scholar
• Atkins W. M., Sligar S. G. Metabolic switching in cytochrome P450cam: deuterium isotope effects on regiospecificity and the monooxygenase/oxydase reaction. J. Am. Chem. Soc 1987; 109: 3754
   Web of Science ®Google Scholar
• Raag R., Poulos T. L. Crystal structure of the carbon monoxide-substrate-cytochrome P450cam ternary complex. Biochemistry 1989; 28: 7586
   PubMed Web of Science ®Google Scholar
• Raag R., Martinis S. A., Sligar S. G., Poulos T. L. Crystal structure of the cytochrome P450cam active site mutant. Biochemistry 1991; 30: 11421
   Web of Science ®Google Scholar
• Brinigar W. S., Chang C. K., Geibel J., Traylor T. G. Solvent effects on reversible formation and oxidative stability of heme-oxygenase complexes. J. Am. Chem. Soc. 1974; 96: 5597
   PubMed Web of Science ®Google Scholar
• Guengerich F. P., Ballou D. P., Coon M. J. Spectral intermediates in the reaction of oxygen with purified liver microsomal cytochrome P450. Biochem. Biophys. Res. Commun. 1976; 70: 951
   PubMed Web of Science ®Google Scholar
• Tyson C. A., Lipscomb J. D., Gunsalus I. C. The roles of putidaredoxin and P450cam in methylene hydroxylation. J. Biol. Chem. 1972; 247: 5777
   PubMed Web of Science ®Google Scholar
• Nelson D. R., Strobel H. W. On the membrane topology of vertebrate cytochrome P450 proteins. J. Biol. Chem. 1988; 263: 6038
   PubMed Web of Science ®Google Scholar
• Ishigooka M., Shimizu T., Hiroya K., Hatano M. Role of Glu318 at the putative distal site in the catalytic function of cytochrome P450d. Biochemistry 1992; 31: 1528
   PubMed Web of Science ®Google Scholar
• Ekström G., Cronholm T., Ingelman-Sundberg M. Hydroxyl-radical production and ethanol oxidation by liver microsomes isolated from ethanol-treated rats. Biochem. J. 1986; 233: 755
   PubMed Web of Science ®Google Scholar
• Ingelman-Sundberg M., Johansson I. Mechanisms of hydroxyl radical formation and ethanol oxidation by ethanol-inducible and other forms of rabbit liver microsomal cytochrome P450. J. Biol. Chem. 1984; 259: 6447
   PubMed Web of Science ®Google Scholar
• Gorsky L. D., Koop D. R., Coon M. J. On the stoichiometry of the oxidase and monooxygenase reactions catalyzed by liver microsomal cytochrome P450. J. Biol. Chem. 1984; 259: 6812
   PubMed Web of Science ®Google Scholar
• Eliasson E., Johansson I., Ingelman-Sundberg M. Ligand-dependent maintenance of ethanol-inducible cytochrome P450 in primary rat hepatocyte cell cultures. Biochem. Biophys. Res. Commun. 1988; 150: 436
   PubMed Web of Science ®Google Scholar
• Ekström G., Ingelman-Sundberg M. Rat liver microsomal NADPH-supported oxidase activity and lipid peroxidation dependent and ethanol-inducible cytochrome P450 (P450IIEI). Biochem. Pharmacol. 1989; 38: 1313
   PubMed Web of Science ®Google Scholar
• Saito I., Matsumura T., Inoue K. Formation of superoxide ion via one-electron transfer from electron donors to singlet oxygen. J. Am. Chem. Soc. 1982; 105: 3200
   Google Scholar
• Welborn C. H., Dolphin D., James B. R. One-electron electrochemical reduction of a ferrous porphyrin dioxygen complex. J. Am. Chem. Soc. 1981; 100: 627
   Google Scholar
• Guengerich F. P. Oxidation-reduction properties of rat liver cytochromes P-450 and NADPH-cytochrome P-450 reductase related to catalysis in reconstituted systems. Biochemistry 1983; 22: 2811
   PubMed Web of Science ®Google Scholar
• Koppenol W. H., Van Buuren K. J. H., Butler J., Braams R. The kinetics of the reduction of cytochrome C by the superoxide anion radical. Biochim. Biophys. Acta 1976; 449: 157
   PubMed Web of Science ®Google Scholar
• Ekström G., Ingelman-Sundberg M. Mechanisms of lipid peroxidation dependent upon cytochrome P450 LM2. Eur. J. Biochem. 1986; 158: 195
   PubMedGoogle Scholar
• Nordmann R., Ribiere C., Rouach H. Implication of free radical mechanisms in ethanol-induced cellular injury. Free Rad. Biol. Med. 1992; 12: 219
   PubMed Web of Science ®Google Scholar
• Jeffery E. H., Mannering G. J. Interaction of constitutive and phenobarbital-induced cytochrome P450 isoenzymes during the sequential oxidation of benzphetamine. Mol. Pharmacol 1982; 23: 748
   Google Scholar
• Estabrook R. W., Kawano S., Werringloer J., Kuthan H., Tsuji H., Graf H., Ullrich V. Oxycytochrome P450: its breakdown to superoxide for the formation of hydrogen peroxide. Acta Biol. Med. Ger. 1979; 38: 423
   PubMedGoogle Scholar
• Ullrich V., Diehl H. Uncoupling of mono-oxygenation and electron transport by fluoro carbons in liver microsomes. Eur. J. Biochem. 1971; 20: 509
   PubMedGoogle Scholar
• Bast A., Savenije-Chapel E. M., Kroes B. H. Inhibition of monooxygenase and oxidase activity of rat-hepatic cytochrome P450 by H2-receptor blockers. Xenobiotica 1984; 14: 399
   PubMed Web of Science ®Google Scholar
• Takamo T., Iyazaki Y. M., Araki R. Interaction of 1,1,1-trichloroethane with the mixed-function oxidation system in rat liver microsomes. Xenobiotica 1988; 18: 1457
   PubMed Web of Science ®Google Scholar
• Schenkman J. B., Remmer H., Estabrook R. W. Spectral studies of drug interaction with hepatic microsomal cytochrome P 450. Mol. Pharmacol. 1967; 3: 113
   PubMed Web of Science ®Google Scholar
• Bush M. T., Weller H. The metabolic fate of hexobarbital. Drug Metab. Rev. 1973; 1: 249
   Web of Science ®Google Scholar
• Van der Graaf M., Vermeulen N. P. E. Disposition of hexobarbital: 15 years of an intriguing model substrate. Drug Metab. Rev. 1988; 19: 109
   PubMed Web of Science ®Google Scholar
• Heinemeyer G., Nigam S., Hildebrandt A. G. Hexobarbital-binding, hydroxylation and hexobarbital-dependent hydrogen peroxide production in hepatic microsomes of guinea pig, rat and rabbit. Naunyn Schmiedeberg's Arch. Pharmacol. 1980; 314: 201
   Google Scholar
• Hildebrandt A. G., Speck M., Roots I. Possible control of hydrogen peroxide production and degradation on microsomes during mixed function oxidation reactions. Biochem. Biophys. Res. Commun. 1973; 54: 968
   PubMed Web of Science ®Google Scholar
• Estabrook R. W., Werringloer J. Active oxygen — fact or fantasy. Microsomes and Drug Oxidations, V. Ullrich, I. Roots, A. G. Hildebrandt, R. W. Estabrook, A. H. Conney. Pergamon Press, New York 1977; 748
   Google Scholar
• Degkwitz E., Ullrich V., Stankinger J. Metabolism and cytochrome P450 binding spectra of (+)-and (-)-hexobarbital in rat liver microsomes. Hoppe Seyler's Z. Physiol. Chem. 1969; 350: 547
   PubMedGoogle Scholar
• Klinger W., Reytag A. F., Schmitt W. Influence of age, hexobarbital, and aniline on NADPH/NADH dependent hydrogen peroxide production in rat hepatic microsomes. Arch. Toxicol. 1986; 382, Suppl. 9
   Google Scholar
• Bast A., Goossens P. A. L., Savenije-Chapel E. M. Dependence of hydrogen peroxide formation in rat liver microsomes and the molecular structure of cytochrome P450-substrates: a study with barbiturates and β-adrenoceptor antagonists. Eur. J. Drug. Metab. Pharmakokinet. 1989; 14: 93
   PubMed Web of Science ®Google Scholar
• Estabrook R. W., Werringloer J. Cytochrome P-450 — its role in oxygen activation for drug metabolism. Drug Metabolism Concepts, S. Jerina. American Chemical Society, Washington, D. C. 1977; 1
   Google Scholar
• Tsong T. Y., Yang C. S. Rapid conformational changes of cytochrome P-450: effect of dimyristoyl lecithin. Proc. Natl. Acad. Sci. USA. 1978; 75: 5955
   PubMed Web of Science ®Google Scholar
• Imai Y., Sato R., Yanagi T. I. Rate-limiting step in the reconstituted microsomal drug hydroxylase system. J. Biochem. 1977; 22: 1237
   Google Scholar
• Ullrich V., Kuthan H. Biochemical and Biophysical Regulation of Cytochrome P-450, J. A. Gustafsson, J. Carlstedt-Duke, A. Mode, I. Raffer. Elsevier, Amsterdam 1980; 267
   Google Scholar
• Van de Straat R., De Vries J., Vermeulen N. P. E. Role of hepatic microsomal and purified cytochrome P450 in one-electron reduction of two quinoneimines and concomitant reduction of molecular oxygen. Biochem. Pharmacol. 1987; 36: 613
   PubMed Web of Science ®Google Scholar
• Ingelman-Sundberg M., Johansson I. Mechanisms of hydroxyl radical formation and ethanol oxidation by ethanol-inducible and other forms of rabbit liver microsomal cytochrome P450. J. Biol. Chem. 1984; 259: 6447
   PubMed Web of Science ®Google Scholar
• Auclair C., De Prost D., Hakim J. Superoxide anion production by liver microsomes from phenobarbital treated rat. Biochem. Pharmacol. 1978; 27: 355
   PubMed Web of Science ®Google Scholar
• Goeptar A. R., Te Koppele J. M., Neve E. P. A., Vermeulen N. P. E. Reductase and oxidase activity of rat liver cytochrome P450 with 2,3,5,6-tetramethylbenzoquinone as substrate. Chem. Biol. Interact. 1992; 83: 249
   PubMed Web of Science ®Google Scholar
• Parkinson A., Ryan D. E., Thomas P. E., Jerina D. M., Sayer J. M., Van Bladeren P. J., Haniu M., Shively J. E., Levin W. Chemical modification and inactivation of rat liver microsomal cytochrome P450c by 2-bromo-4′-mtroacetophenone. J. Biol. Chem. 1986; 261: 11478
   PubMed Web of Science ®Google Scholar
• Parkinson A., Thomas P. E., Ryan D. E., Gorsky L. D., Shively J. E., Sayer J. M., Jerina D. M., Levin W. Mechanism of inactivation of rat liver microsomal cytochrome P450c by 2-bromo-4′-nitroacetophenone. J. Biol. Chem. 1986; 261: 11487
   PubMed Web of Science ®Google Scholar
• Goeptar A. R., Te Koppele J. M., Van Maanen J. M. S., Zoetemelk C. E. M., Vermeulen N. P. E. One-electron reductive bioactivation of 2,3,5,6-tetramethyl-benzoquinone by cytochrome P450. Biochem. Pharmacol. 1992; 43: 343
   PubMed Web of Science ®Google Scholar
• Persson J. O., Terelius Y., Ingelman-Sundberg M. Cytochrome P450-dependent formation of reactive oxygen radicals: isozyme-specific inhibition of P450-mediated reduction of oxygen and carbon tetrachloride. Xenobiotica 1990; 20: 887
   PubMed Web of Science ®Google Scholar
• Goldblum A., Loew G. H. Quantum chemical studies of anaerobic reductive metabolism of halothane by cytochrome P450. Chem. Biol. Interact. 1980; 32: 83
   PubMed Web of Science ®Google Scholar
• Luke B. T., Loew G. H., McLean A. D. Theoretical investigations of the anaerobic reduction of halogenated alkanes by cytochrome P450.1. Structure, inversion barriers, and heats of formation of halomethyl radicals. J. Am. Chem. Soc. 1987; 109: 1307
   Web of Science ®Google Scholar
• Nastainczyk W., Ullrich V. Effect of oxygen concentration on the reaction of halothane with cytochrome P450 in liver microsomes and isolated perfused rat liver. Biochem. Pharmacol. 1978; 27: 387
   PubMed Web of Science ®Google Scholar
• De Groot H., Noll T. The crucial role of low steady state oxygen partial pressure in haloalkane free radical mediated lipid peroxidation. Biochem. Pharmacol. 1986; 35: 15
   PubMed Web of Science ®Google Scholar
• Knecht K. T., Mason R. P. In vivo radical trapping and biliary secretion of radical adducts of carbon tetrachloride-derived free radical metabolites. Drug Metab. Dispos. 1988; 16: 813
   PubMed Web of Science ®Google Scholar
• Gooding P. E., Chayen J., Sawyer B., Slater T. F. Cytochrome P-450 distribution in rat liver and the effect of sodium phenobarbitone administration. Chem. Biol. Interact. 1978; 20: 299
   PubMed Web of Science ®Google Scholar
• Kessler M., Lang H., Sinagowitz E., Rink R., Höper J. Oxygen Transport to Tissues, A Part, D. F. Bruley, H. I. Bicker. Plenum Press, New York 1973; 351
   Google Scholar
• Koop D. R. Oxidative and reductive metabolism by cytochrome P450 2E1. The FASEB J. 1992; 6: 724
   PubMed Web of Science ®Google Scholar
• Vromans R. M., Van de Straat R., Groeneveld M., Vermeulen N. P. E. One-electron reduction of mitomycin C by rat liver: role of cytochrome P450 and NADPH-cytochrome P450 reductase. Xenobiotica 1990; 20: 967
   PubMed Web of Science ®Google Scholar
• Kennedy K. A., Sligar S. G., Polonski L., Sartorelli A. C. Metabolic activation of mitomycin C by liver microsomes and nuclei. Biochem. Pharmacol. 1982; 31: 2011
   PubMed Web of Science ®Google Scholar
• Goeptar A. R., Te Koppele J. M., Lamme E. K., Piqué J. M., Vermeulen N. P. E. Cytochrome P450IIB1-mediated one-electron reduction of adriamycin: a study with rat liver microsomes and purified enzymes. Mol. Pharmacol. 1993; 44: 1267
   PubMed Web of Science ®Google Scholar
• Chesis P. L., Levin D. E., Smit M. T., Ernster L., Ames B. N. Mutagenicity of quinones: pathways of metabolic activation and detoxification. Proc. Natl. Acad. Sci. U.S.A. 1984; 81: 1696
   PubMed Web of Science ®Google Scholar
• Weiner L. M., Gritzan N. P., Bezhnin N. M., Lyakhovich V. V. Microsomal and photochemical oxidation and reduction of 1-piperidinoanthraquinone. Biochim. Biophys. Acta 1982; 714: 234
   PubMed Web of Science ®Google Scholar
• Davis S., Weiss M. J., Wong J. R., Lampidis T. L., Chen L. B. Mitochondrial and plasma membrane potentials cause unusual accumulation and retention of rhodamine 123 by human breast adeno-carcinoma-derived MCF-7 cells. J. Biol. Chem. 1985; 260: 13844
   PubMed Web of Science ®Google Scholar
• Mikalsen A., Alexander J., Andersen R. A., Ingelman-Sundberg M. Effect of in vivo chromate actone and combined treatment on rat liver in vitro microsomal chromium (VI) reductive activity and on cytochrome P450 expression. Pharmacol. Toxicol. 1991; 68: 546
   Google Scholar
• Vaz A. D. N., Roberts E. S., Coon M. J. Reductive β-scission of the hydroperoxide of fatty acids and xenobiotics: Role of alcohol-inducible cytochrome P450. Proc. Natl. Acad. Sci. U.S.A. 1990; 87: 5499
   PubMed Web of Science ®Google Scholar
• Manno M., Ferrara R., Cazzaro S., Rigotti P., Ancona E. Suicidal inactivation of human cytochrome P450 by carbon tetrachloride and halothane in vitro. Pharmacol. Toxicol. 1992; 70: 13
   PubMedGoogle Scholar
• Mansuy D., Fontecave M. Reduction of benzylhalides by liver microsomes. Formation of 478 nm-absorbing σ-alkyl-ferric cytochrome P450 complexes. Biochem. Pharmacol. 1971; 32, 1983
   Google Scholar
• Testai E., Vitozzi L. Biochemical alterations elicited in rat liver microsomes by oxidation and reduction products of chloroform metabolism. Chem. Biol. Interact. 1986; 59: 157
   PubMed Web of Science ®Google Scholar
• Baker M. T., Nelson R. M., Van Dyke R. A. The formation of chlorobenzene and benzene by the reductive metabolism of lindane in rat liver microsomes. Arch. Biochem. Biophys. 1985; 236: 506
   PubMed Web of Science ®Google Scholar
• Thompson J. A., Ho B., Mastovich S. C. Reductive metabolism of 1,1,1,2-tetrachloroethane and related chloroethanes by rat liver microsomes. Chem. Biol. Interact. 1984; 51: 321
   PubMed Web of Science ®Google Scholar
• McGirr L. G., Khan S., Lauriault V., O'Brien P. J. Molecular mechanisms for bromotrichloromethane cytotoxicity in isolated rat hepatocytes. Xenobiotica 1990; 20: 933
   PubMed Web of Science ®Google Scholar
• De Toranzo E. G. D., Villarruel M. C., Castro J. A. Early destruction of cytochrome P-450 in testis of carbon tetrachloride poisoned rats. Toxicology 1978; 10: 39
   PubMed Web of Science ®Google Scholar
• Reiner O., Athanassopoulos S., Hellmer K. H., Murray R. E., Uehleke H. Bilkung von Chloroform aus Tetrachlorkohlen Stoff in Leber-mikrosomen, Lipidperoxidation und Zerstorung vor Cytochrom P450. Arch. Toxikol. 1977; 29: 219
   Google Scholar
• Noguchi T., Fong K. L., Lai E. K., Alexander S. S., King M. M., Olson L., Poyer J. L., McCay P. B. Specificity of a phenobarbital-induced cytochrome P450 for metabolism of carbon tetrachloride to the trichloromethyl radical. Biochem. Pharmacol. 1982; 31: 615
   PubMed Web of Science ®Google Scholar
• Farber J. L., Gerson R. J. Mechanisms of cell injury with hepatotoxic chemicals. Am. Soc. Pharmacol. Exp. Ther. 1984; 36: 71
   Google Scholar
• Waller R. L., Recknagel R. O. Evaluation of a role for phosgene production in the hepatotoxic mechanism of action of carbon tetrachloride and bromotrichloromethane. Toxicol. Appl. Pharmacol. 1982; 66: 172
   PubMed Web of Science ®Google Scholar
• Kubic V. L., Anders M. W. Metabolism of carbon tetrachloride to phosgene. Life Sci. 1980; 26: 2151
   PubMed Web of Science ®Google Scholar
• Nadkarni G. S., D'Souza N. B. Hepatic antioxidant enzymes and lipid peroxidation in carbon tetrachloride-induced liver cirrhosis in rats. Biochem. Med. Metob. Biol. 1988; 40: 42
   PubMedGoogle Scholar
• Glende E. A., Jr., Recknagel T. O. An indirect method demonstrating that CCl4-dependent hepatocyte injury is linked to a rise in intracellular calciumion concentration. Res. Comun. Chem. Pathol. Pharmacol 1992; 73: 41
   Google Scholar
• Reinke L. A., Towner R. A., Janzen E. G. Spin trapping of free radical metabolites of carbon tetrachloride in vitro and in vivo: effect of acute ethanol administration. Toxicol. Appl. Pharmacol. 1992; 112: 17
   PubMed Web of Science ®Google Scholar
• De Groot H., Haas W. Self-catalyzed, O2 independent inactivation of NADPH- or dithionite-reduced microsomal cytochrome P450 by carbon tetrachloride. Biochem. Pharmacol. 1981; 30: 2343
   PubMed Web of Science ®Google Scholar
• Manno M., King L. J., De Matteis F. The degradation of haem by carbon tetrachloride: metabolic activation required a free axial co-ordination site on the haem iron and electron donation. Xenobiotica 1989; 19: 1023
   PubMed Web of Science ®Google Scholar
• Strubelt O. Alcohol potentation of liver injury. Fundam. Appl Toxicol. 1984; 4: 144
   PubMedGoogle Scholar
• Johansson I., Ingelman-Sundberg M. Carbon tetrachloride-induced lipid peroxidation dependent on an ethanol-inducible form of rabbit liver microsomal cytochrome P450. FEBS Lett. 1985; 183: 265
   PubMed Web of Science ®Google Scholar
• Ekström G., Von Bahr C., Ingelman-Sundberg M. Human liver microsomal cytochrome P450IIE1. Immunological evaluation of its contribution to microsomal ethanol oxidation, carbon tetrachloride reduction and NADPH oxidase activity. Biochem. Pharmacol. 1989; 38: 689
   PubMed Web of Science ®Google Scholar
• Hiad B., Moody D. E., Woo C. H., Smuckler E. A. Alterations of specific forms of cytochrome P450 in rat liver during acute carbon tetrachloride intoxication. Toxicol. Appl. Pharmacol. 1981; 61: 286
   PubMed Web of Science ®Google Scholar
• Stier A. Trifluoroacetic acid as metabolite of halothane. Biochem. Pharmacol. 1964; 13: 1544
   PubMed Web of Science ®Google Scholar
• Tomasi A., Billing S., Garner A., Slater T. F., Albano E. The metabolism of halothane by hepatocytes: a comparison between free radical spin trapping and lipid peroxidation in relation to cell damage. Chem. Biol. Interact. 1983; 46: 353
   PubMed Web of Science ®Google Scholar
• Mukai S., Morio M., Fujii K., Hanaki C. Volatile metabolites of halothane in the rabbit. Anaesthesiology 1977; 47: 248
   PubMed Web of Science ®Google Scholar
• Manno M., Cazzaro S., Rezzadore M. The mechanism of the suicidal reductive inactivation of microsomal cytochrome P450 by halothane. Arch. Toxicol. 1991; 65: 191
   PubMed Web of Science ®Google Scholar
• Akita S., Kawahara M., Takeshita T., Morio M., Fuji K. Halothane-induced hepatic microsomal lipid peroxidation in guinea pigs and rats. J. Appl. Toxicol. 1989; 9: 9
   PubMed Web of Science ®Google Scholar
• Baker M. T., Vasquiz M. T., Chiang C. K. Evidence for the stability and cytochrome P450 specificity of the phenobarbital induced reductive halothane-cytochrome P450 complex formed in rat hepatic microsomes. Biochem. Pharmacol. 1991; 41: 1691
   PubMed Web of Science ®Google Scholar
• Johnson R. F., Zenhausern A., Zollingen H. Azo dyes. Kirk-Othmer Encyclopedia of Chemical Technology, Vol 2, 2nd ed, H. F. Mark, J. J. McKetta, Jr., D. F. Othmer, A. Standen. John Wiley & Sons, New York 1978; 686
   Google Scholar
• Levine W. G. Metabolism of azodyes: implication for detoxication and activation. Drug Metab. Rev. 1991; 23: 253
   PubMed Web of Science ®Google Scholar
• Martin C. N., Kennelly J. C. Rat liver microsomal azoreductase activity of four azodyes derived from benzidine, 3,3′-dimethylbenzidine or 3,3′-dimethoxybenzidine. Carcinogenesis 1981; 2: 307
   PubMed Web of Science ®Google Scholar
• Huang M. T., Miwa G. T., Cronheim N., Lu A. Y. H. Rat liver cytosolic azoreductase, electron transport properties and the mechanism of dicumarol inhibition of the purified enzyme. J. Biol Chem. 1979; 254: 11223
   PubMed Web of Science ®Google Scholar
• Chung K. T., Stevens S. E., Cerniglia C. E. The reduction of azodyes by the intestinal microflora. Crit. Rev. Microbiol. 1992; 18: 175
   PubMed Web of Science ®Google Scholar
• Kitamura S., Tatsumi K. Azoreductive activity of aldehyde oxidase. Chem. Pharm. Bull. 1983; 31: 3334
   PubMed Web of Science ®Google Scholar
• Hernandez P. H., Mazel P., Gillette J. R. Studies on the mechanism of action of mammalian hepatic reductase II. The effect of phenobarbital and 3-methylcholanthrene on carbon monoxide sensitive and insensitive azoreductase activities. Biochem. Pharmacol. 1967; 16: 1877
   PubMed Web of Science ®Google Scholar
• Levine W. G., Raza H. Mechanisms of azoreduction of dimethylaminoazobenzene by rat liver NADPH-cytochrome P450 reductase and partially purified cytochrome P450. Oxygen and carbon monoxide sensitivity and stimulation by FAD and FMN. Drug Metab. Dispos. 1988; 16: 441
   PubMed Web of Science ®Google Scholar
• Peterson F. J., Holtzman J. L., Crankshaw D., Mason R. P. Two sites of azoreduction in the monooxygenase system. Mol. Pharmacol. 1989; 34: 597
   Web of Science ®Google Scholar
• Levine W. G., Zbaida S. Two classes of azodye reductase activity associated with rat liver microsomal cytochrome P450. Adv. Exp. Med. Biol. 1991; 283: 315
   PubMedGoogle Scholar
• Raza H., Levine W. G. Azoreduction ofN, N-dimethyl-4-aminoazobenzene (DAB) by rat hepatic microsomes. Selective induction by clofibrate. Drug Metab. Dispos. 1986; 41: 19
   Google Scholar
• Levine W. G., Stoddart A., Zbaida S. Multiple mechanisms in hepatic microsomal azoreduction. Xenobiotica 1992; 22: 1111
   PubMed Web of Science ®Google Scholar
• Testa B., Jenner P. Inhibitors of cytochrome P450 and their mechanism of action. Drug. Met. Rev. 1981; 12: 1
   PubMed Web of Science ®Google Scholar
• Newson S., Eastring R., Bergman H., Roth R. Inhibition of benzo(a)pyrene monooxygenase by α-naphthoflavone may be partially mediated by the metabolite 9-hydroxy-α-naphthoflavone. Toxicol. Lett. 1982; 14: 7
   PubMed Web of Science ®Google Scholar
• Zbaida S., Stoddart A. M., Levine W. G. Studies on the mechanism of reduction of azodye carcinogens by rat liver microsomal cytochrome P450. Chem. Biol. Interact. 1989; 69: 61
   PubMed Web of Science ®Google Scholar
• Zbaida S., Levine W. G. Role of electronic factors in binding and reduction of azo dyes by hepatic microsomes. J. Pharmacol. Exp. Therapeut. 1992; 260: 554
   PubMed Web of Science ®Google Scholar
• Zbaida S., Levine W. G. A novel application of cyclic voltammetry for direct investigation of metabolic intermediates in microsomal azoreduction. Chem. Res. Toxicol. 1991; 4: 82
   PubMed Web of Science ®Google Scholar
• Mason R. P., Peterson F. J., Holtzman J. L. Inhibition of azoreductase by oxygen. The role of the azo anion free radical metabolite in the reduction of oxygen to superoxide. Mol. Pharmacol. 1978; 14: 661
   Web of Science ®Google Scholar
• Powis G. Free radical formation by antitumor quinones. Free Rad. Biol. Med. 1989; 6: 63
   PubMed Web of Science ®Google Scholar
• Powis G. Metabolism and reactions of quinoid anticancer agents. Pharmac. Ther. 1987; 35: 57
   PubMed Web of Science ®Google Scholar
• O'Brien P. J. Molecular mechanisms of quinone cytotoxicity. Chem. Biol. Interact. 1991; 80: 1
   PubMed Web of Science ®Google Scholar
• Sinha B. K. Free radicals in anticancer drug pharmacology. Chem. Biol. Interact. 1989; 69: 293
   PubMed Web of Science ®Google Scholar
• Svingen B. A., Powis G. Pulse radiolysis studies of antitumor quinones: radical lifetimes, reactivity with oxygen, and one-electron reduction potentials. Arch. Biochem. Biophys. 1981; 209: 119
   PubMed Web of Science ®Google Scholar
• Traver R. D., Horikoshi T., Danenberg K. D., Stadlbauer T. H. W., Danenberg P. V., Ross D., Gibson N. W. NAD(P)H: quino oxidoreductase gene expression in human colon carcinoma cells: characterization of a mutant which modulates DT-diaphorase activity and mitomycin C sensitivity. Cancer Res. 1992; 52: 797
   PubMed Web of Science ®Google Scholar
• Odom A. L., Hatwig C. A., Stanley J. S., Benson A. M. Biochemical determinants of adriamycin toxicity in mouse liver, heart and intestine. Biochem. Pharmacol. 1992; 43: 831
   PubMed Web of Science ®Google Scholar
• Kalyanaraman B., Perez-Reyes E., Mason R. P. Spin-trapping and direct electron spin resonance investigations of the redox metabolism of quinone anticancer drugs. Biochim. Biophys. Acta 1980; 630: 119
   PubMed Web of Science ®Google Scholar
• Gustafson D. L., Swanson J. D., Pristos C. A. Role of xanthine oxidase in the potentation of doxorubicin-induced cardiotoxicity by mitomycin C. Cancer Commun. 1991; 3: 299
   PubMed Web of Science ®Google Scholar
• Powis G., Appel P. L. Relationship of the single-electron reduction potentials of quinones to their reduction by flavoproteins. Biochem. Pharmacol. 1980; 29: 2567
   PubMed Web of Science ®Google Scholar
• Doroshow J. Role of hydrogen peroxide and hydroxyl formation in the killing of Ehrlich cancer cell by antitumor quinones. Proc. Natl. Acad. Sci. U.S.A. 1986; 83: 4514
   PubMed Web of Science ®Google Scholar
• Bachur N. R., Gordon S. L., Gee M. V., Kon H. NADPH-cytochrome P450 reductase activation of quinone anticancer agents to free radicals. Proc. Natl. Acad. Sci. U.S.A. 1979; 76: 954
   PubMed Web of Science ®Google Scholar
• Nakamura Y., Ohtaki S., Makino R., Tanaka T., Ishimura Y. Superoxide anion in the initial product in the hydrogen peroxide formation catalyzed by NADPH oxidase in porcine thyroid plasma membrane. J. Biol. Chem. 1989; 264: 4759
   PubMed Web of Science ®Google Scholar
• Gutteridge J. M. Iron promoters of the Fenton reaction and lipid peroxidation can be released from haemoglobin by peroxides. FEBS Lett. 1986; 201: 291
   PubMed Web of Science ®Google Scholar
• Rumyantseva G. V., Weiner L. M. Redox transformations of quinone antitumor drugs in liver microsomes. FEBS Lett. 1988; 234: 459
   PubMed Web of Science ®Google Scholar
• Fisher G. R., Brown J. R., Patterson L. H. Involvement of hydroxyl radical formation and DNA strand breakage in the cytotoxicity of anthraquinone antitumor agents. Free Rad. Res. Commun. 1990; 11: 117
   PubMed Web of Science ®Google Scholar
• Rumyantseva G. V., Weiner L. M., Frolova E. I., Fedorova O. S. Hydroxyl radical generation and DNA strand scission mediated by natural anticancer and synthetic quinones. FEBS Lett. 1989; 242: 397
   PubMed Web of Science ®Google Scholar
• Blount S., Griffiths H. R., Lunec J. Reactive oxygen species induce antigenic changes in DNA. FEBS Lett. 1989; 245: 100
   PubMed Web of Science ®Google Scholar
• Chatterjee S. N., Agarwal S., Jana A. K., Bose B. Membrane lipid peroxidation and its pathological consequences. Indian J. Biochem. Biophys. 1988; 25: 25
   PubMed Web of Science ®Google Scholar
• Mimnaugh E. G., Trush M. A., Gram T. E. A possible role for membrane lipid peroxidation in anthracycline nephrotoxicity. Biochem. Pharmacol. 1986; 35: 4327
   PubMed Web of Science ®Google Scholar
• Vaca C. E., Harms-Ringdahl M. Nuclear membrane lipid peroxidation products bind to nuclear macromolecules. Arch. Biochem. Biophys. 1989; 269: 548
   PubMed Web of Science ®Google Scholar
• Hauptlorenz S., Esterbauer H., Mol W., Rumpoll R., Schauenstein E., Puschendorf B. Effects of the lipid peroxidation product 4-hydroxynonenal and related aldehyde on proliferation and viability of cultured Ehrlich ascites tumor cells. Biochem. Pharmacol. 1985; 34: 3803
   PubMed Web of Science ®Google Scholar
• Docampo R., Moreno S. N. J. The metabolism and mode of action of gentian violet. Drug Metab. Rev. 1990; 22: 161
   PubMed Web of Science ®Google Scholar
• Thomas S. M., MacPhee D. G. Crystal violet: a direct-acting frameshift mutagen whose mutagenicity is enhanced by mammalian metabolism. Mutat. Res. 1984; 140: 165
   PubMed Web of Science ®Google Scholar
• Harrelson W. G., Mason R. P. Microsomal reduction of gentian violet; evidence for cytochrome P-450-catalyzed free radical formation. Mol. Pharmacol. 1982; 22: 239
   PubMed Web of Science ®Google Scholar
• Harrelson W. G., Jr., Mason R. P. Microsomal reduction of gentian violet. Evidence for cytochrome P450 catalyzed free radical formation. Mol. Pharmacol. 1982; 22: 239
   PubMed Web of Science ®Google Scholar
• McDonald J. J., Cerniglia C. E. Biotransformation of gentian violet to leucogentian violet by human, rat, and chicken intestinal flora. Drug Metab. Dispos. 1984; 12: 330
   PubMed Web of Science ®Google Scholar
• Tokiwa H., Nakagawa R., Horikawa K. Mutagenic/carcinogenic agents in indoor pollutants. The dinitropyrene generated by kerosene heaters and fuel gas and liquified petroleum gas burner. Mutat. Res. 1985; 157: 39
   PubMed Web of Science ®Google Scholar
• Sweetman J. A., Zielinska B., Atkinson R., Randhal T., Winer A. M., Pitts J. N, Jr. A possible formation pathway for the 2-nitrofluoranthene observed in ambient particulate organic matter. Atmos. Environ. 1986; 20: 235
   Web of Science ®Google Scholar
• Pitts J. N., Jr., Van Cauwenberghe R. A., Grosjean D., Schmid J. P., Fitz D. R., Beeser W. L., Jr., Knudson G. B., Hunds P. M. Atmospheric reactions of polycyclic aromatic hydrocarbons: facile formation of mutagenic nitro derivatives. Science 1979; 202: 515
   Web of Science ®Google Scholar
• Zielinska B., Harger W. P., Arey J., Winer A. M., Haar R. A., Hanson C. V. The mutagenicity of 2-nitrofluoranthene and its in vitro hepatic metabolites. Mutat. Res. 1987; 190: 259
   PubMed Web of Science ®Google Scholar
• Dubin M., Villamil S. H. F., De Blumefeld M. P., Stoppani A. O. M. Inhibition of microsomal lipid peroxidation and cytochrome P450-catalyzed reactions by nitrofuran compounds. Free Rad. Res. Commun. 1991; 14: 419
   PubMed Web of Science ®Google Scholar
• Masana M., De Toranzo E. G. D., Castro J. A. Reductive metabolism and activation of benznidazole. Biochem. Pharmacol. 1984; 33: 1041
   PubMed Web of Science ®Google Scholar
• O'Brien P. J., Wong W. C., Silva J., Khan S. Toxicity of nitrobenzene compounds towards isolated hepatocytes: dependence on reduction potential. Xenobiotica 1990; 20: 945
   PubMed Web of Science ®Google Scholar
• Mori M. A., Matsuhashi T., Miyahara T., Shibara S., Izima C., Kozuka H. Reduction of 2,4-dinitrotoluene by Wistar rat liver microsomal and cytosol fractions. Toxicol. Appl. Pharmacol. 1984; 76: 105
   PubMed Web of Science ®Google Scholar
• Lloyd R. V., Duling D. R., Rumyantseva G. V., Mason R. P., Bridson P. K. Microsomal reduction of 3-amine-1,2,4-benzotriazine 1,4-dioxide to a free radical. Mol. Pharmacol. 1991; 40: 440
   PubMed Web of Science ®Google Scholar
• Tatsumi K., Kitamura S., Narai N. Reductive metabolism of aromatic nitro compounds including carcinogens by rabbit liver preparations. Cancer Res. 1986; 46: 1089
   PubMed Web of Science ®Google Scholar
• Belisaria M. A., Pecce R., Dalla Morte R., Arena A. R., Cecinato A., Ciccioli P., Stainno N. Characterization of oxidative and reductive metabolism in vitro of nitrofluor-anthenes by rat liver enzymes. Carcinogenesis 1990; 11: 214
   Web of Science ®Google Scholar
• Saito K., Kamataki T., Kato R. Participation of cytochrome P450 in the reductive metabolism of 1-nitropyrene by rat liver microsomes. Cancer Res. 1984; 44: 3169
   PubMed Web of Science ®Google Scholar
• Harada N., Omura T. Participation of cytochrome P450 in the reduction of nitro compounds by rat liver microsomes. J. Biochem. 1980; 87: 1539
   PubMed Web of Science ®Google Scholar
• Gilette J. R., Kamm J. J., Sasame H. A. Mechanism of p-nitrobenzoate reduction in liver: the possible role of cytochrome P450 in liver microsomes. Mol. Pharmacol. 1968; 4: 541
   PubMed Web of Science ®Google Scholar
• Mason R. P., Josephy P. S. Free Radical Mechanism of Nitroreductase. Toxicity of Nitro-aromatic Compounds, D. E. Rickert. Hemisphere, Washington, D.C. 1985; 121
   Google Scholar
• Corbett M. D., Corbelt B. R. Metabolism of 4-chloronitrobenzene by die yeast. Rhodosporidium sp., Appl. Environ. Microbiol. 1981; 41: 942
   PubMed Web of Science ®Google Scholar
• Mermelstein R., Kiriazide D. K., Butter M., McCoy E. C., Rozenkranz H. S. The extraordinary mutagenicity of nitropyrenes in bacteria. Mutat. Res. 1981; 89: 187
   PubMed Web of Science ®Google Scholar
• Takayama S., Tanaka M., Katoh Y., Terada M., Sugimaura T. Mutagenicity of nitropyrenes in Chinese hamster V79 cells. Gann 1983; 74: 338
   PubMedGoogle Scholar
• Nachtman J. P., Wolff S. Activity of nitropolynuclear aromatic hydrocarbons in the sister chromatid exchange assay with and without metabolic activation. Environ. Mutagen. 1982; 4: 1
   PubMedGoogle Scholar
• Campbell J., Crumplin G. C., Garner J. V., Garner R. C., Martin C. M., Rutler A. Nitrated polycyclic aromatic hydrocarbon: potent bacterial mutagens and stimulators of DNA synthesis in cultured human cells. Carcinogenesis 1981; 2: 559
   PubMed Web of Science ®Google Scholar
• Hirose M., Lee M., Vaught J. B., Wang C. Y., King C. M. Carcinogenicity and metabolic activation of 1-nitropyrene. Proc. Am. Assoc. Cancer Res. 1983; 24: 83
   Google Scholar
• Hong J., Pan J., Gonzales F. J., Gelboin H. V., Yang C. S. The induction of a specific form of cytochrome P450 (P450j) by fasting. Biochem. Biophys. Res. Commun. 1987; 142: 1077
   PubMed Web of Science ®Google Scholar
• Koymans L., Donné-Op den Kelder G. M., Te Koppele J. M., Vermeulen N. P. E. Cytochromes P450: Their active-site stracture and mechanism of oxidation. Drug. Metab. Rev. 1993; 25: 325
   PubMed Web of Science ®Google Scholar
• Poulos T. L., Finzel B. C., Howard A. J. Crystal structure of substrate-freePseudomonas putida cytochrome P450. Biochemistry 1986; 25: 5314
   PubMed Web of Science ®Google Scholar
• Poulos T. L., Finzel B. C., Howard A. J. High-resolution crystal structure of cytochrome P450cam. J. Mol. Biol. 1987; 195: 687
   PubMed Web of Science ®Google Scholar
• Murray M., Reidy G. F. Selectivity in the inhibition of mammalian cytochromes P450 by chemical agents. Pharmacol. Rev. 1990; 42: 85
   PubMed Web of Science ®Google Scholar