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Volumn 51, Issue 50, 2012, Pages 9995-10007

Oxidation of methyl and ethyl nitrosamines by cytochrome P450 2E1 and 2B1

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; C-H BOND; CATALYTIC EFFICIENCIES; CYTOCHROME P450; DENITROSATION; DEUTERIUM ISOTOPE EFFECT; GENERAL PATTERNS; INTRINSIC KINETICS; LAG PHASE; MINOR PRODUCTS; N-NITROSODIMETHYLAMINE; PROCESSIVITY; RAT LIVER MICROSOMES; RATE LIMITING; SINGLE MOLECULE;

EID: 84871260739     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi301092c     Document Type: Article
Times cited : (54)

References (67)
  • 2
    • 0002211689 scopus 로고
    • Detoxication enzymes
    • In (Jakoby, W. B. Ed.) Vol. pp, Academic Press, New York.
    • Jakoby, W. B. (1980) Detoxication enzymes. In Enzymatic Basis of Detoxication (Jakoby, W. B., Ed.) Vol. 1, pp 1-6, Academic Press, New York.
    • (1980) Enzymatic Basis of Detoxication , vol.1 , pp. 1-6
    • Jakoby, W.B.1
  • 3
    • 84892246340 scopus 로고    scopus 로고
    • Human cytochrome P450 enzymes
    • In (Ortiz de Montellano, P. R. Ed.) 3rd ed. pp, Kluwer Academic/Plenum Press, New York.
    • Guengerich, F. P. (2005) Human cytochrome P450 enzymes. In Cytochrome P450: Structure, Mechanism, and Biochemistry (Ortiz de Montellano, P. R., Ed.) 3rd ed., pp 377-530, Kluwer Academic/Plenum Press, New York.
    • (2005) Cytochrome P450: Structure, Mechanism, and Biochemistry , pp. 377-530
    • Guengerich, F.P.1
  • 4
    • 0001315679 scopus 로고
    • The metabolism of 4-dimethylaminoazobenzene by rat liver homogenates
    • Mueller, G. C. and Miller, J. A. (1948) The metabolism of 4-dimethylaminoazobenzene by rat liver homogenates J. Biol. Chem. 176, 535-544
    • (1948) J. Biol. Chem. , vol.176 , pp. 535-544
    • Mueller, G.C.1    Miller, J.A.2
  • 5
    • 0034097234 scopus 로고    scopus 로고
    • Metabolism of chemical carcinogens
    • Guengerich, F. P. (2000) Metabolism of chemical carcinogens Carcinogenesis 21, 345-351
    • (2000) Carcinogenesis , vol.21 , pp. 345-351
    • Guengerich, F.P.1
  • 6
    • 84863920443 scopus 로고    scopus 로고
    • Contributions of human enzymes in carcinogen metabolism
    • Rendic, S. and Guengerich, F. P. (2012) Contributions of human enzymes in carcinogen metabolism Chem. Res. Toxicol. 25, 1316-1383
    • (2012) Chem. Res. Toxicol. , vol.25 , pp. 1316-1383
    • Rendic, S.1    Guengerich, F.P.2
  • 7
    • 0014757218 scopus 로고
    • Carcinogenesis by chemicals: An overview. G.H.A. Clowes Memorial Lecture
    • Miller, J. A. (1970) Carcinogenesis by chemicals: An overview. G.H.A. Clowes Memorial Lecture Cancer Res. 30, 559-576
    • (1970) Cancer Res. , vol.30 , pp. 559-576
    • Miller, J.A.1
  • 8
    • 38949094492 scopus 로고    scopus 로고
    • Cytochrome P450 and chemical toxicology
    • Guengerich, F. P. (2008) Cytochrome P450 and chemical toxicology Chem. Res. Toxicol. 21, 70-83
    • (2008) Chem. Res. Toxicol. , vol.21 , pp. 70-83
    • Guengerich, F.P.1
  • 9
    • 0011278203 scopus 로고
    • N -Nitroso carcinogens in the environment
    • In (Searle, C. E. Ed.) 2nd ed. Vol. pp, American Chemical Society, Washington, DC.
    • Preussmann, R. and Eisenbrand, G. (1984) N -Nitroso carcinogens in the environment. In Chemical Carcinogens (Searle, C. E., Ed.) 2nd ed., Vol. 2, pp 829-868, American Chemical Society, Washington, DC.
    • (1984) Chemical Carcinogens , vol.2 , pp. 829-868
    • Preussmann, R.1    Eisenbrand, G.2
  • 10
    • 38949170926 scopus 로고    scopus 로고
    • Progress and challenges in selected areas of tobacco carcinogenesis
    • Hecht, S. S. (2008) Progress and challenges in selected areas of tobacco carcinogenesis Chem. Res. Toxicol. 21, 160-171
    • (2008) Chem. Res. Toxicol. , vol.21 , pp. 160-171
    • Hecht, S.S.1
  • 12
    • 0026744568 scopus 로고
    • Cytochrome P450 2E1 and 2A6 enzymes as major catalysts for metabolic activation of N -nitrosodialkylamines and tobacco-related nitrosamines in human liver microsomes
    • Yamazaki, H., Inui, Y., Yun, C.-H., Mimura, M., Guengerich, F. P., and Shimada, T. (1992) Cytochrome P450 2E1 and 2A6 enzymes as major catalysts for metabolic activation of N -nitrosodialkylamines and tobacco-related nitrosamines in human liver microsomes Carcinogenesis 13, 1789-1794
    • (1992) Carcinogenesis , vol.13 , pp. 1789-1794
    • Yamazaki, H.1    Inui, Y.2    Yun, C.-H.3    Mimura, M.4    Guengerich, F.P.5    Shimada, T.6
  • 13
    • 0025179176 scopus 로고
    • Human cytochrome P450IIA3: CDNA sequence, role of the enzyme in the metabolic activation of promutagens, comparison to nitrosamine activation by human cytochrome P450IIE1
    • Crespi, C. L., Penman, B. W., Leakey, J. A. E., Arlotto, M. P., Stark, A., Parkinson, A., Turner, T., Steimel, D. T., Rudo, K., Davies, R. L., and Langenbach, R. (1990) Human cytochrome P450IIA3: cDNA sequence, role of the enzyme in the metabolic activation of promutagens, comparison to nitrosamine activation by human cytochrome P450IIE1 Carcinogenesis 11, 1293-1300
    • (1990) Carcinogenesis , vol.11 , pp. 1293-1300
    • Crespi, C.L.1    Penman, B.W.2    Leakey, J.A.E.3    Arlotto, M.P.4    Stark, A.5    Parkinson, A.6    Turner, T.7    Steimel, D.T.8    Rudo, K.9    Davies, R.L.10    Langenbach, R.11
  • 14
    • 0025848338 scopus 로고
    • A tobacco smoke-derived nitrosamine, 4-(methylnitrosamino)-1-(3-pyridyl)- 1-butanone, is activated by multiple human cytochrome P450s including the polymorphic human cytochrome P4502D6
    • Crespi, C. L., Penman, B. W., Gelboin, H. V., and Gonzalez, F. J. (1991) A tobacco smoke-derived nitrosamine, 4-(methylnitrosamino)-1-(3-pyridyl)-1- butanone, is activated by multiple human cytochrome P450s including the polymorphic human cytochrome P4502D6 Carcinogenesis 12, 1197-1201
    • (1991) Carcinogenesis , vol.12 , pp. 1197-1201
    • Crespi, C.L.1    Penman, B.W.2    Gelboin, H.V.3    Gonzalez, F.J.4
  • 15
    • 77950908768 scopus 로고    scopus 로고
    • Oxidation of N -nitrosodimethylamine and N -nitrosodiethylamine by human cytochrome P450 2A6: Sequential oxidation to carboxylic acids and analysis of reaction steps
    • Chowdhury, G., Calcutt, M. W., and Guengerich, F. P. (2010) Oxidation of N -nitrosodimethylamine and N -nitrosodiethylamine by human cytochrome P450 2A6: Sequential oxidation to carboxylic acids and analysis of reaction steps J. Biol. Chem. 285, 8031-8044
    • (2010) J. Biol. Chem. , vol.285 , pp. 8031-8044
    • Chowdhury, G.1    Calcutt, M.W.2    Guengerich, F.P.3
  • 16
    • 0022342407 scopus 로고
    • Demethylation and denitrosation of nitrosamines by cytochrome P-450 isozymes
    • Tu, Y. Y. and Yang, C. S. (1985) Demethylation and denitrosation of nitrosamines by cytochrome P-450 isozymes Arch. Biochem. Biophys. 242, 32-40
    • (1985) Arch. Biochem. Biophys. , vol.242 , pp. 32-40
    • Tu, Y.Y.1    Yang, C.S.2
  • 18
    • 37049019073 scopus 로고    scopus 로고
    • Role of CYP2E1 in diethylnitrosamine-induced hepatocarcinogenesis in vivo
    • Kang, J. S., Wanibuchi, H., Morimura, K., Gonzalez, F. J., and Fukushima, S. (2007) Role of CYP2E1 in diethylnitrosamine-induced hepatocarcinogenesis in vivo Cancer Res. 67, 11141-11146
    • (2007) Cancer Res. , vol.67 , pp. 11141-11146
    • Kang, J.S.1    Wanibuchi, H.2    Morimura, K.3    Gonzalez, F.J.4    Fukushima, S.5
  • 19
    • 0015786351 scopus 로고
    • Deuterium isotope effect on the carcinogenicity of dimethylnitrosamine in rat liver
    • Keefer, L. K., Lijinsky, W., and Garcia, H. (1973) Deuterium isotope effect on the carcinogenicity of dimethylnitrosamine in rat liver J. Natl. Cancer Inst. 51, 299-302
    • (1973) J. Natl. Cancer Inst. , vol.51 , pp. 299-302
    • Keefer, L.K.1    Lijinsky, W.2    Garcia, H.3
  • 20
    • 0023194618 scopus 로고
    • Deuterium isotope effect on denitrosation and demethylation of N -nitrosodimethylamine by rat liver microsomes
    • Wade, D., Yang, C. S., Metral, C. J., Roman, J. M., Hrabie, J. A., Riggs, C. W., Anjo, T., Keefer, L. K., and Mico, B. A. (1987) Deuterium isotope effect on denitrosation and demethylation of N -nitrosodimethylamine by rat liver microsomes Cancer Res. 47, 3373-3377
    • (1987) Cancer Res. , vol.47 , pp. 3373-3377
    • Wade, D.1    Yang, C.S.2    Metral, C.J.3    Roman, J.M.4    Hrabie, J.A.5    Riggs, C.W.6    Anjo, T.7    Keefer, L.K.8    Mico, B.A.9
  • 22
    • 26944462419 scopus 로고    scopus 로고
    • Structures of human microsomal cytochrome P450 2A6 complexed with coumarin and methoxsalen
    • Yano, J. K., Hsu, M. H., Griffin, K. J., Stout, C. D., and Johnson, E. F. (2005) Structures of human microsomal cytochrome P450 2A6 complexed with coumarin and methoxsalen Nat. Struct. Biol. 12, 822-823
    • (2005) Nat. Struct. Biol. , vol.12 , pp. 822-823
    • Yano, J.K.1    Hsu, M.H.2    Griffin, K.J.3    Stout, C.D.4    Johnson, E.F.5
  • 23
    • 57749122048 scopus 로고    scopus 로고
    • Structures of human cytochrome P-450 2E1. Insights into the binding of inhibitors and both small molecular weight and fatty acid substrates
    • Porubsky, P. R., Meneely, K. M., and Scott, E. E. (2008) Structures of human cytochrome P-450 2E1. Insights into the binding of inhibitors and both small molecular weight and fatty acid substrates J. Biol. Chem. 283, 33698-33707
    • (2008) J. Biol. Chem. , vol.283 , pp. 33698-33707
    • Porubsky, P.R.1    Meneely, K.M.2    Scott, E.E.3
  • 24
    • 84864531088 scopus 로고    scopus 로고
    • Nicotine and 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone binding and access channel in human cytochrome P450 2A6 and 2A13 enzymes
    • Devore, N. M. and Scott, E. E. (2012) Nicotine and 4-(methylnitrosamino)- 1-(3-pyridyl)-1-butanone binding and access channel in human cytochrome P450 2A6 and 2A13 enzymes J. Biol. Chem. 287, 26576-26585
    • (2012) J. Biol. Chem. , vol.287 , pp. 26576-26585
    • Devore, N.M.1    Scott, E.E.2
  • 25
    • 0017409770 scopus 로고
    • Separation and purification of multiple forms of microsomal cytochrome P-450. Activities of different forms of cytochrome P-450 towards several compounds of environmental interest
    • Guengerich, F. P. (1977) Separation and purification of multiple forms of microsomal cytochrome P-450. Activities of different forms of cytochrome P-450 towards several compounds of environmental interest J. Biol. Chem. 252, 3970-3979
    • (1977) J. Biol. Chem. , vol.252 , pp. 3970-3979
    • Guengerich, F.P.1
  • 26
    • 0020434524 scopus 로고
    • Purification and characterization of liver microsomal cytochromes P-450: Electrophoretic, spectral, catalytic, and immunochemical properties and inducibility of eight isozymes isolated from rats treated with phenobarbital or β-naphthoflavone
    • Guengerich, F. P., Dannan, G. A., Wright, S. T., Martin, M. V., and Kaminsky, L. S. (1982) Purification and characterization of liver microsomal cytochromes P-450: Electrophoretic, spectral, catalytic, and immunochemical properties and inducibility of eight isozymes isolated from rats treated with phenobarbital or β-naphthoflavone Biochemistry 21, 6019-6030
    • (1982) Biochemistry , vol.21 , pp. 6019-6030
    • Guengerich, F.P.1    Dannan, G.A.2    Wright, S.T.3    Martin, M.V.4    Kaminsky, L.S.5
  • 27
    • 3042553224 scopus 로고    scopus 로고
    • Structure of mammalian cytochrome P450 2B4 complexed with 4-(4-chlorophenyl)imidazole at 1.9-Å resolution: Insight into the range of P450 conformations and the coordination of redox partner binding
    • Scott, E. E., White, M. A., He, Y. A., Johnson, E. F., Stout, C. D., and Halpert, J. R. (2004) Structure of mammalian cytochrome P450 2B4 complexed with 4-(4-chlorophenyl)imidazole at 1.9-Å resolution: Insight into the range of P450 conformations and the coordination of redox partner binding J. Biol. Chem. 279, 27294-27301
    • (2004) J. Biol. Chem. , vol.279 , pp. 27294-27301
    • Scott, E.E.1    White, M.A.2    He, Y.A.3    Johnson, E.F.4    Stout, C.D.5    Halpert, J.R.6
  • 28
    • 41849149011 scopus 로고    scopus 로고
    • Analysis and characterization of enzymes and nucleic acids
    • In (Hayes, A. W. Ed.) 5th ed. pp, CRC Press, Boca Raton, FL.
    • Guengerich, F. P. and Bartleson, C. J. (2007) Analysis and characterization of enzymes and nucleic acids. In Principles and Methods of Toxicology (Hayes, A. W., Ed.) 5th ed., pp 1981-2048, CRC Press, Boca Raton, FL.
    • (2007) Principles and Methods of Toxicology , pp. 1981-2048
    • Guengerich, F.P.1    Bartleson, C.J.2
  • 29
    • 77955294012 scopus 로고    scopus 로고
    • Mitochondria-targeted cytochrome P450 2E1 preferentially induces oxidative damage and augments alcohol mediated mitochodrial dysfunction in cultured cells
    • Bansal, S., Liu, C.-P., Sepuri, N. B. V., Anandatheerthavarada, H. K., Guengerich, F. P., and Avadhani, N. G. (2010) Mitochondria-targeted cytochrome P450 2E1 preferentially induces oxidative damage and augments alcohol mediated mitochodrial dysfunction in cultured cells J. Biol. Chem. 285, 24609-24619
    • (2010) J. Biol. Chem. , vol.285 , pp. 24609-24619
    • Bansal, S.1    Liu, C.-P.2    Sepuri, N.B.V.3    Anandatheerthavarada, H.K.4    Guengerich, F.P.5    Avadhani, N.G.6
  • 30
    • 0028023169 scopus 로고
    • Expression of modified human cytochrome P450 2E1 in Escherichia coli, purification, and spectral and catalytic properties
    • Gillam, E. M. J., Guo, Z., and Guengerich, F. P. (1994) Expression of modified human cytochrome P450 2E1 in Escherichia coli, purification, and spectral and catalytic properties Arch. Biochem. Biophys. 312, 59-66
    • (1994) Arch. Biochem. Biophys. , vol.312 , pp. 59-66
    • Gillam, E.M.J.1    Guo, Z.2    Guengerich, F.P.3
  • 31
    • 0031822496 scopus 로고    scopus 로고
    • Role of the alanine at position 363 of cytochrome P450 2B2 in influencing the NADPH- and hydroperoxide-supported activities
    • Hanna, I. H., Teiber, J. F., Kokones, K. L., and Hollenberg, P. F. (1998) Role of the alanine at position 363 of cytochrome P450 2B2 in influencing the NADPH- and hydroperoxide-supported activities Arch. Biochem. Biophys. 350, 324-332
    • (1998) Arch. Biochem. Biophys. , vol.350 , pp. 324-332
    • Hanna, I.H.1    Teiber, J.F.2    Kokones, K.L.3    Hollenberg, P.F.4
  • 32
    • 78651165715 scopus 로고
    • The carbon monoxide-binding pigment of liver microsomes. I. Evidence for its hemoprotein nature
    • Omura, T. and Sato, R. (1964) The carbon monoxide-binding pigment of liver microsomes. I. Evidence for its hemoprotein nature J. Biol. Chem. 239, 2370-2378
    • (1964) J. Biol. Chem. , vol.239 , pp. 2370-2378
    • Omura, T.1    Sato, R.2
  • 34
    • 0027294648 scopus 로고
    • Examination of α-carbonyl derivatives of nitrosodimethylamine and ethylnitrosomethylamine as putative proximate carcinogens
    • Elespuru, R. K., Saavedra, J. E., Kovatch, R. M., and Lijinsky, W. (1993) Examination of α-carbonyl derivatives of nitrosodimethylamine and ethylnitrosomethylamine as putative proximate carcinogens Carcinogenesis 14, 1189-1193
    • (1993) Carcinogenesis , vol.14 , pp. 1189-1193
    • Elespuru, R.K.1    Saavedra, J.E.2    Kovatch, R.M.3    Lijinsky, W.4
  • 35
    • 77049138167 scopus 로고
    • The colorimetric estimation of formaldehyde by means of the Hantzsch reaction
    • Nash, T. (1953) The colorimetric estimation of formaldehyde by means of the Hantzsch reaction Biochem. J. 55, 416-421
    • (1953) Biochem. J. , vol.55 , pp. 416-421
    • Nash, T.1
  • 36
    • 0033596310 scopus 로고    scopus 로고
    • Mechanism of aqueous decomposition of trichloroethylene oxide
    • Cai, H. and Guengerich, F. P. (1999) Mechanism of aqueous decomposition of trichloroethylene oxide J. Am. Chem. Soc. 121, 11656-11663
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 11656-11663
    • Cai, H.1    Guengerich, F.P.2
  • 37
    • 0023263168 scopus 로고
    • Nature of N -nitrosodimethylamine demethylase and its inhibitors
    • Yoo, J. S. H., Cheung, R. J., Patten, C. J., Wade, D., and Yang, C. S. (1987) Nature of N -nitrosodimethylamine demethylase and its inhibitors Cancer Res. 47, 3378-3383
    • (1987) Cancer Res. , vol.47 , pp. 3378-3383
    • Yoo, J.S.H.1    Cheung, R.J.2    Patten, C.J.3    Wade, D.4    Yang, C.S.5
  • 38
    • 0026546777 scopus 로고
    • Role of cytochrome P450 in the oxidation of glycerol by reconstituted systems and microsomes
    • Clejan, L. A. and Cederbaum, A. I. (1992) Role of cytochrome P450 in the oxidation of glycerol by reconstituted systems and microsomes FASEB J. 6, 765-770
    • (1992) FASEB J. , vol.6 , pp. 765-770
    • Clejan, L.A.1    Cederbaum, A.I.2
  • 39
    • 0020431639 scopus 로고
    • The nature of nitrosamine denitrosation by rat liver microsomes
    • Lorr, N. A., Tu, Y. Y., and Yang, C. S. (1982) The nature of nitrosamine denitrosation by rat liver microsomes Carcinogenesis 3, 1039-1043
    • (1982) Carcinogenesis , vol.3 , pp. 1039-1043
    • Lorr, N.A.1    Tu, Y.Y.2    Yang, C.S.3
  • 40
    • 84871260498 scopus 로고    scopus 로고
    • High-performance liquid chromatography for determination of N -nitrosodimethylamine in water
    • In, pp, Water Environment Federation, Alexandria, VA.
    • Cha, W., Nalinakumari, B., and Fox, P. (2006) High-performance liquid chromatography for determination of N -nitrosodimethylamine in water. In Proceedings of the Water Environment Federation, WEFTEC 2006, pp 889-900, Water Environment Federation, Alexandria, VA (http://www.environmental-expert.com/ Files/5306/articles/8712/065.pdf).
    • (2006) Proceedings of the Water Environment Federation, WEFTEC 2006 , pp. 889-900
    • Cha, W.1    Nalinakumari, B.2    Fox, P.3
  • 41
    • 0020345922 scopus 로고
    • Deuterium and tritium kinetic isotope effects on initial rates
    • Northrop, D. B. (1982) Deuterium and tritium kinetic isotope effects on initial rates Methods Enzymol. 87, 607-625
    • (1982) Methods Enzymol. , vol.87 , pp. 607-625
    • Northrop, D.B.1
  • 42
    • 0023180336 scopus 로고
    • Regulation of cytochrome P-450j, a high-affinity N -nitrosodimethylamine demethylase, in rat hepatic microsomes
    • Thomas, P. E., Bandiera, S., Maines, S. L., Ryan, D. E., and Levin, W. (1987) Regulation of cytochrome P-450j, a high-affinity N -nitrosodimethylamine demethylase, in rat hepatic microsomes Biochemistry 26, 2280-2289
    • (1987) Biochemistry , vol.26 , pp. 2280-2289
    • Thomas, P.E.1    Bandiera, S.2    Maines, S.L.3    Ryan, D.E.4    Levin, W.5
  • 43
    • 0016832598 scopus 로고
    • Steady-state analysis of kinetic isotope effects in enzymic reactions
    • Northrop, D. B. (1975) Steady-state analysis of kinetic isotope effects in enzymic reactions Biochemistry 14, 2644-2651
    • (1975) Biochemistry , vol.14 , pp. 2644-2651
    • Northrop, D.B.1
  • 44
    • 0000679208 scopus 로고    scopus 로고
    • Secondary deuterium kinetic isotope effects and transition state structure
    • Matsson, O. and Westaway, K. C. (1998) Secondary deuterium kinetic isotope effects and transition state structure Adv. Phys. Org. Chem. 31, 143-248
    • (1998) Adv. Phys. Org. Chem. , vol.31 , pp. 143-248
    • Matsson, O.1    Westaway, K.C.2
  • 45
    • 0038311604 scopus 로고    scopus 로고
    • Stereospecific deuterium substitution attenuates the tumorigenicity and metabolism of the tobacco-specific nitrosamine 4-(methylnitrosamino)-1-(3- pyridyl)-1-butanone (NNK)
    • Jalas, J. R., McIntee, E. J., Kenney, P. M., Upadhyaya, P., Peterson, L. A., and Hecht, S. S. (2003) Stereospecific deuterium substitution attenuates the tumorigenicity and metabolism of the tobacco-specific nitrosamine 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone (NNK) Chem. Res. Toxicol. 16, 794-806
    • (2003) Chem. Res. Toxicol. , vol.16 , pp. 794-806
    • Jalas, J.R.1    McIntee, E.J.2    Kenney, P.M.3    Upadhyaya, P.4    Peterson, L.A.5    Hecht, S.S.6
  • 46
    • 0023447643 scopus 로고
    • Kinetic isotope effects and 'metabolic switching' in cytochrome P450-catalyzed reactions
    • Miwa, G. T. and Lu, A. Y. H. (1987) Kinetic isotope effects and 'metabolic switching' in cytochrome P450-catalyzed reactions BioEssays 7, 215-219
    • (1987) BioEssays , vol.7 , pp. 215-219
    • Miwa, G.T.1    Lu, A.Y.H.2
  • 47
    • 0033588164 scopus 로고    scopus 로고
    • Kinetics of cytochrome P450 2E1-catalyzed oxidation of ethanol to acetic acid via acetaldehyde
    • Bell-Parikh, L. C. and Guengerich, F. P. (1999) Kinetics of cytochrome P450 2E1-catalyzed oxidation of ethanol to acetic acid via acetaldehyde J. Biol. Chem. 274, 23833-23840
    • (1999) J. Biol. Chem. , vol.274 , pp. 23833-23840
    • Bell-Parikh, L.C.1    Guengerich, F.P.2
  • 48
    • 0023146026 scopus 로고
    • Concurrent generation of methylamine and nitrite during denitrosation of N -nitrosodimethylamine by rat liver microsomes
    • Keefer, L. K., Anjo, T., Wade, D., Wang, T., and Yang, C. S. (1987) Concurrent generation of methylamine and nitrite during denitrosation of N -nitrosodimethylamine by rat liver microsomes Cancer Res. 47, 447-452
    • (1987) Cancer Res. , vol.47 , pp. 447-452
    • Keefer, L.K.1    Anjo, T.2    Wade, D.3    Wang, T.4    Yang, C.S.5
  • 52
    • 0017265342 scopus 로고
    • Dimethylnitrosamine-demethylase: Absence of increased enzyme catabolism and multiplicity of effector sites in repression. Hemoprotein involvement
    • Argus, M. F., Arcos, J. C., Pastor, K. M., Wu, B. C., and Venkatesan, N. (1976) Dimethylnitrosamine-demethylase: absence of increased enzyme catabolism and multiplicity of effector sites in repression. Hemoprotein involvement Chem.-Biol. Interact. 13, 127-140
    • (1976) Chem.-Biol. Interact. , vol.13 , pp. 127-140
    • Argus, M.F.1    Arcos, J.C.2    Pastor, K.M.3    Wu, B.C.4    Venkatesan, N.5
  • 54
    • 0026091599 scopus 로고
    • Quantitation of microsomal α-hydroxylation of the tobacco-specific nitrosamine, 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone
    • Peterson, L. A., Mathew, R., and Hecht, S. S. (1991) Quantitation of microsomal α-hydroxylation of the tobacco-specific nitrosamine, 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone Cancer Res. 51, 5495-5500
    • (1991) Cancer Res. , vol.51 , pp. 5495-5500
    • Peterson, L.A.1    Mathew, R.2    Hecht, S.S.3
  • 55
    • 0029740207 scopus 로고    scopus 로고
    • Effects of structure on the reactivity of α- hydroxydialkylnitrosamines in aqueous solutions
    • Mesic, M. and Fishbein, J. C. (1996) Effects of structure on the reactivity of α-hydroxydialkylnitrosamines in aqueous solutions J. Am. Chem. Soc. 118, 7412-7413
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 7412-7413
    • Mesic, M.1    Fishbein, J.C.2
  • 56
    • 0017800253 scopus 로고
    • Aliphatic hydroxylation by highly purified liver microsomal cytochrome P-450: Evidence for a carbon radical intermediate
    • Groves, J. T., McClusky, G. A., White, R. E., and Coon, M. J. (1978) Aliphatic hydroxylation by highly purified liver microsomal cytochrome P-450: Evidence for a carbon radical intermediate Biochem. Biophys. Res. Commun. 81, 154-160
    • (1978) Biochem. Biophys. Res. Commun. , vol.81 , pp. 154-160
    • Groves, J.T.1    McClusky, G.A.2    White, R.E.3    Coon, M.J.4
  • 57
    • 4143133130 scopus 로고    scopus 로고
    • Rate-limiting steps in oxidations catalyzed by rabbit cytochrome P450 1A2
    • Guengerich, F. P., Krauser, J. A., and Johnson, W. W. (2004) Rate-limiting steps in oxidations catalyzed by rabbit cytochrome P450 1A2 Biochemistry 43, 10775-10788
    • (2004) Biochemistry , vol.43 , pp. 10775-10788
    • Guengerich, F.P.1    Krauser, J.A.2    Johnson, W.W.3
  • 58
    • 16844371090 scopus 로고    scopus 로고
    • Kinetic analysis of oxidation of coumarins by human cytochrome P450 2A6
    • Yun, C.-H., Kim, K.-H., Calcutt, M. W., and Guengerich, F. P. (2005) Kinetic analysis of oxidation of coumarins by human cytochrome P450 2A6 J. Biol. Chem. 280, 12279-12291
    • (2005) J. Biol. Chem. , vol.280 , pp. 12279-12291
    • Yun, C.-H.1    Kim, K.-H.2    Calcutt, M.W.3    Guengerich, F.P.4
  • 60
    • 0037862197 scopus 로고
    • Bond dissociation energies by kinetic methods
    • Kerr, J. A. (1966) Bond dissociation energies by kinetic methods Chem. Rev. 66, 465-500
    • (1966) Chem. Rev. , vol.66 , pp. 465-500
    • Kerr, J.A.1
  • 62
    • 0030781147 scopus 로고    scopus 로고
    • Kinetics of ferric cytochrome P450 reduction by NADPH-cytochrome P450 reductase: Rapid reduction in absence of substrate and variations among cytochrome P450 systems
    • Guengerich, F. P. and Johnson, W. W. (1997) Kinetics of ferric cytochrome P450 reduction by NADPH-cytochrome P450 reductase: Rapid reduction in absence of substrate and variations among cytochrome P450 systems Biochemistry 36, 14741-14750
    • (1997) Biochemistry , vol.36 , pp. 14741-14750
    • Guengerich, F.P.1    Johnson, W.W.2
  • 63
    • 0000353491 scopus 로고
    • A nuclear magnetic resonance study of the reversible hydration of aliphatic aldehydes and ketones. II. The acid-catalyzed oxygen exchange of acetaldehyde
    • Greenzaid, P., Luz, Z., and Samuel, D. (1967) A nuclear magnetic resonance study of the reversible hydration of aliphatic aldehydes and ketones. II. The acid-catalyzed oxygen exchange of acetaldehyde J. Am. Chem. Soc. 89, 756-759
    • (1967) J. Am. Chem. Soc. , vol.89 , pp. 756-759
    • Greenzaid, P.1    Luz, Z.2    Samuel, D.3
  • 64
    • 0000659605 scopus 로고
    • A nuclear magnetic resonance study of the reversible hydration of aliphatic aldehydes and ketones. I. Oxygen-17 and proton spectra and equilibrium constants
    • Greenzaid, P., Luz, Z., and Samuel, D. (1967) A nuclear magnetic resonance study of the reversible hydration of aliphatic aldehydes and ketones. I. Oxygen-17 and proton spectra and equilibrium constants J. Am. Chem. Soc. 89, 749-755
    • (1967) J. Am. Chem. Soc. , vol.89 , pp. 749-755
    • Greenzaid, P.1    Luz, Z.2    Samuel, D.3
  • 65
    • 79951570615 scopus 로고    scopus 로고
    • Multi-step oxidations catalyzed by cytochrome P450 enzymes: Processive vs. distributive kinetics and the issue of carbonyl oxidation
    • Guengerich, F. P., Sohl, C. D., and Chowdhury, G. (2011) Multi-step oxidations catalyzed by cytochrome P450 enzymes: Processive vs. distributive kinetics and the issue of carbonyl oxidation Arch. Biochem. Biophys. 507, 126-134
    • (2011) Arch. Biochem. Biophys. , vol.507 , pp. 126-134
    • Guengerich, F.P.1    Sohl, C.D.2    Chowdhury, G.3
  • 66
    • 84892193594 scopus 로고    scopus 로고
    • Substrate oxidation by cytochrome P450 enzymes
    • In (Ortiz de Montellano, P. R. Ed.) 3rd ed. pp, Kluwer Academic/Plenum Publishers, New York.
    • Ortiz de Montellano, P. R. and De Voss, J. J. (2005) Substrate oxidation by cytochrome P450 enzymes. In Cytochrome P450: Structure, Mechanism, and Biochemistry (Ortiz de Montellano, P. R., Ed.) 3rd ed., pp 183-245, Kluwer Academic/Plenum Publishers, New York.
    • (2005) Cytochrome P450: Structure, Mechanism, and Biochemistry , pp. 183-245
    • Ortiz De Montellano, P.R.1    De Voss, J.J.2
  • 67
    • 81555222817 scopus 로고    scopus 로고
    • Structures of cytochrome P450 2B6 bound to 4-benzylpyridine and 4-(4-nitrobenzyl)pyridine: Insight into inhibitor binding and rearrangement of active site side chains
    • Shah, M. B., Pascual, J., Zhang, Q. H., Stout, C. D., and Halpert, J. R. (2011) Structures of cytochrome P450 2B6 bound to 4-benzylpyridine and 4-(4-nitrobenzyl)pyridine: Insight into inhibitor binding and rearrangement of active site side chains Mol. Pharmacol. 80, 1047-1055
    • (2011) Mol. Pharmacol. , vol.80 , pp. 1047-1055
    • Shah, M.B.1    Pascual, J.2    Zhang, Q.H.3    Stout, C.D.4    Halpert, J.R.5


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