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Volumn 51, Issue 1, 1997, Pages 147-151

Evidence for a role of a perferryl-oxygen complex, FeO3+, in the N- oxygenation of amines by cytochrome P450 enzymes

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; AMINE; BENZENE DERIVATIVE; CYTOCHROME P450; FERRIC OXIDE; GLYCERYL TRINITRATE; HYDROGEN PEROXIDE; LEUCINE; QUERCETIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

EID: 0031015267     PISSN: 0026895X     EISSN: None     Source Type: Journal    
DOI: 10.1124/mol.51.1.147     Document Type: Article
Times cited : (52)

References (40)
  • 1
    • 0025895757 scopus 로고
    • Reactions and significance of cytochrome P-450 enzymes
    • Guengerich, F. P. Reactions and significance of cytochrome P-450 enzymes. J. Biol. Chem. 266:10019-10022 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 10019-10022
    • Guengerich, F.P.1
  • 3
    • 0002751786 scopus 로고
    • Oxygen activation and reactivity
    • (Ortiz de Montellano, P. R., ed.). 2nd ed. Plenum Press, New York
    • Ortiz de Montellano, P. R. Oxygen activation and reactivity, in Cytochrome P450: Structure, Mechanism, and Biochemistry (Ortiz de Montellano, P. R., ed.). 2nd ed. Plenum Press, New York, 245-303 (1995).
    • (1995) Cytochrome P450: Structure, Mechanism, and Biochemistry , pp. 245-303
    • Ortiz De Montellano, P.R.1
  • 4
    • 33845469510 scopus 로고
    • Chemical mechanisms of catalysis by cytochromes P-450: A unified view
    • Guengerich, F. P., and T. L. Macdonald. Chemical mechanisms of catalysis by cytochromes P-450: a unified view. Acc. Chem. Res. 17:9-16 (1984).
    • (1984) Acc. Chem. Res. , vol.17 , pp. 9-16
    • Guengerich, F.P.1    Macdonald, T.L.2
  • 5
    • 0016307907 scopus 로고
    • The N-hydroxylation of phentermine (2-methyl-2-amino-1-phenylpropane). Properties of the enzyme system
    • Cho, A. K., B. Lindeke, and C. Y. Sum. The N-hydroxylation of phentermine (2-methyl-2-amino-1-phenylpropane). Properties of the enzyme system. Drug Metab. Dispos. 2:1-8 (1974).
    • (1974) Drug Metab. Dispos. , vol.2 , pp. 1-8
    • Cho, A.K.1    Lindeke, B.2    Sum, C.Y.3
  • 6
    • 0001167305 scopus 로고
    • Enzymatic oxidation of alkyl sulfides by cytochrome P-450 and hydroxyl radical
    • Watanabe, Y., T. Numata, T. Iyanagi, and S. Oae. Enzymatic oxidation of alkyl sulfides by cytochrome P-450 and hydroxyl radical. Bull. Chem. Soc. Jpn. 54:1163-1170 (1981).
    • (1981) Bull. Chem. Soc. Jpn. , vol.54 , pp. 1163-1170
    • Watanabe, Y.1    Numata, T.2    Iyanagi, T.3    Oae, S.4
  • 7
    • 0022512213 scopus 로고
    • Interactions of diethylphenylphosphine with purified, reconstituted mouse liver cytochrome P-450 monooxygenase systems
    • Smyser, B. P., P. E. Levi, and E. Hodgson. Interactions of diethylphenylphosphine with purified, reconstituted mouse liver cytochrome P-450 monooxygenase systems. Biochem. Pharmacol. 35:1719-1723 (1986).
    • (1986) Biochem. Pharmacol. , vol.35 , pp. 1719-1723
    • Smyser, B.P.1    Levi, P.E.2    Hodgson, E.3
  • 8
    • 0024326020 scopus 로고
    • Oxidation of halogenated compounds by cytochrome P-450, peroxidases, and model metalloporphyrins
    • Guengerich, F. P. Oxidation of halogenated compounds by cytochrome P-450, peroxidases, and model metalloporphyrins. J. Biol. Chem. 264: 17198-17205 (1989).
    • (1989) J. Biol. Chem. , vol.264 , pp. 17198-17205
    • Guengerich, F.P.1
  • 9
    • 33845282999 scopus 로고
    • Control of the catalytic activity of prosthetic heme by the structure of hemoproteins
    • Ortiz de Montellano, P. R. Control of the catalytic activity of prosthetic heme by the structure of hemoproteins. Acc. Chem. Res. 20:289-294 (1987).
    • (1987) Acc. Chem. Res. , vol.20 , pp. 289-294
    • Ortiz De Montellano, P.R.1
  • 10
    • 0027470428 scopus 로고
    • Evidence for specific base catalysis in N-dealkylation reactions catalyzed by cytochrome P450 and chloroperoxidase: Differences in rates of deprotonation of aminium radicals as an explanation for high kinetic hydrogen isotope effects observed with peroxidases
    • Okazaki, O., and F. P. Guengerich. Evidence for specific base catalysis in N-dealkylation reactions catalyzed by cytochrome P450 and chloroperoxidase: differences in rates of deprotonation of aminium radicals as an explanation for high kinetic hydrogen isotope effects observed with peroxidases. J. Biol. Chem. 268:1546-1552 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 1546-1552
    • Okazaki, O.1    Guengerich, F.P.2
  • 11
    • 0023894686 scopus 로고
    • Flavin-containing monooxygenases: Catalytic mechanism and substrate specificities
    • Ziegler, D. M. Flavin-containing monooxygenases: catalytic mechanism and substrate specificities. Drug Metab. Rev. 19:1-32 (1988).
    • (1988) Drug Metab. Rev. , vol.19 , pp. 1-32
    • Ziegler, D.M.1
  • 12
    • 0022467917 scopus 로고
    • Oxidation of quinidine by human liver cytochrome P-450
    • Guengerich, F. P., D. Müller-Enoch, and I. A. Blair. Oxidation of quinidine by human liver cytochrome P-450. Mol. Pharmacol. 30:287-295 (1986).
    • (1986) Mol. Pharmacol. , vol.30 , pp. 287-295
    • Guengerich, F.P.1    Müller-Enoch, D.2    Blair, I.A.3
  • 13
    • 0023616179 scopus 로고
    • A new metabolite of methamphetamine: Evidence for formation of N-[1-methyl-1-phenylethyl-]ethanimine N-oxide
    • Baba, T., H. Yamada, K. Oguri, and H. Yoshimura. A new metabolite of methamphetamine: evidence for formation of N-[1-methyl-1-phenyl)ethyl-]ethanimine N-oxide. Xenobiotica 17:1029-1038 (1987).
    • (1987) Xenobiotica , vol.17 , pp. 1029-1038
    • Baba, T.1    Yamada, H.2    Oguri, K.3    Yoshimura, H.4
  • 14
    • 0024359771 scopus 로고
    • Bioactivation and detoxication of the pyrrolizidine alkaloid senecionine by cytochrome P-450 isozymes in rat liver
    • Williams, D. E., R. L. Reed, B. Kedzierski, F. P. Guengerich, and D. C. Buhler. Bioactivation and detoxication of the pyrrolizidine alkaloid senecionine by cytochrome P-450 isozymes in rat liver. Drug Metab. Dispos. 17:387-392 (1989).
    • (1989) Drug Metab. Dispos. , vol.17 , pp. 387-392
    • Williams, D.E.1    Reed, R.L.2    Kedzierski, B.3    Guengerich, F.P.4    Buhler, D.C.5
  • 15
    • 0024507387 scopus 로고
    • Oxidation of cycloalkylamines by cytochrome P-450. Mechanism-based inactivation, adduct formation, ring expansion, and nitrone formation
    • Bondon, A., T. L. Macdonald, T. M. Harris, and F. P. Guengerich. Oxidation of cycloalkylamines by cytochrome P-450. Mechanism-based inactivation, adduct formation, ring expansion, and nitrone formation. J. Biol. Chem. 264:1988-1997 (1989).
    • (1989) J. Biol. Chem. , vol.264 , pp. 1988-1997
    • Bondon, A.1    Macdonald, T.L.2    Harris, T.M.3    Guengerich, F.P.4
  • 16
    • 0027289112 scopus 로고
    • Partitioning between N-dealkylation and N-oxygenation in the oxidation of N,N-dialkylarylamines catalyzed by cytochrome P450 2B1
    • Seto, Y., and F. P. Guengerich. Partitioning between N-dealkylation and N-oxygenation in the oxidation of N,N-dialkylarylamines catalyzed by cytochrome P450 2B1. J. Biol. Chem. 268:9986-9997 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 9986-9997
    • Seto, Y.1    Guengerich, F.P.2
  • 17
    • 0020073188 scopus 로고
    • Mechanistic studies on C-19 demethylation in oestrogen biocynthesis
    • Akhtar, M., M. R. Calder, D. L. Corina, and J. N. Wright. Mechanistic studies on C-19 demethylation in oestrogen biocynthesis. Biochem. J. 201:569-580 (1982).
    • (1982) Biochem. J. , vol.201 , pp. 569-580
    • Akhtar, M.1    Calder, M.R.2    Corina, D.L.3    Wright, J.N.4
  • 18
    • 0000889090 scopus 로고
    • Mechanistic studies on a placental aromatase model reaction
    • Cole, P. A., and C. H. Robinson. Mechanistic studies on a placental aromatase model reaction. J. Am. Chem. Soc. 113:8130-8137 (1991).
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 8130-8137
    • Cole, P.A.1    Robinson, C.H.2
  • 19
    • 0027938904 scopus 로고
    • Aromatization of a bicyclic steroid analog, 3-oxodecalin-4-ene-10-carboxaldehyde, by liver microsomal cytochrome P450 2B4
    • Vaz, A. D. N., K. J. Kessell, and M. J. Coon. Aromatization of a bicyclic steroid analog, 3-oxodecalin-4-ene-10-carboxaldehyde, by liver microsomal cytochrome P450 2B4. Biochemistry 33:13651-13661 (1994).
    • (1994) Biochemistry , vol.33 , pp. 13651-13661
    • Vaz, A.D.N.1    Kessell, K.J.2    Coon, M.J.3
  • 20
    • 0001149840 scopus 로고
    • Olefin formation in the oxidative deformylation of aldehydes by cytochrome P-450. Mechanistic implications for catalysis by oxygen-derived peroxide
    • Vaz, A. D. N., E. S. Roberts, and M. J. Coon. Olefin formation in the oxidative deformylation of aldehydes by cytochrome P-450. Mechanistic implications for catalysis by oxygen-derived peroxide. J. Am. Chem. Soc. 113:5886-5887 (1991).
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 5886-5887
    • Vaz, A.D.N.1    Roberts, E.S.2    Coon, M.J.3
  • 21
    • 0030004087 scopus 로고    scopus 로고
    • Peroxo-iron and oxenoid-iron species as alternative oxygenating agents in cytochrome P450-catalyzed reactions: Switching by threonine-302 to alanine mutagenesis of cytochrome P450 2B4
    • Vaz, A. D. N., S. J. Pernecky, G. M. Raner, and M. J. Coon. Peroxo-iron and oxenoid-iron species as alternative oxygenating agents in cytochrome P450-catalyzed reactions: switching by threonine-302 to alanine mutagenesis of cytochrome P450 2B4. Proc. Natl. Acad. Sci. USA 93:4644-4648 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 4644-4648
    • Vaz, A.D.N.1    Pernecky, S.J.2    Raner, G.M.3    Coon, M.J.4
  • 23
    • 0014781246 scopus 로고
    • An improved preparation of tertiary amine N-oxides
    • Craig, J. C., and K. K. Purushothaman. An improved preparation of tertiary amine N-oxides. J. Org. Chem. 35:1721-1722 (1970).
    • (1970) J. Org. Chem. , vol.35 , pp. 1721-1722
    • Craig, J.C.1    Purushothaman, K.K.2
  • 24
    • 0022980412 scopus 로고
    • Reactions of the 4a-hydroperoxide of liver microsomal flavin-containing monooxygenase with nucleophilic and electrophilic substrates
    • Jones, K. C., and D. P. Ballou. Reactions of the 4a-hydroperoxide of liver microsomal flavin-containing monooxygenase with nucleophilic and electrophilic substrates. J. Biol. Chem. 261:2553-2559 (1986).
    • (1986) J. Biol. Chem. , vol.261 , pp. 2553-2559
    • Jones, K.C.1    Ballou, D.P.2
  • 26
    • 0019249174 scopus 로고
    • Purification of cytochrome P-450, NADPH-cytochrome P-450 reductase, and epoxide hydratase from a single preparation of rat liver microsomes
    • Guengerich, F. P., and M. V. Martin. Purification of cytochrome P-450, NADPH-cytochrome P-450 reductase, and epoxide hydratase from a single preparation of rat liver microsomes. Arch. Biochem. Biophys. 205:365-379 (1980).
    • (1980) Arch. Biochem. Biophys. , vol.205 , pp. 365-379
    • Guengerich, F.P.1    Martin, M.V.2
  • 27
    • 0028358220 scopus 로고
    • Expression of modified human cytochrome P450 1A2 in Escherichia coli: Stabilization, purification, spectral characterization, and catalytic activities of the enzyme
    • Sandhu, P., Z. Guo, T. Baba, M. V. Martin, R. H. Tukey, and F. P. Guengerich. Expression of modified human cytochrome P450 1A2 in Escherichia coli: stabilization, purification, spectral characterization, and catalytic activities of the enzyme. Arch. Biochem. Biophys. 309:168-177 (1994).
    • (1994) Arch. Biochem. Biophys. , vol.309 , pp. 168-177
    • Sandhu, P.1    Guo, Z.2    Baba, T.3    Martin, M.V.4    Tukey, R.H.5    Guengerich, F.P.6
  • 28
    • 0027223881 scopus 로고
    • Expression of modified human cytochrome P450 3A4 in Escherichia coli and purification and reconstitution of the enzyme
    • Gillam, E. M. J., T. Baba, B. -R. Kim, S. Ohmori, and F. P. Guengerich. Expression of modified human cytochrome P450 3A4 in Escherichia coli and purification and reconstitution of the enzyme. Arch. Biochem. Biophys. 305:123-131 (1993).
    • (1993) Arch. Biochem. Biophys. , vol.305 , pp. 123-131
    • Gillam, E.M.J.1    Baba, T.2    Kim, B.R.3    Ohmori, S.4    Guengerich, F.P.5
  • 30
    • 0017088267 scopus 로고
    • Some properties of a detergent-solubilized NADPH-cytochrome c (cytochrome P-450) reductase purified by biospecific affinity chromatography
    • Yasukochi, Y., and B. S. S. Masters. Some properties of a detergent-solubilized NADPH-cytochrome c (cytochrome P-450) reductase purified by biospecific affinity chromatography. J. Biol. Chem. 251:5337-5344 (1976).
    • (1976) J. Biol. Chem. , vol.251 , pp. 5337-5344
    • Yasukochi, Y.1    Masters, B.S.S.2
  • 31
    • 0021965297 scopus 로고
    • Simultaneous purification of multiple forms of rat liver microsomal cytochrome P-450 by high-performance liquid chromatography
    • Funae, Y., and S. Imaoka. Simultaneous purification of multiple forms of rat liver microsomal cytochrome P-450 by high-performance liquid chromatography. Biochim. Biophys. Acta. 842:119-132 (1985).
    • (1985) Biochim. Biophys. Acta , vol.842 , pp. 119-132
    • Funae, Y.1    Imaoka, S.2
  • 32
    • 0018095311 scopus 로고
    • Destruction of heme and hemoproteins mediated by liver microsomal reduced nicotinamide adenine dinucleotide phosphate-cytochrome P-450 reductase
    • Guengerich, F. P. Destruction of heme and hemoproteins mediated by liver microsomal reduced nicotinamide adenine dinucleotide phosphate-cytochrome P-450 reductase. Biochemistry 17:3633-3639 (1978).
    • (1978) Biochemistry , vol.17 , pp. 3633-3639
    • Guengerich, F.P.1
  • 33
    • 0024538443 scopus 로고
    • Oxidation of substituted N,N-dimethylanilines by cytochrome P-450: Estimation of the effective oxidation-reduction potential of cytochrome P-450
    • Macdonald, T. L., W. G. Gutheim, R. B. Martin, and F. P. Guengerich. Oxidation of substituted N,N-dimethylanilines by cytochrome P-450: estimation of the effective oxidation-reduction potential of cytochrome P-450. Biochemistry 28:2071-2077 (1989).
    • (1989) Biochemistry , vol.28 , pp. 2071-2077
    • Macdonald, T.L.1    Gutheim, W.G.2    Martin, R.B.3    Guengerich, F.P.4
  • 34
    • 78651165715 scopus 로고
    • The carbon monoxide-binding pigment of liver microsomes. I. Evidence for its hemoprotein nature
    • Omura, T., and R. Sato. The carbon monoxide-binding pigment of liver microsomes. I. Evidence for its hemoprotein nature. J. Biol. Chem. 239: 2370-2378 (1964).
    • (1964) J. Biol. Chem. , vol.239 , pp. 2370-2378
    • Omura, T.1    Sato, R.2
  • 36
    • 0018791836 scopus 로고
    • Studies on the mechanism of hepatic microsomal N-oxide formation: N-oxidation of NN-dimethylaniline by a reconstituted rabbit liver microsomal cytochrome P-448 enzyme system
    • Hlavica, P., and S. Hülsmann. Studies on the mechanism of hepatic microsomal N-oxide formation: N-oxidation of NN-dimethylaniline by a reconstituted rabbit liver microsomal cytochrome P-448 enzyme system. Biochem. J. 182:109-116 (1979).
    • (1979) Biochem. J. , vol.182 , pp. 109-116
    • Hlavica, P.1    Hülsmann, S.2
  • 37
    • 0024346126 scopus 로고
    • Oxidative N-demethylation of N,N-dimethylaniline by purified isozymes of cytochrome P-450
    • Pandey, R. N., A. P. Armstrong, and P. F. Hollenberg. Oxidative N-demethylation of N,N-dimethylaniline by purified isozymes of cytochrome P-450. Biochem. Pharmacol. 38:2181-2185 (1989).
    • (1989) Biochem. Pharmacol. , vol.38 , pp. 2181-2185
    • Pandey, R.N.1    Armstrong, A.P.2    Hollenberg, P.F.3
  • 38
    • 0001541099 scopus 로고
    • Uncoupling of the cytochrome P-450cam monooxygenase reaction by a single mutation, threonine-252 to alanine or valine: A possible role of the hydroxy amino acid in oxygen activation
    • Imai, M., H. Shimada, Y. Watanabe, Y. Matsushima-Hibiya, R. Makino, H. Koga, T. Horiuchi, and Y. Ishimura. Uncoupling of the cytochrome P-450cam monooxygenase reaction by a single mutation, threonine-252 to alanine or valine: a possible role of the hydroxy amino acid in oxygen activation. Proc. Natl. Acad. Sci. USA 86:7823-7827 (1989).
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 7823-7827
    • Imai, M.1    Shimada, H.2    Watanabe, Y.3    Matsushima-Hibiya, Y.4    Makino, R.5    Koga, H.6    Horiuchi, T.7    Ishimura, Y.8
  • 39
    • 0000730697 scopus 로고
    • Sequential electron transfer reactions catalyzed by cytochrome P-450 enzymes
    • (Mariano, P. S., ed.). JAI Press, Greenwich, CT
    • Guengerich, F. P., and Macdonald, T. L. Sequential electron transfer reactions catalyzed by cytochrome P-450 enzymes, in Advances in Electron Transfer Chemistry (Mariano, P. S., ed.). Vol. 3. JAI Press, Greenwich, CT, 191-241 (1993).
    • (1993) Advances in Electron Transfer Chemistry , vol.3 , pp. 191-241
    • Guengerich, F.P.1    Macdonald, T.L.2
  • 40
    • 0000946090 scopus 로고
    • One electron transfer mechanism in the enzymatic oxygenation of sulfoxide to sulfone promoted by a reconstituted system with purified cytochrome P-450
    • Watanabe, Y., T. Iyanagi, and S. Oae. One electron transfer mechanism in the enzymatic oxygenation of sulfoxide to sulfone promoted by a reconstituted system with purified cytochrome P-450. Tetrahedron Lett. 23:533-536 (1982).
    • (1982) Tetrahedron Lett. , vol.23 , pp. 533-536
    • Watanabe, Y.1    Iyanagi, T.2    Oae, S.3


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