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Volumn , Issue , 2005, Pages 861-873

Isotope effects from partitioning of intermediates in enzyme-catalyzed hydroxylation reactions

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EID: 33748505959     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1201/9781420028027     Document Type: Chapter
Times cited : (12)

References (34)
  • 1
    • 0016832598 scopus 로고
    • Steady-state analysis of kinetic isotope effects in enzymic reactions
    • Northrop, D. B., Steady-state analysis of kinetic isotope effects in enzymic reactions, Biochemistry, 14, 2644-2651, 1975.
    • (1975) Biochemistry , vol.14 , pp. 2644-2651
    • Northrop, D.B.1
  • 2
    • 0019524346 scopus 로고
    • pH variation of isotope effects in enzyme-catalyzed reactions. 1. Isotope- and pH-dependent steps the same
    • Cook, P. F. and Cleland, W. W., pH variation of isotope effects in enzyme-catalyzed reactions. 1. Isotope- and pH-dependent steps the same, Biochemistry, 20, 1797-1805, 1981.
    • (1981) Biochemistry , vol.20 , pp. 1797-1805
    • Cook, P.F.1    Cleland, W.W.2
  • 3
    • 0018971732 scopus 로고
    • Kinetic isotope effects in cytochrome P-450-catalyzed oxidation reactions. Intermolecular and intramolecular deuterium isotope effects during the N-demethylation of N, N-dimethylphentermine
    • Miwa, G. T., Garland, W. A., Hodshon, B. J., Lu, A. Y. H., and Northrop, D. B., Kinetic isotope effects in cytochrome P-450-catalyzed oxidation reactions. Intermolecular and intramolecular deuterium isotope effects during the N-demethylation of N, N-dimethylphentermine, J. Biol. Chem., 255, 6049-6054, 1980.
    • (1980) J. Biol. Chem. , vol.255 , pp. 6049-6054
    • Miwa, G.T.1    Garland, W.A.2    Hodshon, B.J.3    Lu, A.Y.H.4    Northrop, D.B.5
  • 4
    • 0000497670 scopus 로고
    • Isotopically sensitive branching and its effect on the observed intramolecular isotope effects in cytochrome P-450 catalyzed reactions: A new method for the estimation of intrinsic isotope effects
    • Jones, J. P., Korzekwa, K., Rettie, A. E., and Trager, W., Isotopically sensitive branching and its effect on the observed intramolecular isotope effects in cytochrome P-450 catalyzed reactions: a new method for the estimation of intrinsic isotope effects, J. Am. Chem. Soc., 108, 7074-7078, 1986.
    • (1986) J. Am. Chem. Soc. , vol.108 , pp. 7074-7078
    • Jones, J.P.1    Korzekwa, K.2    Rettie, A.E.3    Trager, W.4
  • 5
    • 0024451771 scopus 로고
    • Theory for the observed isotope effects from enzymatic systems that form multiple products via branched reaction patyways: Cytochrome P-450
    • Korzekwa, K. R., Trager, W. F., and Gillette, J. R., Theory for the observed isotope effects from enzymatic systems that form multiple products via branched reaction patyways: Cytochrome P-450, Biochemistry, 28, 9012-9018, 1989.
    • (1989) Biochemistry , vol.28 , pp. 9012-9018
    • Korzekwa, K.R.1    Trager, W.F.2    Gillette, J.R.3
  • 8
    • 0024980098 scopus 로고
    • Deuterium isotope effects on toluene metabolism. Product release as a rate-limiting step in cytochrome P-450 catalysis
    • Ling, K.-H. J. and Hanzlik, R. P., Deuterium isotope effects on toluene metabolism. Product release as a rate-limiting step in cytochrome P-450 catalysis, Biochem. Biophys. Res. Commun., 160, 844-849, 1989.
    • (1989) Biochem. Biophys. Res. Commun. , vol.160 , pp. 844-849
    • Ling, K.-H.J.1    Hanzlik, R.P.2
  • 9
    • 0017392344 scopus 로고
    • Intramolecular determination of primary kinetic isotope effects in hydroxylations catalyzed by cytochrome P-450
    • Hjelmeland, L. M., Aronow, L., and Trudell, J. R., Intramolecular determination of primary kinetic isotope effects in hydroxylations catalyzed by cytochrome P-450, Biochem. Biophys. Res. Commun., 76, 541-549, 1977.
    • (1977) Biochem. Biophys. Res. Commun. , vol.76 , pp. 541-549
    • Hjelmeland, L.M.1    Aronow, L.2    Trudell, J.R.3
  • 10
    • 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., Aliphatic hydroxylation by highly purified liver microsomal cytochrome P-450. Evidence for a carbon radical intermediate, Biochem. Biophys. Res. Commun., 81, 154-160, 1978.
    • (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
  • 11
    • 12044258092 scopus 로고
    • Active site dynamics of xylene hydroxylation by cytochrome P-450 as revealed by kinetic deuterium isotope effects
    • Hanzlik, R. P. and Ling, K.-H. J., Active site dynamics of xylene hydroxylation by cytochrome P-450 as revealed by kinetic deuterium isotope effects, J. Am. Chem. Soc., 115, 9363-9370, 1993.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 9363-9370
    • Hanzlik, R.P.1    Ling, K.-H.J.2
  • 12
    • 0033550491 scopus 로고    scopus 로고
    • Experimental theoretical study of the effect of active-site constrained substrate motion on the magnitude of the observed intramolecular isotope effect for the p450 101 catalyzed benzylic hydroxylation of isomeric xylenes and 4,40-dimethylbiphenyl
    • Audergon, C., Iyer, K. R., Jones, J. P., Darbyshire, J. F., and Trager, W. F., Experimental theoretical study of the effect of active-site constrained substrate motion on the magnitude of the observed intramolecular isotope effect for the p450 101 catalyzed benzylic hydroxylation of isomeric xylenes and 4,40-dimethylbiphenyl, J. Am. Chem. Soc., 121, 41-47, 1999.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 41-47
    • Audergon, C.1    Iyer, K.R.2    Jones, J.P.3    Darbyshire, J.F.4    Trager, W.F.5
  • 13
    • 0024991656 scopus 로고
    • Active site dynamics of toluene hydroxylation by cytochrome P-450
    • Hanzlik, R. P. and Ling, K.-H. J., Active site dynamics of toluene hydroxylation by cytochrome P-450, J. Org. Chem., 55, 3992-3997, 1990.
    • (1990) J. Org. Chem. , vol.55 , pp. 3992-3997
    • Hanzlik, R.P.1    Ling, K.-H.J.2
  • 14
    • 0000385707 scopus 로고
    • The separation of the intramolecular isotope effect for the cytochrome P-450 catalyzed hydroxylation of n-octane into its primary and secondary components
    • Jones, J. P. and Trager, W., The separation of the intramolecular isotope effect for the cytochrome P-450 catalyzed hydroxylation of n-octane into its primary and secondary components, J. Am. Chem. Soc., 109, 2171-2173, 1987.
    • (1987) J. Am. Chem. Soc. , vol.109 , pp. 2171-2173
    • Jones, J.P.1    Trager, W.2
  • 15
    • 0021100472 scopus 로고
    • The use of intramolecular isotope effects to distinguish between deprotonation and hydrogen atom abstraction mechanisms in cytochrome P-450-and peroxidase-catalyzed N-demethylation reactions
    • Miwa, G. T., Walsh, J. S., Kedderis, G. L., and Hollenberg, P. F., The use of intramolecular isotope effects to distinguish between deprotonation and hydrogen atom abstraction mechanisms in cytochrome P-450-and peroxidase-catalyzed N-demethylation reactions, J. Biol. Chem., 258, 14445-14449, 1983.
    • (1983) J. Biol. Chem. , vol.258 , pp. 14445-14449
    • Miwa, G.T.1    Walsh, J.S.2    Kedderis, G.L.3    Hollenberg, P.F.4
  • 16
    • 0000901543 scopus 로고
    • On isotope effects for the cytochrome P-450 oxidation of substituted N, N-dimethylanilines
    • Dinnocenzo, J. P., Karki, S. B., and Jones, J. P., On isotope effects for the cytochrome P-450 oxidation of substituted N, N-dimethylanilines, J. Am. Chem. Soc., 115, 7111-7116, 1993.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 7111-7116
    • Dinnocenzo, J.P.1    Karki, S.B.2    Jones, J.P.3
  • 17
    • 0029970784 scopus 로고    scopus 로고
    • Evidence for a 1-electron oxidation mechanism in N-dealkylation of N, N-dialkylanilines by cytochrome P450 2B1. Kinetic hydrogen isotope effects, linear free energy relationships, comparisons with horseradish peroxidase, and studies with oxygen surrogates
    • Guengerich, F. P., Yun, C.-H., and MacDonald, T. L., Evidence for a 1-electron oxidation mechanism in N-dealkylation of N, N-dialkylanilines by cytochrome P450 2B1. Kinetic hydrogen isotope effects, linear free energy relationships, comparisons with horseradish peroxidase, and studies with oxygen surrogates, J. Biol. Chem., 271, 27321-27329, 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 27321-27329
    • Guengerich, F.P.1    Yun, C.-H.2    MacDonald, T.L.3
  • 18
    • 0025279722 scopus 로고
    • Kinetic deuterium isotope effects on the N-demethylation of tertiary amides by cytochrome P-450
    • Hall, L. R. and Hanzlik, R. P., Kinetic deuterium isotope effects on the N-demethylation of tertiary amides by cytochrome P-450, J. Biol. Chem., 265, 12349-12355, 1990.
    • (1990) J. Biol. Chem. , vol.265 , pp. 12349-12355
    • Hall, L.R.1    Hanzlik, R.P.2
  • 19
    • 0028947612 scopus 로고
    • Mechanism of oxidative amine dealkylation of substituted N, N-dimethylanilines by cytochrome P-450: Application of isotope effects profiles
    • Karki, S. B., Dinnocenzo, J. P., Jones, J. P., and Korzekwa, K. R., Mechanism of oxidative amine dealkylation of substituted N, N-dimethylanilines by cytochrome P-450: application of isotope effects profiles, J. Am. Chem. Soc., 117, 3657-3664, 1995.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 3657-3664
    • Karki, S.B.1    Dinnocenzo, J.P.2    Jones, J.P.3    Korzekwa, K.R.4
  • 20
    • 0024843596 scopus 로고
    • Deprotonation of tertiary amine cation radicals. A direct experimental approach
    • Dinnocenzo, J. P. and Banach, T. E., Deprotonation of tertiary amine cation radicals. A direct experimental approach, J. Am. Chem. Soc., 111, 8646-8653, 1989.
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 8646-8653
    • Dinnocenzo, J.P.1    Banach, T.E.2
  • 21
    • 0032852842 scopus 로고    scopus 로고
    • The tetrahydropterin-dependent amino acid hydroxylases
    • Fitzpatrick, P. F., The tetrahydropterin-dependent amino acid hydroxylases, Annu. Rev. Biochem., 68, 355-381, 1999.
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 355-381
    • Fitzpatrick, P.F.1
  • 22
    • 0345492036 scopus 로고    scopus 로고
    • Mechanism of aromatic amino acid hydroxylation
    • Fitzpatrick, P. F., Mechanism of aromatic amino acid hydroxylation, Biochemistry, 42, 14083-14091, 2003.
    • (2003) Biochemistry , vol.42 , pp. 14083-14091
    • Fitzpatrick, P.F.1
  • 24
    • 0033534158 scopus 로고    scopus 로고
    • The influence of steric bulk and electrostatics on the hydroxylation regiospecificity of tryptophan hydroxylase: Characterization of methyltryptophans and azatryptophans as substrates
    • Moran, G. R., Phillips, R. S., and Fitzpatrick, P. F., The influence of steric bulk and electrostatics on the hydroxylation regiospecificity of tryptophan hydroxylase: characterization of methyltryptophans and azatryptophans as substrates, Biochemistry, 38, 16283-16289, 1999.
    • (1999) Biochemistry , vol.38 , pp. 16283-16289
    • Moran, G.R.1    Phillips, R.S.2    Fitzpatrick, P.F.3
  • 25
    • 0025777217 scopus 로고
    • The steady state kinetic mechanism of rat tyrosine hydroxylase
    • Fitzpatrick, P. F., The steady state kinetic mechanism of rat tyrosine hydroxylase, Biochemistry, 30, 3658-3662, 1991.
    • (1991) Biochemistry , vol.30 , pp. 3658-3662
    • Fitzpatrick, P.F.1
  • 26
    • 0025900994 scopus 로고
    • Studies of the rate-limiting step in the tyrosine hydroxylase reaction: Alternate substrates, solvent isotope effects, and transition state analogs
    • Fitzpatrick, P. F., Studies of the rate-limiting step in the tyrosine hydroxylase reaction: alternate substrates, solvent isotope effects, and transition state analogs, Biochemistry, 30, 6386-6391, 1991.
    • (1991) Biochemistry , vol.30 , pp. 6386-6391
    • Fitzpatrick, P.F.1
  • 27
    • 0346434118 scopus 로고    scopus 로고
    • Uncoupled forms of tyrosine hydroxylase unmask kinetic isotope effects on chemical steps
    • Frantom, P. A. and Fitzpatrick, P. F., Uncoupled forms of tyrosine hydroxylase unmask kinetic isotope effects on chemical steps, J. Am. Chem. Soc., 125, 16190-16191, 2003.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 16190-16191
    • Frantom, P.A.1    Fitzpatrick, P.F.2
  • 28
    • 3643061399 scopus 로고    scopus 로고
    • A mechanism for hydroxylation by tyrosine hydroxylase based on partitioning of substituted phenylalanines
    • Hillas, P. J. and Fitzpatrick, P. F., A mechanism for hydroxylation by tyrosine hydroxylase based on partitioning of substituted phenylalanines, Biochemistry, 35, 6969-6975, 1996.
    • (1996) Biochemistry , vol.35 , pp. 6969-6975
    • Hillas, P.J.1    Fitzpatrick, P.F.2
  • 29
    • 0037165727 scopus 로고    scopus 로고
    • Intrinsic deuterium isotope effects on benzylic hydroxylation by tyrosine hydroxylase
    • Frantom, P. A., Pongdee, R., Sulikowski, G. A., and Fitzpatrick, P. F., Intrinsic deuterium isotope effects on benzylic hydroxylation by tyrosine hydroxylase, J. Am. Chem. Soc., 124, 4202-4203, 2002.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 4202-4203
    • Frantom, P.A.1    Pongdee, R.2    Sulikowski, G.A.3    Fitzpatrick, P.F.4
  • 30
    • 7744231498 scopus 로고    scopus 로고
    • Mechanisms whereby mononuclear copper proteins functionalize organic substrates
    • Klinman, J. P., Mechanisms whereby mononuclear copper proteins functionalize organic substrates, Chem. Rev., 96, 2541-2562, 1996.
    • (1996) Chem. Rev. , vol.96 , pp. 2541-2562
    • Klinman, J.P.1
  • 31
    • 0021861145 scopus 로고
    • Secondary isotope effects and structure-reactivity correlations in the dopamine b-monooxygenase reaction: Evidence for a chemical mechanism
    • Miller, S. M. and Klinman, J. P., Secondary isotope effects and structure-reactivity correlations in the dopamine b-monooxygenase reaction: evidence for a chemical mechanism, Biochemistry, 24, 2114-2127, 1985.
    • (1985) Biochemistry , vol.24 , pp. 2114-2127
    • Miller, S.M.1    Klinman, J.P.2
  • 32
    • 0021109407 scopus 로고
    • Magnitude of intrinsic isotope effects in the dopamine β-monooxygenase reaction
    • Miller, S. M. and Klinman, J. P., Magnitude of intrinsic isotope effects in the dopamine β-monooxygenase reaction, Biochemistry, 22, 3091-3096, 1983.
    • (1983) Biochemistry , vol.22 , pp. 3091-3096
    • Miller, S.M.1    Klinman, J.P.2
  • 33
    • 0021799987 scopus 로고
    • 3-Phenylpropenes as mechanism-based inhibitors of dopamine b-hydroxylase: Evidence for a radical mechanism
    • Fitzpatrick, P. F., Flory, D. R. Jr., and Villafranca, J. J., 3-Phenylpropenes as mechanism-based inhibitors of dopamine b-hydroxylase: evidence for a radical mechanism, Biochemistry, 24, 2108-2114, 1985.
    • (1985) Biochemistry , vol.24 , pp. 2108-2114
    • Fitzpatrick, P.F.1    Flory, D.R.2    Villafranca, J.J.3
  • 34
    • 0023002228 scopus 로고
    • The mechanism of inactivation of dopamine b-hydroxylase by hydrazines
    • Fitzpatrick, P. F. and Villafranca, J. J., The mechanism of inactivation of dopamine b-hydroxylase by hydrazines, J. Biol. Chem., 261, 4510-4518, 1986.
    • (1986) J. Biol. Chem. , vol.261 , pp. 4510-4518
    • Fitzpatrick, P.F.1    Villafranca, J.J.2


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