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Volumn 30, Issue 4, 1998, Pages 739-786

The P450 catalytic cycle and oxygenation mechanism

Author keywords

[No Author keywords available]

Indexed keywords

CAMPHOR; CYTOCHROME P450; HEMOPROTEIN; LIGAND; OXYGEN;

EID: 0031757422     PISSN: 03602532     EISSN: None     Source Type: Journal    
DOI: 10.3109/03602539808996329     Document Type: Review
Times cited : (65)

References (175)
  • 2
    • 0020625539 scopus 로고
    • Source of the oxygen atom in the product of cytochrome P-450-catalyzed N-demethylation reactions
    • G. L. Kedderis, L. A. Dwyer, D. E. Rickert, and P. F. Hollenberg, Source of the oxygen atom in the product of cytochrome P-450-catalyzed N-demethylation reactions, Molec. Pharmacol., 23, 758-760 (1983).
    • (1983) Molec. Pharmacol. , vol.23 , pp. 758-760
    • Kedderis, G.L.1    Dwyer, L.A.2    Rickert, D.E.3    Hollenberg, P.F.4
  • 3
    • 0344418499 scopus 로고
    • Mechanism of microsomal electron transfer reactions: Role of cytochrome P-450
    • M. J. Coon and A. D. N. Vaz, Mechanism of microsomal electron transfer reactions: Role of cytochrome P-450, Chem. Scripta, 274, 17-19 (1987).
    • (1987) Chem. Scripta , vol.274 , pp. 17-19
    • Coon, M.J.1    Vaz, A.D.N.2
  • 4
    • 0007924115 scopus 로고
    • Multiple activities of cytochrome P-450
    • K. Ruckpaul and H. Rein, eds., Taylor and Francis, London
    • A. I. Archakov and A. A. Zhukov, Multiple activities of cytochrome P-450, in Frontiers in Biotransformation, Volume 1 (K. Ruckpaul and H. Rein, eds.), Taylor and Francis, London, 1989, pp. 151-175.
    • (1989) Frontiers in Biotransformation , vol.1 , pp. 151-175
    • Archakov, A.I.1    Zhukov, A.A.2
  • 6
    • 0344418496 scopus 로고
    • Biochemical aspects of the mono-oxygenase system in the endoplasmic reticulum of mammalian liver
    • K. Ruckpaul and H. Rein, eds., Akademie Verlag, Berlin
    • K. Ruckpaul and R. Bernhardt, Biochemical aspects of the mono-oxygenase system in the endoplasmic reticulum of mammalian liver, in Cytochrome P-450 (K. Ruckpaul and H. Rein, eds.), Akademie Verlag, Berlin, 1984, pp. 9-57.
    • (1984) Cytochrome P-450 , pp. 9-57
    • Ruckpaul, K.1    Bernhardt, R.2
  • 7
    • 0022628230 scopus 로고
    • Is formation of reactive oxygen by cytochrome P-450 perilous and predictable?
    • A. Bast, Is formation of reactive oxygen by cytochrome P-450 perilous and predictable? Trends Pharmacol. Sci., 7, 266-270 (1986).
    • (1986) Trends Pharmacol. Sci. , vol.7 , pp. 266-270
    • Bast, A.1
  • 8
    • 0018111938 scopus 로고
    • Oxygen reduction by the P450 monooxygenase systems
    • I. C. Gunsalus and S. G. Sligar, Oxygen reduction by the P450 monooxygenase systems, Adv. Enzymol., 47, 1-44 (1978).
    • (1978) Adv. Enzymol. , vol.47 , pp. 1-44
    • Gunsalus, I.C.1    Sligar, S.G.2
  • 9
    • 0025997617 scopus 로고
    • Cytochrome P-450 oxidations and the generation of biologically reactive intermediates
    • C. M. Witmer, R. R. Snyder, D. J. Jollow, G. F. Kaff, J. J. Kocsis, and I. G. Sipes, eds., Plenum, New York
    • F. P. Guengerich, T. Shimada, A. Bondon, and T. L. Macdonald, Cytochrome P-450 oxidations and the generation of biologically reactive intermediates, in Biological Reactive Intermediates IV (C. M. Witmer, R. R. Snyder, D. J. Jollow, G. F. Kaff, J. J. Kocsis, and I. G. Sipes, eds.), Plenum, New York, 1991, pp. 1-11.
    • (1991) Biological Reactive Intermediates IV , pp. 1-11
    • Guengerich, F.P.1    Shimada, T.2    Bondon, A.3    Macdonald, T.L.4
  • 10
    • 0001884824 scopus 로고    scopus 로고
    • The chemistry of cytochrome P450 reactions
    • C. Ioannides, ed., CRC Press, Boca Raton, FL
    • F. P. Guengerich, The chemistry of cytochrome P450 reactions, in Cytochromes P450: Metabolic and Toxicological Aspects (C. Ioannides, ed.), CRC Press, Boca Raton, FL, 1996, pp. 55-74.
    • (1996) Cytochromes P450: Metabolic and Toxicological Aspects , pp. 55-74
    • Guengerich, F.P.1
  • 11
    • 0345712977 scopus 로고
    • Cytochrome P-450 and the metabolism of environmental chemicals
    • A. Jacobs and M. Worwood, eds., Academic Press, New York
    • F. De Matteis, Cytochrome P-450 and the metabolism of environmental chemicals, in Iron in Biochemistry and Medicine II (A. Jacobs and M. Worwood, eds.), Academic Press, New York, 1980, pp. 293-324.
    • (1980) Iron in Biochemistry and Medicine II , pp. 293-324
    • De Matteis, F.1
  • 12
    • 0344850048 scopus 로고
    • Mechanisms of cytochrome P-450-catalyzed reactions
    • R. Sato and T. Omura, eds., Kodansha, Tokyo
    • Y. Ishimura, Mechanisms of cytochrome P-450-catalyzed reactions, in Cytochrome P-450 (R. Sato and T. Omura, eds.), Kodansha, Tokyo, 1978, pp. 209-227.
    • (1978) Cytochrome P-450 , pp. 209-227
    • Ishimura, Y.1
  • 13
    • 84962400669 scopus 로고
    • Oxygen activation and transfer
    • T. Omura, Y. Ishimura, and Y. Fujii-Kuriyama, eds., Kodansha, Tokyo
    • Y. Ishimura, Oxygen activation and transfer, in Cytochrome P-450, 2nd ed. (T. Omura, Y. Ishimura, and Y. Fujii-Kuriyama, eds.), Kodansha, Tokyo, 1993, pp. 80-91.
    • (1993) Cytochrome P-450, 2nd Ed. , pp. 80-91
    • Ishimura, Y.1
  • 14
    • 0002882393 scopus 로고
    • Oxygen activation and transfer
    • P. R. Ortiz de Montellano, ed., Plenum, New York
    • P. R. Ortiz de Montellano, Oxygen activation and transfer, in Cytochrome P-450 (P. R. Ortiz de Montellano, ed.), Plenum, New York, 1986, pp. 217-271.
    • (1986) Cytochrome P-450 , pp. 217-271
    • Ortiz De Montellano, P.R.1
  • 15
    • 0024429854 scopus 로고
    • Cytochrome P-450 catalysis: Radical intermediates and dehydrogenation reactions
    • P. R. Ortiz de Montellano, Cytochrome P-450 catalysis: Radical intermediates and dehydrogenation reactions, Trends Pharmaceut. Sci., 10, 354-359 (1989).
    • (1989) Trends Pharmaceut. Sci. , vol.10 , pp. 354-359
    • Ortiz De Montellano, P.R.1
  • 16
    • 0027470428 scopus 로고
    • Evidence for specific base catalysis in N-dealkylation reactions catalyzed by cytochrome P450 and chloroperoxidase
    • O. Okazaki and F. P. Guengerich, Evidence for specific base catalysis in N-dealkylation reactions catalyzed by cytochrome P450 and chloroperoxidase, J. Biol Chem., 268, 1546-1552 (1993).
    • (1993) J. Biol Chem. , vol.268 , pp. 1546-1552
    • Okazaki, O.1    Guengerich, F.P.2
  • 17
    • 0344418493 scopus 로고
    • Oxidative functionalization reactions
    • B. Testa and P. Jenner, eds., Marcel Dekker, Inc., New York
    • W. F. Trager, Oxidative functionalization reactions, in Concepts in Drug Metabolism (B. Testa and P. Jenner, eds.), Marcel Dekker, Inc., New York, 1980, pp. 177-209.
    • (1980) Concepts in Drug Metabolism , pp. 177-209
    • Trager, W.F.1
  • 18
    • 0000933501 scopus 로고
    • Superoxide radical and superoxide dismutase
    • I. Fridovich, Superoxide radical and superoxide dismutase, Acc. Chem. Res., 5, 321-326 (1972).
    • (1972) Acc. Chem. Res. , vol.5 , pp. 321-326
    • Fridovich, I.1
  • 19
    • 33947335041 scopus 로고
    • Physical theory of chemiluminescence in systems evolving molecular oxygen
    • A. V. Khan and M. Kasha, Physical theory of chemiluminescence in systems evolving molecular oxygen, J. Am. Chem. Soc., 88, 1574-1576 (1966).
    • (1966) J. Am. Chem. Soc. , vol.88 , pp. 1574-1576
    • Khan, A.V.1    Kasha, M.2
  • 20
    • 85038545604 scopus 로고
    • 2O
    • E. Carafoli and G. Semenza, eds., Springer-Verlag, New York
    • 2O, in Membrane Biochemistry (E. Carafoli and G. Semenza, eds.), Springer-Verlag, New York, 1979, pp. 113-119.
    • (1979) Membrane Biochemistry , pp. 113-119
    • Richter, C.1
  • 22
    • 0002032215 scopus 로고
    • Biological roles of singlet oxygen
    • H. H. Wasserman, ed., Academic Press, New York
    • N. Krinsky, Biological roles of singlet oxygen, in Singlet Oxygen (H. H. Wasserman, ed.), Academic Press, New York, 1979, pp. 597-641.
    • (1979) Singlet Oxygen , pp. 597-641
    • Krinsky, N.1
  • 23
    • 0023776303 scopus 로고
    • The paradox of oxygen: Thermodynamics versus toxicity
    • T. E. King, H. S. Mason, and M. Morrison, eds., Alan R. Liss, New York
    • W. H. Koppenol, The paradox of oxygen: Thermodynamics versus toxicity, in Oxidases and Related Redox Systems (T. E. King, H. S. Mason, and M. Morrison, eds.), Alan R. Liss, New York, 1988, pp. 93-109.
    • (1988) Oxidases and Related Redox Systems , pp. 93-109
    • Koppenol, W.H.1
  • 24
    • 0008352830 scopus 로고
    • Biochemical effects of excited state molecular oxygen
    • J. Bland, Biochemical effects of excited state molecular oxygen, J. Chem. Ed., 53, 274-279 (1976).
    • (1976) J. Chem. Ed. , vol.53 , pp. 274-279
    • Bland, J.1
  • 25
    • 0344850045 scopus 로고
    • Activation of oxygen and nitrogen in biological systems
    • D. R. Williams, ed., CC Thomas, Springfield, IL
    • R. F. Jameson and N. J. Blackburn, Activation of oxygen and nitrogen in biological systems, in An Introduction to Bio-Inorganic Chemistry (D. R. Williams, ed.), CC Thomas, Springfield, IL, 1976, pp. 90-119.
    • (1976) An Introduction to Bio-Inorganic Chemistry , pp. 90-119
    • Jameson, R.F.1    Blackburn, N.J.2
  • 26
    • 0014059179 scopus 로고
    • Spectral studies of drug interaction with hepatic microsomal cytochrome
    • J. B. Schenkman, H. Remmer, and R. W. Estabrook, Spectral studies of drug interaction with hepatic microsomal cytochrome, Molec. Pharmacol., 3, 113-123 (1967).
    • (1967) Molec. Pharmacol. , vol.3 , pp. 113-123
    • Schenkman, J.B.1    Remmer, H.2    Estabrook, R.W.3
  • 27
    • 0345281399 scopus 로고
    • Counterpoise-regulation of the steady-state concentration of oxy-cytochrome P-450: A definition of the rate-limiting step in the catalytic cycle of liver microscomal cytochrome P-450
    • R. Sato and R. Kato, eds., Wiley, New York
    • J. Werringloer, Counterpoise-regulation of the steady-state concentration of oxy-cytochrome P-450: A definition of the rate-limiting step in the catalytic cycle of liver microscomal cytochrome P-450, in Microsomes, Drug Oxidations and Drug Toxicity (R. Sato and R. Kato, eds.), Wiley, New York, 1982, pp. 175-186.
    • (1982) Microsomes, Drug Oxidations and Drug Toxicity , pp. 175-186
    • Werringloer, J.1
  • 28
    • 0026022322 scopus 로고
    • The involvement of free radicals in the mechanisms of monooxygenases
    • R. E. White, The involvement of free radicals in the mechanisms of monooxygenases, Pharmacol. Therapeut., 49, 21-42 (1991).
    • (1991) Pharmacol. Therapeut. , vol.49 , pp. 21-42
    • White, R.E.1
  • 29
    • 0013343497 scopus 로고
    • The nature of the primary oxidants in oxidations mediated by metal ions
    • T. E. King, H. S. Mason, and M. Morrison, eds., Pergamon, Oxford
    • C. Walling, The nature of the primary oxidants in oxidations mediated by metal ions, in Oxidases and Related Redox Systems (T. E. King, H. S. Mason, and M. Morrison, eds.), Pergamon, Oxford, 1982, pp. 85-99.
    • (1982) Oxidases and Related Redox Systems , pp. 85-99
    • Walling, C.1
  • 30
    • 0002751786 scopus 로고
    • Oxygen activation and reactivity
    • P. R. Ortiz de Montellano, ed., Plenum, New York
    • P. R. Ortiz de Montellano, Oxygen activation and reactivity, in Cytochrome P450 (P. R. Ortiz de Montellano, ed.), Plenum, New York, 1995, pp. 245-303.
    • (1995) Cytochrome P450 , pp. 245-303
    • Ortiz De Montellano, P.R.1
  • 31
    • 0011285882 scopus 로고
    • Cytochrome P-450, a versatile catalyst in monooxygenation reactions
    • T. G. Spiro, ed., Wiley, New York
    • M. J. Coon and R. E. White, Cytochrome P-450, a versatile catalyst in monooxygenation reactions, in Metal Ion Activation of Dioxygen (T. G. Spiro, ed.), Wiley, New York, 1980, pp. 73-123.
    • (1980) Metal Ion Activation of Dioxygen , pp. 73-123
    • Coon, M.J.1    White, R.E.2
  • 32
    • 0344418490 scopus 로고
    • Mechanism of action of cytochrome P-450 studies with peracids as oxygen donors
    • W. S. Caughey, ed., Academic Press, New York
    • R. C. Blake and M. J. Coon, Mechanism of action of cytochrome P-450 studies with peracids as oxygen donors, in Biochemical and Clinical Aspects of Oxygen (W. S. Caughey, ed.), Academic Press, New York, 1979, pp. 263-275.
    • (1979) Biochemical and Clinical Aspects of Oxygen , pp. 263-275
    • Blake, R.C.1    Coon, M.J.2
  • 33
    • 0019877830 scopus 로고
    • On the mechanism of action of cytochrome P-450
    • R. C. Blake and M. J. Coon, On the mechanism of action of cytochrome P-450, J. Biol. Chem., 256, 12127-12133 (1981).
    • (1981) J. Biol. Chem. , vol.256 , pp. 12127-12133
    • Blake, R.C.1    Coon, M.J.2
  • 34
    • 0024506371 scopus 로고
    • On the mechanism of action of cytochrome P-450: Spectral intermediates in the reaction with iodosobenzene and its derivatives
    • R. C. Blake and M. J. Coon, On the mechanism of action of cytochrome P-450: Spectral intermediates in the reaction with iodosobenzene and its derivatives, J. Biol. Chem., 264, 3694-3701 (1989).
    • (1989) J. Biol. Chem. , vol.264 , pp. 3694-3701
    • Blake, R.C.1    Coon, M.J.2
  • 35
    • 0018847714 scopus 로고
    • Mechanisms of reaction of hemoproteins with oxygen and hydrogen peroxide in the oxidation of organic substrates
    • C. E. Castro, Mechanisms of reaction of hemoproteins with oxygen and hydrogen peroxide in the oxidation of organic substrates, Pharmacol. Therap., 10, 171-189 (1980).
    • (1980) Pharmacol. Therap. , vol.10 , pp. 171-189
    • Castro, C.E.1
  • 36
    • 0345281398 scopus 로고
    • The chemical basis of mixed function oxidation
    • T. E. King, H. S. Mason, and M. Morrison, eds., Pergamon, Oxford
    • S. G. Sligar, K. A. Kennedy, and D. C. Pearson, The chemical basis of mixed function oxidation, in Oxidases and Related Redox Systems (T. E. King, H. S. Mason, and M. Morrison, eds.), Pergamon, Oxford, 1982, pp. 837-855.
    • (1982) Oxidases and Related Redox Systems , pp. 837-855
    • Sligar, S.G.1    Kennedy, K.A.2    Pearson, D.C.3
  • 37
    • 0021326691 scopus 로고
    • Bio-organic chemistry and cytochrome P-450-dependent catalysis
    • S. G. Sligar, M. H. Gelb, and D. C. Heimbrook, Bio-organic chemistry and cytochrome P-450-dependent catalysis, Xenobiotica, 14, 63-86 (1984).
    • (1984) Xenobiotica , vol.14 , pp. 63-86
    • Sligar, S.G.1    Gelb, M.H.2    Heimbrook, D.C.3
  • 38
    • 0005085193 scopus 로고
    • Oxo- and peroxo-transition metal species in chemical and biochemical oxidations: Possible models for the oxygen activation and transfer catalyzed by cytochrome P-450
    • W. S. Caughey, ed., Academic Press, New York
    • J. T. Groves and G. A. McClusky, Oxo- and peroxo-transition metal species in chemical and biochemical oxidations: Possible models for the oxygen activation and transfer catalyzed by cytochrome P-450, in Biochemical and Clinical Aspects of Oxygen (W. S. Caughey, ed.), Academic Press, New York, 1979, pp. 277-309.
    • (1979) Biochemical and Clinical Aspects of Oxygen , pp. 277-309
    • Groves, J.T.1    McClusky, G.A.2
  • 39
    • 33845278472 scopus 로고
    • Reactive iron porphyrin derivatives related to the catalytic cycles of cytochrome P-450 and peroxidase: Studies of the mechanism of oxygen activation
    • J. T. Groves and Y. Watanabe, Reactive iron porphyrin derivatives related to the catalytic cycles of cytochrome P-450 and peroxidase: Studies of the mechanism of oxygen activation, J. Am. Chem. Soc., 110, 8443-8452 (1988).
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 8443-8452
    • Groves, J.T.1    Watanabe, Y.2
  • 40
    • 0344418487 scopus 로고
    • The microsomal electron transport system revisited: A new look at cytochrome P-450 function
    • T. E. King, H. S. Mason, and M. Morrison, eds., Pergamon, Oxford
    • R. W. Estabrook, J. Werringloer, B. S. S. Masters, and J. A. Peterson, The microsomal electron transport system revisited: A new look at cytochrome P-450 function, in Oxidases and Related Redox Systems (T. E. King, H. S. Mason, and M. Morrison, eds.), Pergamon, Oxford, 1982, pp. 811-835.
    • (1982) Oxidases and Related Redox Systems , pp. 811-835
    • Estabrook, R.W.1    Werringloer, J.2    Masters, B.S.S.3    Peterson, J.A.4
  • 41
    • 0345281397 scopus 로고
    • - and peroxide-supported hydroxylation reactions
    • T. E. King, H. S. Mason, and M. Morrison, eds., Pergamon, Oxford
    • - and peroxide-supported hydroxylation reactions, in Oxidases and Related Redox Systems (T. E. King, H. S. Mason, and M. Morrison, eds.), Pergamon, Oxford, 1982, pp. 857-885.
    • (1982) Oxidases and Related Redox Systems , pp. 857-885
    • Coon, M.J.1    White, R.E.2    Blake, R.C.3
  • 43
    • 0018817225 scopus 로고
    • Oxygen activation by cytochrome P-450
    • R. E. White and M. J. Coon, Oxygen activation by cytochrome P-450, Annu. Rev. Biochem., 49, 315-356 (1980).
    • (1980) Annu. Rev. Biochem. , vol.49 , pp. 315-356
    • White, R.E.1    Coon, M.J.2
  • 44
    • 0342446136 scopus 로고
    • Biophysical properties of cytochrome P-450, analysis of the reaction mechanism-thermodynamic aspects
    • K. Ruckpaul and H. Rein, eds., Akademie Verlag, Berlin
    • H. Rein, C. Jung, O. Ristau, and J. Friedrich, Biophysical properties of cytochrome P-450, analysis of the reaction mechanism-thermodynamic aspects, in Cytochrome P-450 (K. Ruckpaul and H. Rein, eds.), Akademie Verlag, Berlin, 1984, pp. 163-249.
    • (1984) Cytochrome P-450 , pp. 163-249
    • Rein, H.1    Jung, C.2    Ristau, O.3    Friedrich, J.4
  • 45
    • 33845379583 scopus 로고
    • Control of heme protein redox potential and reduction rate: Linear free energy relation between potential and ferric spin state equilibrium
    • M. T. Fisher and S. G. Sligar, Control of heme protein redox potential and reduction rate: Linear free energy relation between potential and ferric spin state equilibrium, J. Am. Chem. Soc., 107, 5018-5019 (1985).
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 5018-5019
    • Fisher, M.T.1    Sligar, S.G.2
  • 46
    • 0021832318 scopus 로고
    • High-pressure investigations of cytochrome P-450 spin and substrate binding equilibria
    • M. T. Fisher, S. F. Scarlata, and S. G. Sligar, High-pressure investigations of cytochrome P-450 spin and substrate binding equilibria, Arch. Biochem. Biophys., 240, 456-463 (1985).
    • (1985) Arch. Biochem. Biophys. , vol.240 , pp. 456-463
    • Fisher, M.T.1    Scarlata, S.F.2    Sligar, S.G.3
  • 47
    • 0343751441 scopus 로고
    • Cytochrome P-450: Biophysical properties and catalytic function
    • D. Dolphin, ed., Academic Press, New York
    • B. W. Griffin, J. A. Peterson, and R. W. Estabrook, Cytochrome P-450: Biophysical properties and catalytic function, in The Porphyrins, Volume 7 (D. Dolphin, ed.), Academic Press, New York, 1979, pp. 333-375.
    • (1979) The Porphyrins , vol.7 , pp. 333-375
    • Griffin, B.W.1    Peterson, J.A.2    Estabrook, R.W.3
  • 48
    • 0345281396 scopus 로고
    • Oxygen activation by heme-containing mono-oxygenases: Cytochrome P-450 and secondary amine monooxygenase. Active site structures and mechanisms of action
    • K. Ruckpaul and H. Rein, eds., Taylor and Francis, London
    • B. K. Hawkins and J. H. Dawson, Oxygen activation by heme-containing mono-oxygenases: Cytochrome P-450 and secondary amine monooxygenase. Active site structures and mechanisms of action, in Frontiers in Biotransformation, Volume II (K. Ruckpaul and H. Rein, eds.), Taylor and Francis, London, 1972, pp. 4740-4746.
    • (1972) Frontiers in Biotransformation , vol.2 , pp. 4740-4746
    • Hawkins, B.K.1    Dawson, J.H.2
  • 49
    • 0001700868 scopus 로고
    • Elementary electronic excitations and the mechanism of cytochrome P450
    • P. M. Champion, Elementary electronic excitations and the mechanism of cytochrome P450, J. Am. Chem. Soc., 111, 3433-3434 (1989).
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 3433-3434
    • Champion, P.M.1
  • 50
    • 33845281456 scopus 로고
    • Alteration of heme axial ligands by site-directed mutagenesis: A cytochrome becomes a catalytic demethylase
    • S. G. Sligar, K. D. Egeberg, J. T. Sage, D. Morikis, and P. M. Champion, Alteration of heme axial ligands by site-directed mutagenesis: A cytochrome becomes a catalytic demethylase, J. Am. Chem. Soc., 109, 7896-7897 (1987).
    • (1987) J. Am. Chem. Soc. , vol.109 , pp. 7896-7897
    • Sligar, S.G.1    Egeberg, K.D.2    Sage, J.T.3    Morikis, D.4    Champion, P.M.5
  • 51
    • 0022919721 scopus 로고
    • Crystal structure of substrate-free Pseudomonas putida cytochrome P-450
    • T. L. Poulos, B. C. Finzel, and A. J. Howard, Crystal structure of substrate-free Pseudomonas putida cytochrome P-450, Biochemistry, 25, 5314-5322 (1986).
    • (1986) Biochemistry , vol.25 , pp. 5314-5322
    • Poulos, T.L.1    Finzel, B.C.2    Howard, A.J.3
  • 53
    • 0015495445 scopus 로고
    • Camphor binding by Pseudomonas putida cytochrome P-450: Kinetics and thermodynamics of the reaction
    • B. W. Griffin and J. A. Peterson, Camphor binding by Pseudomonas putida cytochrome P-450: Kinetics and thermodynamics of the reaction, Biochemistry, 11, 4740-4746 (1972).
    • (1972) Biochemistry , vol.11 , pp. 4740-4746
    • Griffin, B.W.1    Peterson, J.A.2
  • 54
    • 0017170343 scopus 로고
    • Coupling of spin, substrate and redox equilibria in cytochrome P-450
    • S. G. Sligar, Coupling of spin, substrate and redox equilibria in cytochrome P-450, Biochemistry, 15, 5399-5406 (1976).
    • (1976) Biochemistry , vol.15 , pp. 5399-5406
    • Sligar, S.G.1
  • 56
    • 0018129356 scopus 로고
    • Haem exposure as the determinate of oxidation-reduction potential of haem proteins
    • E. Stellwagen, Haem exposure as the determinate of oxidation-reduction potential of haem proteins, Nature, 275, 73-74 (1978).
    • (1978) Nature , vol.275 , pp. 73-74
    • Stellwagen, E.1
  • 57
    • 0015928945 scopus 로고
    • A theoretical model for the effects of local nonpolar heme environment on the redox potentials in cytochromes
    • R. J. Kassner, A theoretical model for the effects of local nonpolar heme environment on the redox potentials in cytochromes, J. Am. Chem. Soc., 95, 2674-2677 (1973).
    • (1973) J. Am. Chem. Soc. , vol.95 , pp. 2674-2677
    • Kassner, R.J.1
  • 59
    • 0001127948 scopus 로고
    • A thermodynamic model of regulation: Modulation of redox equilibria in camphor monoxygenase
    • S. G. Sligar and I. C. Gunsalus, A thermodynamic model of regulation: Modulation of redox equilibria in camphor monoxygenase, Proc. Natl. Acad. Sci. USA, 73, 1078-1082 (1976).
    • (1976) Proc. Natl. Acad. Sci. USA , vol.73 , pp. 1078-1082
    • Sligar, S.G.1    Gunsalus, I.C.2
  • 60
    • 0006494160 scopus 로고
    • Substrate interaction with cytochrome P-450
    • J. B. Schenkman and D. Kupfer, eds., Pergamon, Oxford
    • J. B. Schenkman, S. G. Sligar, and D. L. Cinti, Substrate interaction with cytochrome P-450, in Hepatic Cytochrome P-450 Monooxygenase System (J. B. Schenkman and D. Kupfer, eds.), Pergamon, Oxford, 1982, pp. 587-615.
    • (1982) Hepatic Cytochrome P-450 Monooxygenase System , pp. 587-615
    • Schenkman, J.B.1    Sligar, S.G.2    Cinti, D.L.3
  • 61
    • 0021363059 scopus 로고
    • Cytochrome P-450 spin state: Inorganic biochemistry of haem iron ligation and functional significance
    • G. G. Gibson and P. P. Tamburini, Cytochrome P-450 spin state: Inorganic biochemistry of haem iron ligation and functional significance, Xenobiotica, 14, 27-47 (1984).
    • (1984) Xenobiotica , vol.14 , pp. 27-47
    • Gibson, G.G.1    Tamburini, P.P.2
  • 63
    • 0014964826 scopus 로고
    • One interpretation of the thermal equilibrium between high-spin and low-spin states in ferrihemoproteins
    • J. Otsuka, One interpretation of the thermal equilibrium between high-spin and low-spin states in ferrihemoproteins, Biochim. Biophys. Acta, 214, 233-235 (1970).
    • (1970) Biochim. Biophys. Acta , vol.214 , pp. 233-235
    • Otsuka, J.1
  • 64
    • 0001314440 scopus 로고
    • Revised values of effective ionic radii
    • R. D. Shannon and C. T. Prewitt, Revised values of effective ionic radii, Acta Crystallogr. 1326, 1046-1048 (1970).
    • (1970) Acta Crystallogr. , vol.1326 , pp. 1046-1048
    • Shannon, R.D.1    Prewitt, C.T.2
  • 65
    • 0010976907 scopus 로고
    • Haem-proteins and oxygen
    • A. Jacobs and M. Worwood, eds., Academic Press, New York
    • R. J. P. Williams, Haem-proteins and oxygen, in Iron in Biochemistry and Medicine (A. Jacobs and M. Worwood, eds.), Academic Press, New York, 1974, pp. 183-219.
    • (1974) Iron in Biochemistry and Medicine , pp. 183-219
    • Williams, R.J.P.1
  • 66
    • 0021096850 scopus 로고
    • Oxidation-reduction properties of rat liver cytochromes P-450 and NADPH-cytochrome P-450 reductase related to catalysis in reconstituted systems
    • F. P. Guengerich, Oxidation-reduction properties of rat liver cytochromes P-450 and NADPH-cytochrome P-450 reductase related to catalysis in reconstituted systems, Biochemistry, 22, 2811-2820 (1983).
    • (1983) Biochemistry , vol.22 , pp. 2811-2820
    • Guengerich, F.P.1
  • 67
    • 0020365954 scopus 로고
    • scc: Effect of cholesterol and intermediates on its stability and optical characteristics
    • scc: Effect of cholesterol and intermediates on its stability and optical characteristics, J. Biol. Chem., 257, 9309-9314 (1982).
    • (1982) J. Biol. Chem. , vol.257 , pp. 9309-9314
    • Tuckey, R.C.1    Kamin, H.2
  • 68
    • 0019822916 scopus 로고
    • Beef adrenal cortical cytochrome P-450 which catalyzes the conversion of cholesterol to pregnenolone: Oxidation-reduction potentials of the free, steroid-complexed and adrenodoxin-complexed P-450
    • D. R. Light and N. R. Orme-Johnson, Beef adrenal cortical cytochrome P-450 which catalyzes the conversion of cholesterol to pregnenolone: Oxidation-reduction potentials of the free, steroid-complexed and adrenodoxin-complexed P-450, J. Biol. Chem., 256, 343-350 (1981).
    • (1981) J. Biol. Chem. , vol.256 , pp. 343-350
    • Light, D.R.1    Orme-Johnson, N.R.2
  • 69
    • 0006875943 scopus 로고
    • The molecular basis of electron transfer in cytochrome P-450 enzyme systems
    • K. Ruckpaul and H. Rein, eds., Akademie Verlag, Berlin
    • R. D. Gray, The molecular basis of electron transfer in cytochrome P-450 enzyme systems, in Frontiers in Biotransformation, Volume 7 (K. Ruckpaul and H. Rein, eds.), Akademie Verlag, Berlin, 1992, pp. 321-350.
    • (1992) Frontiers in Biotransformation , vol.7 , pp. 321-350
    • Gray, R.D.1
  • 70
    • 0001225288 scopus 로고
    • Electron transfer
    • I. Bertini, H. B. Gray, S. J. Lippard, and J. S. Valentine, eds., University Sciences Books, Mill Valley, CA
    • H. B. Gray and W. R. Ellis, Electron transfer, in Bioinorganic Chemistry (I. Bertini, H. B. Gray, S. J. Lippard, and J. S. Valentine, eds.), University Sciences Books, Mill Valley, CA, 1994, pp. 315-363.
    • (1994) Bioinorganic Chemistry , pp. 315-363
    • Gray, H.B.1    Ellis, W.R.2
  • 71
    • 33750128829 scopus 로고
    • Intramolecular long-distance electron transfer in organic molecules
    • G. L. Closs and J. R. Miller, Intramolecular long-distance electron transfer in organic molecules, Science, 240, 440-447 (1988).
    • (1988) Science , vol.240 , pp. 440-447
    • Closs, G.L.1    Miller, J.R.2
  • 72
    • 0345712972 scopus 로고
    • The mechanism of electron transfer in the electron transport chain
    • T. E. King, H. S. Mason, and M. Morrison, eds., Pergamon, Oxford
    • J. J. Hopfield, The mechanism of electron transfer in the electron transport chain, in Oxidases and Related Redox Systems (T. E. King, H. S. Mason, and M. Morrison, eds.), Pergamon, Oxford, 1982, pp. 35-60.
    • (1982) Oxidases and Related Redox Systems , pp. 35-60
    • Hopfield, J.J.1
  • 74
    • 0006876258 scopus 로고
    • Quantitative structure-activity relationships for the reaction of hydrated electrons with heme proteins
    • B. B. Hasinoff, Quantitative structure-activity relationships for the reaction of hydrated electrons with heme proteins, Biochim. Biophys. Acta, 829, 1-5 (1985).
    • (1985) Biochim. Biophys. Acta , vol.829 , pp. 1-5
    • Hasinoff, B.B.1
  • 76
    • 0017076594 scopus 로고
    • Spectral intermediates in the reaction of oxygen with purified liver microsomal cytochrome P-450
    • F. P. Guengerich, D. P. Ballou, and M. J. Coon, Spectral intermediates in the reaction of oxygen with purified liver microsomal cytochrome P-450, Biochem. Biophys. Res. Commun., 70, 951-956 (1976).
    • (1976) Biochem. Biophys. Res. Commun. , vol.70 , pp. 951-956
    • Guengerich, F.P.1    Ballou, D.P.2    Coon, M.J.3
  • 77
    • 33845552473 scopus 로고
    • Formation of superoxide ion via one-electron transfer from electron donors to singlet oxygen
    • I. Saito, T. Matsuura, and K. Inoue, Formation of superoxide ion via one-electron transfer from electron donors to singlet oxygen, J. Am. Chem. Soc., 105, 3200-3206 (1983).
    • (1983) J. Am. Chem. Soc. , vol.105 , pp. 3200-3206
    • Saito, I.1    Matsuura, T.2    Inoue, K.3
  • 80
    • 0010290469 scopus 로고
    • Ligand-dependent redox chemistry of Glycera dibranchiata hemoglobin
    • A. W. Addison and S. Burman, Ligand-dependent redox chemistry of Glycera dibranchiata hemoglobin, Biochim. Biophys. Acta, 828, 362-368 (1985).
    • (1985) Biochim. Biophys. Acta , vol.828 , pp. 362-368
    • Addison, A.W.1    Burman, S.2
  • 81
    • 0002208332 scopus 로고
    • Biological and synthetic dioxygen carriers
    • I. Bertini, H. B. Gray, S. J. Lippard, and J. S. Valentine, eds., University Science Books, Mill Valley, CA
    • G. B. Jameson and J. A. Ibers, Biological and synthetic dioxygen carriers, in Bioinorganic Chemistry (I. Bertini, H. B. Gray, S. J. Lippard, and J. S. Valentine, eds.), University Science Books, Mill Valley, CA, 1994, pp. 167-251.
    • (1994) Bioinorganic Chemistry , pp. 167-251
    • Jameson, G.B.1    Ibers, J.A.2
  • 82
    • 0001124777 scopus 로고
    • The transition metal-isocyanide bond: An approximate molecular orbital study
    • A. C. Sarapu and R. F. Fenske, The transition metal-isocyanide bond: An approximate molecular orbital study, Inorg. Chem., 14, 247-253 (1975).
    • (1975) Inorg. Chem. , vol.14 , pp. 247-253
    • Sarapu, A.C.1    Fenske, R.F.2
  • 83
    • 0001626605 scopus 로고
    • 6 octahedral complexes
    • 6 octahedral complexes, J. Am. Chem. Soc., 104, 1299-1304 (1982).
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 1299-1304
    • Bursten, B.E.1
  • 85
    • 0344418484 scopus 로고
    • Oxidation-reduction chemistry of hydrogen peroxide in aprotic and aqueous solution
    • M. M. Morrison, J. L. Roberts, and D. T. Sawyer, Oxidation-reduction chemistry of hydrogen peroxide in aprotic and aqueous solution, Inorgan. Chem., 18, 1971-1979 (1979).
    • (1979) Inorgan. Chem. , vol.18 , pp. 1971-1979
    • Morrison, M.M.1    Roberts, J.L.2    Sawyer, D.T.3
  • 86
    • 0017101786 scopus 로고
    • The kinetics of the reduction of cytochrome c by the superoxide anion radical
    • W. H. Koppenol, K. J. H. van Burren, J. Butler, and R. Braams, The kinetics of the reduction of cytochrome c by the superoxide anion radical, Biochim. Biophys. Acta, 449, 157-168 (1976).
    • (1976) Biochim. Biophys. Acta , vol.449 , pp. 157-168
    • Koppenol, W.H.1    Van Burren, K.J.H.2    Butler, J.3    Braams, R.4
  • 87
    • 21044457844 scopus 로고
    • The organic chemistry of superoxide
    • E. Lee-Ruff, The organic chemistry of superoxide, Chem. Soc. Rev., 6, 195-214 (1977).
    • (1977) Chem. Soc. Rev. , vol.6 , pp. 195-214
    • Lee-Ruff, E.1
  • 88
    • 0344850041 scopus 로고
    • The superoxide ion and the toxicity of molecular oxygen
    • R. J. P. Williams and J. J. R. F. DaSilva, eds., Academic Press, New York
    • H. A. O. Hill, The superoxide ion and the toxicity of molecular oxygen, in New Trends in Bio-Inorganic Chemistry (R. J. P. Williams and J. J. R. F. DaSilva, eds.), Academic Press, New York, 1978, pp. 173-208.
    • (1978) New Trends in Bio-Inorganic Chemistry , pp. 173-208
    • Hill, H.A.O.1
  • 92
    • 33845559486 scopus 로고
    • Redox chemistry of dioxygen species
    • J. Wilshire and D. T. Sawyer, Redox chemistry of dioxygen species, Acc. Chem. Res., 12, 105-110 (1979).
    • (1979) Acc. Chem. Res. , vol.12 , pp. 105-110
    • Wilshire, J.1    Sawyer, D.T.2
  • 93
    • 0000007016 scopus 로고
    • Proton-induced disproportionation of superoxide ion in aprotic media
    • D.-H. Chin, G. Chiericato, E.-J. Nanni, and D. T. Sawyer, Proton-induced disproportionation of superoxide ion in aprotic media, J. Am. Chem. Soc., 104, 1296-1299 (1982).
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 1296-1299
    • Chin, D.-H.1    Chiericato, G.2    Nanni, E.-J.3    Sawyer, D.T.4
  • 95
    • 0345705424 scopus 로고
    • cam: Substrate specificity, catalysis and electron transfer
    • K. Ruckpaul and H. Rein, eds., Taylor and Francis, London
    • cam: Substrate specificity, catalysis and electron transfer, in Frontiers in Biotransformation, Volume 4 (K. Ruckpaul and H. Rein, eds.), Taylor and Francis, London, 1991, pp. 54-86.
    • (1991) Frontiers in Biotransformation , vol.4 , pp. 54-86
    • Martinis, S.A.1    Ropp, J.D.2    Sligar, S.G.3    Gunsalus, I.C.4
  • 97
    • 0027056273 scopus 로고
    • Crystal structure of a complex between electron transfer partners, cytochrome c peroxidase and cytochrome c
    • H. Pelletier and J. Kraut, Crystal structure of a complex between electron transfer partners, cytochrome c peroxidase and cytochrome c, Science, 258, 1748-1755 (1992).
    • (1992) Science , vol.258 , pp. 1748-1755
    • Pelletier, H.1    Kraut, J.2
  • 100
    • 0003059166 scopus 로고
    • cam: Factors controlling substrate metabolism
    • K. Ruckpaul and H. Rein, eds., Taylor and Francis, London
    • cam: Factors controlling substrate metabolism, in Frontiers in Biotransformation, Volume 7 (K. Ruckpaul and H. Rein, eds.), Taylor and Francis, London, 1992, pp. 1-43.
    • (1992) Frontiers in Biotransformation , vol.7 , pp. 1-43
    • Raag, R.1    Poulos, T.L.2
  • 101
    • 0344850037 scopus 로고
    • The cytochrome P-450 reaction mechanism - Kinetic aspects
    • K. Ruckpaul and H. Rein, eds., Akademie-Verlag, Berlin
    • J. Blanck, G. Smettan, and S. Greschner, The cytochrome P-450 reaction mechanism - kinetic aspects, in Cytochrome P-450 (K. Ruckpaul and H. Rein, eds.), Akademie-Verlag, Berlin, 1984, pp. 111-162.
    • (1984) Cytochrome P-450 , pp. 111-162
    • Blanck, J.1    Smettan, G.2    Greschner, S.3
  • 102
    • 0242392865 scopus 로고
    • Structure and regulation of UDP glucuronosyltransferase
    • K. Ruckpaul and H. Rein, eds., Taylor and Francis, London
    • P. I. Mackenzie, Structure and regulation of UDP glucuronosyltransferase, in Frontiers in Biotransformation, Volume 2 (K. Ruckpaul and H. Rein, eds.), Taylor and Francis, London, 1990, pp. 211-243.
    • (1990) Frontiers in Biotransformation , vol.2 , pp. 211-243
    • Mackenzie, P.I.1
  • 104
    • 0000895446 scopus 로고
    • Tunneling pathway and redox-state-dependent electronic couplings at nearly fixed distance in electron-transfer proteins
    • D. N. Beratan, J. N. Betts, and J. N. Onuchic, Tunneling pathway and redox-state-dependent electronic couplings at nearly fixed distance in electron-transfer proteins, J. Phys. Chem., 96, 2852-2855 (1992).
    • (1992) J. Phys. Chem. , vol.96 , pp. 2852-2855
    • Beratan, D.N.1    Betts, J.N.2    Onuchic, J.N.3
  • 106
    • 0343537840 scopus 로고
    • Regulation mechanisms of the activity of the hepatic endoplasmic cytochrome P-450
    • K. Ruckpaul and H. Rein, eds., Taylor and Francis, London
    • K. Ruckpaul, H. Rein, and J. Blanck, Regulation mechanisms of the activity of the hepatic endoplasmic cytochrome P-450, in Frontiers in Biotransformation, Volume 1 (K. Ruckpaul and H. Rein, eds.), Taylor and Francis, London, 1989, pp. 1-65.
    • (1989) Frontiers in Biotransformation , vol.1 , pp. 1-65
    • Ruckpaul, K.1    Rein, H.2    Blanck, J.3
  • 107
    • 0023719918 scopus 로고
    • Evidence for concerted kinetic oxidation of progesterone by purified rat hepatic cytochrome P-450g
    • D. C. Swinney, D. E. Ryan, P. E. Thomas, and W. Levin, Evidence for concerted kinetic oxidation of progesterone by purified rat hepatic cytochrome P-450g, Biochemistry, 27, 5461-5470 (1988).
    • (1988) Biochemistry , vol.27 , pp. 5461-5470
    • Swinney, D.C.1    Ryan, D.E.2    Thomas, P.E.3    Levin, W.4
  • 108
    • 0001764001 scopus 로고
    • Formation, characterization and reactivity of the oxene adduct of [tetrakis (2,6-dichlorophenyl)porphinato] iron(III) perchlorate in acetonitrile: Model for the reactive intermediate of cytochrome P-450
    • H. Sugimoto, H.-C. Tung, and D. T. Sawyer, Formation, characterization and reactivity of the oxene adduct of [tetrakis (2,6-dichlorophenyl)porphinato] iron(III) perchlorate in acetonitrile: Model for the reactive intermediate of cytochrome P-450, J. Am. Chem. Soc., 110, 2465-2470 (1988).
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 2465-2470
    • Sugimoto, H.1    Tung, H.-C.2    Sawyer, D.T.3
  • 112
    • 0023937270 scopus 로고
    • Computed redox potentials and the design of bioreductive agents
    • C. A. Reynolds, P. M. King, and W. G. Richards, Computed redox potentials and the design of bioreductive agents, Nature, 334, 80-82 (1988).
    • (1988) Nature , vol.334 , pp. 80-82
    • Reynolds, C.A.1    King, P.M.2    Richards, W.G.3
  • 113
    • 0001149840 scopus 로고
    • Olefin formation in the oxidative deformylation of aldehydes by cytochrome P-450: Mechanistic implications for catalysis by oxygen-derived peroxide
    • A. D. N. Vaz, 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
  • 114
    • 0000787430 scopus 로고
    • Model reactions related to cytochrome P-450: Effects of alkene structure on the rates of epoxide formation
    • T. G. Traylor and F. Xu, Model reactions related to cytochrome P-450: Effects of alkene structure on the rates of epoxide formation, J. Am. Chem. Soc., 110, 1953-1958 (1988).
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 1953-1958
    • Traylor, T.G.1    Xu, F.2
  • 116
    • 0028132823 scopus 로고
    • Molecular orbital-based quantitative structure-activity relationship for the cytochrome P450-catalyzed 4-hydroxylation of halogenated anilines
    • N. H. P. Cnubben, S. Peelen, J.-W. Borst, J. Vervoort, C. Veeger, and I. M. C. M. Rietjens, Molecular orbital-based quantitative structure-activity relationship for the cytochrome P450-catalyzed 4-hydroxylation of halogenated anilines, Chem. Res. Toxicol., 7, 590-598 (1994).
    • (1994) Chem. Res. Toxicol. , vol.7 , pp. 590-598
    • Cnubben, N.H.P.1    Peelen, S.2    Borst, J.-W.3    Vervoort, J.4    Veeger, C.5    Rietjens, I.M.C.M.6
  • 118
    • 0025150366 scopus 로고
    • Theoretical studies on cytochrome P-450 mediated hydroxylation: A predictive model for hydrogen atom abstractions
    • K. R. Korzekwa, J. R. Jones, and J. R. Gillette, Theoretical studies on cytochrome P-450 mediated hydroxylation: A predictive model for hydrogen atom abstractions, J. Am. Chem. Soc., 112, 7042-7046 (1990).
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 7042-7046
    • Korzekwa, K.R.1    Jones, J.R.2    Gillette, J.R.3
  • 119
    • 0344772870 scopus 로고
    • Hydrogen abstractions from methyl groups by atomic oxygen: Kinetic isotope effects calculated from MNDO/ UHF results and an assessment of their applicability to monooxygenase-dependent hydroxylations
    • A. T. Pudzianowski and G. H. Loew, Hydrogen abstractions from methyl groups by atomic oxygen: Kinetic isotope effects calculated from MNDO/ UHF results and an assessment of their applicability to monooxygenase-dependent hydroxylations, J. Phys. Chem., 87, 1081-1085 (1983).
    • (1983) J. Phys. Chem. , vol.87 , pp. 1081-1085
    • Pudzianowski, A.T.1    Loew, G.H.2
  • 121
    • 0028947612 scopus 로고
    • Mechanism of oxidative amine dealkylation of substituted N,N-dimethylanilines by cytochrome P-450: Application of isotope effect profiles
    • S. B. Karki, J. P. Dinnocenzo, J. P. Jones, and K. R. Korzekwa, Mechanism of oxidative amine dealkylation of substituted N,N-dimethylanilines by cytochrome P-450: Application of isotope effect 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
  • 122
    • 0008233626 scopus 로고
    • Deuterium isotope effect and its significance in cytochrome P-450 catalyzed reactions
    • K. Ruckpaul and H. Rein, eds., Taylor and Francis, London
    • A. Y. H. Lu, Deuterium isotope effect and its significance in cytochrome P-450 catalyzed reactions, in Frontiers in Biotransformation, Volume 7 (K. Ruckpaul and H. Rein, eds.), Taylor and Francis, London, 1992, pp. 351-363.
    • (1992) Frontiers in Biotransformation , vol.7 , pp. 351-363
    • Lu, A.Y.H.1
  • 123
    • 0021766923 scopus 로고
    • Microsomal hydroxylation of specifically deuterated monosubstituted benzenes: Evidence for direct aromatic hydroxylation
    • R. P. Hanzlik, K. Hogberg, and C. M. Judson, Microsomal hydroxylation of specifically deuterated monosubstituted benzenes: Evidence for direct aromatic hydroxylation, Biochemistry, 23, 3048-3055 (1984).
    • (1984) Biochemistry , vol.23 , pp. 3048-3055
    • Hanzlik, R.P.1    Hogberg, K.2    Judson, C.M.3
  • 124
    • 0027216023 scopus 로고
    • Regioselectivity of cytochrome P-450 catalyzed hydroxylation of fluoro-benzenes predicted by calculated frontier orbital substrate characteristics
    • I. M. C. M. Rietjens, A. E. M. F. Soffers, C. Veeger, and J. Vervoort, Regioselectivity of cytochrome P-450 catalyzed hydroxylation of fluoro-benzenes predicted by calculated frontier orbital substrate characteristics, Biochemistry, 32, 4801-4812 (1993).
    • (1993) Biochemistry , vol.32 , pp. 4801-4812
    • Rietjens, I.M.C.M.1    Soffers, A.E.M.F.2    Veeger, C.3    Vervoort, J.4
  • 125
    • 0002308149 scopus 로고
    • Comparison of the peroxidase activity of hemoproteins and cytochrome P450
    • P. R. Ortiz de Montellano, ed., Plenum, New York
    • L. J. Marnett and T. A. Kennedy, Comparison of the peroxidase activity of hemoproteins and cytochrome P450, in Cytochrome P450 (P. R. Ortiz de Montellano, ed.), Plenum, New York, 1995, pp. 49-80.
    • (1995) Cytochrome P450 , pp. 49-80
    • Marnett, L.J.1    Kennedy, T.A.2
  • 127
    • 0016848752 scopus 로고
    • Electronic structure and electric field gradients in oxyhemoglobin and cytochrome P-450 model compounds
    • G. H. Loew and R. F. Kirchner, Electronic structure and electric field gradients in oxyhemoglobin and cytochrome P-450 model compounds, J. Am. Chem. Soc., 97, 7388-7390 (1975).
    • (1975) J. Am. Chem. Soc. , vol.97 , pp. 7388-7390
    • Loew, G.H.1    Kirchner, R.F.2
  • 128
    • 2642660798 scopus 로고
    • Electronic structure and properties of model oxy and carboxy ferrous cytochrome P450: Comparison of semi-empirical and ab-initio calculations
    • M.-M. Rohmer and G. H. Loew, Electronic structure and properties of model oxy and carboxy ferrous cytochrome P450: Comparison of semi-empirical and ab-initio calculations, Int. J. Quantum Chem., Quantum Biol. Symp., 6, 93-104 (1979).
    • (1979) Int. J. Quantum Chem., Quantum Biol. Symp. , vol.6 , pp. 93-104
    • Rohmer, M.-M.1    Loew, G.H.2
  • 129
    • 0005265915 scopus 로고
    • Metabolic reactions: Mechanisms of substrate oxygenation
    • J. B. Schenkman and H. Griem, eds., Springer-Verlag, Berlin
    • H. Rein and C. Jung, Metabolic reactions: Mechanisms of substrate oxygenation, in Cytochrome P-450 (J. B. Schenkman and H. Griem, eds.), Springer-Verlag, Berlin, 1993, pp. 105-122.
    • (1993) Cytochrome P-450 , pp. 105-122
    • Rein, H.1    Jung, C.2
  • 130
    • 0001500544 scopus 로고
    • The molecular basis of electron transfer in redox enzyme systems
    • K. Ruckpaul and H. Rein, eds., Taylor and Francis, London
    • N. C. Veitch and R. J. P. Williams, The molecular basis of electron transfer in redox enzyme systems, in Frontiers in Biotransformation, Volume 7 (K. Ruckpaul and H. Rein, eds.), Taylor and Francis, London, 1992, pp. 279-320.
    • (1992) Frontiers in Biotransformation , vol.7 , pp. 279-320
    • Veitch, N.C.1    Williams, R.J.P.2
  • 131
    • 0344813785 scopus 로고
    • EXAFS spectroscopy of heme-containing oxygenases and peroxidases
    • L. A. Andersson and J. H. Dawson, EXAFS spectroscopy of heme-containing oxygenases and peroxidases, Struct. Bond., 74, 1-40 (1990).
    • (1990) Struct. Bond. , vol.74 , pp. 1-40
    • Andersson, L.A.1    Dawson, J.H.2
  • 132
    • 0000350777 scopus 로고
    • cam research: Mechanistic insights into oxygenase catalysis
    • P. R. Ortiz de Montellano, ed., Plenum, New York
    • cam research: Mechanistic insights into oxygenase catalysis, in Cytochrome P450 (P. R. Ortiz de Montellano, ed.), Plenum, New York, 1995, pp. 83-124.
    • (1995) Cytochrome P450 , pp. 83-124
    • Mueller, E.J.1    Loida, P.J.2    Sligar, S.G.3
  • 133
    • 0003977039 scopus 로고
    • Modelling of the active site of cytochrome P-450 by means of synthetic analogues
    • K. Ruckpaul and H. Rein, eds., Taylor and Francis, London
    • W.-D. Woggon and S. Matile, Modelling of the active site of cytochrome P-450 by means of synthetic analogues, in Frontiers in Biotransformation, Volume 7 (K. Ruckpaul and H. Rein, eds.), Taylor and Francis, London, 1992, pp. 59-89.
    • (1992) Frontiers in Biotransformation , vol.7 , pp. 59-89
    • Woggon, W.-D.1    Matile, S.2
  • 134
    • 0002156744 scopus 로고
    • Models and mechanisms of cytochrome P450 action
    • P. R. Ortiz de Montellano, ed., Plenum, New York
    • J. T. Groves and Y.-Z. Han, Models and mechanisms of cytochrome P450 action, in Cytochrome P450, 2nd ed. (P. R. Ortiz de Montellano, ed.), Plenum, New York, 1995, pp. 3-48.
    • (1995) Cytochrome P450, 2nd Ed. , pp. 3-48
    • Groves, J.T.1    Han, Y.-Z.2
  • 135
    • 0007329937 scopus 로고
    • One-electron electrochemical reduction of a ferrous porphyrin dioxygen complex
    • C. H. Welborn, D. Dolphin, and B. R. James, One-electron electrochemical reduction of a ferrous porphyrin dioxygen complex, J. Am. Chem. Soc., 103, 2869-2871 (1981).
    • (1981) J. Am. Chem. Soc. , vol.103 , pp. 2869-2871
    • Welborn, C.H.1    Dolphin, D.2    James, B.R.3
  • 137
    • 0026646425 scopus 로고
    • Thianthrene 5-oxide as a probe of the electrophilicity of hemoprotein oxidizing species
    • J. C. Alvarez and P. R. Ortiz de Montellano, Thianthrene 5-oxide as a probe of the electrophilicity of hemoprotein oxidizing species, Biochemistry, 31, 8315-8322 (1992).
    • (1992) Biochemistry , vol.31 , pp. 8315-8322
    • Alvarez, J.C.1    De Ortiz Montellano, P.R.2
  • 139
    • 0026584588 scopus 로고
    • 2 and alkyl hydroperoxide supported N demethylation of N-methylaniline catalyzed by alkaline haematin and microsomal cytochrome P-450
    • 2 and alkyl hydroperoxide supported N demethylation of N-methylaniline catalyzed by alkaline haematin and microsomal cytochrome P-450, J. Inorgan. Biochem., 45, 47-52 (1992).
    • (1992) J. Inorgan. Biochem. , vol.45 , pp. 47-52
    • Adams, C.1    Adams, P.A.2
  • 142
    • 0000889090 scopus 로고
    • Mechanistic studies on a placental aromatase model reaction
    • P. A. Cole 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
  • 143
    • 0029140873 scopus 로고
    • An incredibly fast apparent oxygen rebound rate constant for hydrocarbon hydroxylation by cytochrome P-450 enzymes
    • M. Newcomb, M.-H. Le Tadic, D. A. Putt, and P. F. Hollenberg, An incredibly fast apparent oxygen rebound rate constant for hydrocarbon hydroxylation by cytochrome P-450 enzymes, J. Am. Chem. Soc., 117, 3312-3313 (1995).
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 3312-3313
    • Newcomb, M.1    Le Tadic, M.-H.2    Putt, D.A.3    Hollenberg, P.F.4
  • 144
    • 0018803839 scopus 로고
    • Proton coupling in the cytochrome P-450 spin and redox equilibria
    • S. G. Sligar and I. C. Gunsalus, Proton coupling in the cytochrome P-450 spin and redox equilibria, Biochemistry, 18, 2290-2295 (1979).
    • (1979) Biochemistry , vol.18 , pp. 2290-2295
    • Sligar, S.G.1    Gunsalus, I.C.2
  • 145
    • 0019441973 scopus 로고
    • pH-dependent interaction of microsomal cytochrome P-450 with substrates. I. Effect of pH upon the interaction of exogenous substrates with membrane-bound cytochrome P-450
    • Y. Hachino, T. Matsubara, and B. Hagihara, pH-dependent interaction of microsomal cytochrome P-450 with substrates. I. Effect of pH upon the interaction of exogenous substrates with membrane-bound cytochrome P-450, Chem.-Biol. Interact., 37, 181-190 (1981).
    • (1981) Chem.-Biol. Interact. , vol.37 , pp. 181-190
    • Hachino, Y.1    Matsubara, T.2    Hagihara, B.3
  • 146
    • 84987154511 scopus 로고
    • End-on versus side-on coordination of dioxygen: An ab initio calculation for peroxo-titaniumporphyrin
    • M.-M. Rohmer, M. Barry, A. Dedieu, and A. Veillard, End-on versus side-on coordination of dioxygen: An ab initio calculation for peroxo-titaniumporphyrin, Int. J. Quantum Chem., Quantum Biol. Symp., 4, 337-342 (1977).
    • (1977) Int. J. Quantum Chem., Quantum Biol. Symp. , vol.4 , pp. 337-342
    • Rohmer, M.-M.1    Barry, M.2    Dedieu, A.3    Veillard, A.4
  • 147
    • 0019741323 scopus 로고
    • Oxygen activation and tetrapyrroles
    • R. Bonnett, Oxygen activation and tetrapyrroles, Essays Biochem., 17, 1-51 (1981).
    • (1981) Essays Biochem. , vol.17 , pp. 1-51
    • Bonnett, R.1
  • 148
    • 0028979829 scopus 로고
    • Electrocatalytically driven ω-hydroxylation of fatty acids using cytochrome P450 4A1
    • K. M. Faulkner, M. S. Shet, C. W. Fisher, and R. W. Estabrook, Electrocatalytically driven ω-hydroxylation of fatty acids using cytochrome P450 4A1, Proc. Natl. Acad. Sci. USA, 92, 7705-7709 (1995).
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 7705-7709
    • Faulkner, K.M.1    Shet, M.S.2    Fisher, C.W.3    Estabrook, R.W.4
  • 150
    • 0000589432 scopus 로고
    • Catalytic mechanism of cytochrome P-450; Evidence for a distal charge relay
    • N. C. Gerber and S. G. Sligar, Catalytic mechanism of cytochrome P-450; Evidence for a distal charge relay, J. Am. Chem. Soc., 114, 8742-8743 (1992).
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 8742-8743
    • Gerber, N.C.1    Sligar, S.G.2
  • 151
    • 0028246557 scopus 로고
    • On the mechanism of action of cytochrome P450: Evaluation of hydrogen abstraction in oxygen-dependent alcohol oxidation
    • A. D. N. Vaz and M. J. Coon, On the mechanism of action of cytochrome P450: Evaluation of hydrogen abstraction in oxygen-dependent alcohol oxidation, Biochemistry, 33, 6442-6449 (1994).
    • (1994) Biochemistry , vol.33 , pp. 6442-6449
    • Vaz, A.D.N.1    Coon, M.J.2
  • 152
    • 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
    • A. D. N. Vaz, 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
  • 153
    • 33845282363 scopus 로고
    • cam: Deuterium isotope effects on regiospecificity and the monoxygenase/oxidase ratio
    • cam: Deuterium isotope effects on regiospecificity and the monoxygenase/oxidase ratio, J. Am. Chem. Soc., 109, 3654-3760 (1987).
    • (1987) J. Am. Chem. Soc. , vol.109 , pp. 3654-3760
    • Atkins, W.M.1    Sligar, S.G.2
  • 154
    • 0001312964 scopus 로고
    • Electrochemistry of aromatic hydrocarbons and related substances
    • M. E. Peover, Electrochemistry of aromatic hydrocarbons and related substances, Electroanal. Chem., 2, 1-51 (1967).
    • (1967) Electroanal. Chem. , vol.2 , pp. 1-51
    • Peover, M.E.1
  • 156
    • 0014227971 scopus 로고
    • The mixed function oxygenation of 4-halogenoacetanilides in rat liver microsomes and model systems
    • V. Ullrich, J. Wolf, E. Amadori, and H. Staudinger, The mixed function oxygenation of 4-halogenoacetanilides in rat liver microsomes and model systems, Hoppe-Seyler's Zeitschr. Physiol. Chem., 349, 85-94 (1968).
    • (1968) Hoppe-Seyler's Zeitschr. Physiol. Chem. , vol.349 , pp. 85-94
    • Ullrich, V.1    Wolf, J.2    Amadori, E.3    Staudinger, H.4
  • 157
    • 0344418475 scopus 로고
    • Mechanisms of metal-containing monooxygenases
    • M. A. J. Rodgers and E. L. Powers, eds., Academic Press, New York
    • V. Ullrich and H. Kulthan, Mechanisms of metal-containing monooxygenases, in Oxygen and Oxy-radicals in Chemistry and Biology (M. A. J. Rodgers and E. L. Powers, eds.), Academic Press, New York, 1981, pp. 497-505.
    • (1981) Oxygen and Oxy-radicals in Chemistry and Biology , pp. 497-505
    • Ullrich, V.1    Kulthan, H.2
  • 158
    • 0345712956 scopus 로고
    • Oxygen reactions in model systems
    • J. R. Gillette, A. H. Conney, G. J. Cosmides, R. W. Estabrook, J. R. Fouts, and G. J. Mannering, eds., Academic Press, New York
    • V. Ullrich and H. Staudinger, Oxygen reactions in model systems, in Microsomes and Drug Oxidations (J. R. Gillette, A. H. Conney, G. J. Cosmides, R. W. Estabrook, J. R. Fouts, and G. J. Mannering, eds.), Academic Press, New York, 1969, pp. 199-217.
    • (1969) Microsomes and Drug Oxidations , pp. 199-217
    • Ullrich, V.1    Staudinger, H.2
  • 159
    • 0001093289 scopus 로고
    • The mechanism of the ene reaction of singlet oxygen with olefins
    • L. B. Harding and W. A. Goddard, The mechanism of the ene reaction of singlet oxygen with olefins, J. Am. Chem. Soc., 102, 439-449 (1980).
    • (1980) J. Am. Chem. Soc. , vol.102 , pp. 439-449
    • Harding, L.B.1    Goddard, W.A.2
  • 160
    • 0020479617 scopus 로고
    • The catalytic mechanism of cytochrome P450: Spin-trapping evidence for one electron substrate oxidation
    • O. Augusto, H. S. Beilan, and P. R. Ortiz de Montellano, The catalytic mechanism of cytochrome P450: Spin-trapping evidence for one electron substrate oxidation, J. Biol. Chem., 257, 11288-11295 (1982).
    • (1982) J. Biol. Chem. , vol.257 , pp. 11288-11295
    • Augusto, O.1    Beilan, H.S.2    De Ortiz Montellano, P.R.3
  • 161
    • 0027315887 scopus 로고
    • Mechanistic studies on aromatase and related C-C bond cleaving P-450 enzymes
    • M. Akhtar, V. C. O. Njar, and J. N. Wright, Mechanistic studies on aromatase and related C-C bond cleaving P-450 enzymes, J. Steroid Biochem. Molec. Biol., 44, 375-387 (1993).
    • (1993) J. Steroid Biochem. Molec. Biol. , vol.44 , pp. 375-387
    • Akhtar, M.1    Njar, V.C.O.2    Wright, J.N.3
  • 162
    • 0028794689 scopus 로고
    • Cytochrome P450: Structure, function and generation of reactive oxygen species
    • R. Bernhardt, Cytochrome P450: Structure, function and generation of reactive oxygen species, Rev. Physiol. Biochem. Pharmacol., 127, 137-221 (1995).
    • (1995) Rev. Physiol. Biochem. Pharmacol. , vol.127 , pp. 137-221
    • Bernhardt, R.1
  • 165
    • 0023023246 scopus 로고
    • Physical methods in the study of the active site geometry of cytochromes P-450
    • D. F. V. Lewis, Physical methods in the study of the active site geometry of cytochromes P-450, Drug Metab. Rev., 17, 1-66 (1986).
    • (1986) Drug Metab. Rev. , vol.17 , pp. 1-66
    • Lewis, D.F.V.1
  • 168
    • 0029120886 scopus 로고
    • A quantitative structure-activity relationship study on a series of para-substituted toulenes binding to cytochrome P450 2B4 (CYP284) and also their hydroxylation rates
    • D. F. V. Lewis, C. Ioannides, and D. V. Parke, A quantitative structure-activity relationship study on a series of para-substituted toulenes binding to cytochrome P450 2B4 (CYP284) and also their hydroxylation rates, Biochem. Pharmacol., 50, 619-625 (1995).
    • (1995) Biochem. Pharmacol. , vol.50 , pp. 619-625
    • Lewis, D.F.V.1    Ioannides, C.2    Parke, D.V.3
  • 169
    • 0022518374 scopus 로고
    • Active site mechanics of liver microsomal cytochrome P-450
    • R. E. White and M. B. McCarthy, Active site mechanics of liver microsomal cytochrome P-450, Arch. Biochem. Biophys., 246, 19-32 (1986).
    • (1986) Arch. Biochem. Biophys. , vol.246 , pp. 19-32
    • White, R.E.1    McCarthy, M.B.2
  • 171
    • 33845280446 scopus 로고
    • Comparing the polarities of the amino acids: Side-chain distribution coefficients between the vapor phase, cyclohexane, 1-octanol, and neutral aqueous solution
    • A. Radzicka and R. Wolfenden, Comparing the polarities of the amino acids: Side-chain distribution coefficients between the vapor phase, cyclohexane, 1-octanol, and neutral aqueous solution, Biochemistry, 27, 1664-1670 (1988).
    • (1988) Biochemistry , vol.27 , pp. 1664-1670
    • Radzicka, A.1    Wolfenden, R.2
  • 172
    • 0003063079 scopus 로고
    • A. J. Bard, R. Parsons, and J. Jordan, eds., Marcel Dekker, Inc., New York
    • J. P. Hoare, Oxygen, in Standard Potentials in Aqueous Solution (A. J. Bard, R. Parsons, and J. Jordan, eds.), Marcel Dekker, Inc., New York, 1985, pp. 49-66.
    • (1985) Standard Potentials in Aqueous Solution , pp. 49-66
    • Hoare Oxygen, J.P.1
  • 173
    • 84945310635 scopus 로고
    • Standard electrode potentials and temperature coefficients in water at 298.15 K
    • S. G. Bratsch, Standard electrode potentials and temperature coefficients in water at 298.15 K, J. Phys. Chem. Ref. Data, 18, 1-21 (1989).
    • (1989) J. Phys. Chem. Ref. Data , vol.18 , pp. 1-21
    • Bratsch, S.G.1
  • 174
    • 0343653949 scopus 로고
    • Superoxide, superoxide dismutases and oxygen toxicity
    • T. G. Spiro, ed., Wiley, New York
    • J. A. Fee, Superoxide, superoxide dismutases and oxygen toxicity, in Metal Ion Activation of Dioxygen (T. G. Spiro, ed.), Wiley, New York, 1980, pp. 209-237.
    • (1980) Metal Ion Activation of Dioxygen , pp. 209-237
    • Fee, J.A.1


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