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Volumn 46, Issue 26, 2007, Pages 7852-7864

Allosteric mechanisms in cytochrome P450 3A4 studied by high-pressure spectroscopy: Pivotal role of substrate-induced changes in the accessibility and degree of hydration of the heme pocket

Author keywords

[No Author keywords available]

Indexed keywords

BROMOCRIPTINE (BCT); CYTOCHROME P450 3A4; HIGH-PRESSURE SPECTROSCOPY; NANODISCS;

EID: 34347326224     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi602400y     Document Type: Article
Times cited : (38)

References (43)
  • 1
    • 27144459868 scopus 로고    scopus 로고
    • Kinetics of dithionite-dependent reduction of cytochrome P450 3A4: Heterogeneity of the enzyme caused by its oligomerization
    • Davydov, D. R., Fernando, H., Baas, B. J., Sligar, S. G., and Halpert, J. R. (2005) Kinetics of dithionite-dependent reduction of cytochrome P450 3A4: Heterogeneity of the enzyme caused by its oligomerization, Biochemistry 44, 13902-13913.
    • (2005) Biochemistry , vol.44 , pp. 13902-13913
    • Davydov, D.R.1    Fernando, H.2    Baas, B.J.3    Sligar, S.G.4    Halpert, J.R.5
  • 2
    • 33846135094 scopus 로고    scopus 로고
    • Mechanism of interactions of α-naphthoflavone with cytochrome P450 3A4 explored with an engineered enzyme bearing a fluorescent probe
    • Tsalkova, T. N., Davydova, N. E., Halpert, J. R., and Davydov, D. R. (2007) Mechanism of interactions of α-naphthoflavone with cytochrome P450 3A4 explored with an engineered enzyme bearing a fluorescent probe, Biochemistry 46, 106-119.
    • (2007) Biochemistry , vol.46 , pp. 106-119
    • Tsalkova, T.N.1    Davydova, N.E.2    Halpert, J.R.3    Davydov, D.R.4
  • 3
    • 33749521872 scopus 로고    scopus 로고
    • Time-resolved fluorescence studies of heterotropic ligand binding to cytochrome P450 3A4
    • Lampe, J. N., and Atkins, W. M. (2006) Time-resolved fluorescence studies of heterotropic ligand binding to cytochrome P450 3A4, Biochemistry 45, 12204-12215.
    • (2006) Biochemistry , vol.45 , pp. 12204-12215
    • Lampe, J.N.1    Atkins, W.M.2
  • 4
    • 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
  • 5
    • 33646854265 scopus 로고    scopus 로고
    • Structure of microsomal cytochrome P450 2B4 complexed with the antifungal drug bifonazole: Insight into P450 conformational plasticity and membrane interaction
    • Zhao, Y., White, M. A., Muralidhara, B. K., Sun, L., Halpert, J. R., and Stout, C. D. (2006) Structure of microsomal cytochrome P450 2B4 complexed with the antifungal drug bifonazole: Insight into P450 conformational plasticity and membrane interaction, J. Biol. Chem. 281, 5973-5981.
    • (2006) J. Biol. Chem , vol.281 , pp. 5973-5981
    • Zhao, Y.1    White, M.A.2    Muralidhara, B.K.3    Sun, L.4    Halpert, J.R.5    Stout, C.D.6
  • 6
    • 33748802003 scopus 로고    scopus 로고
    • Structural basis for ligand promiscuity in cytochrome P450 3A4
    • Ekroos, M., and Sjögren, T. (2006) Structural basis for ligand promiscuity in cytochrome P450 3A4, Proc. Natl. Acad. Sci. U.S.A. 103, 13684-13687.
    • (2006) Proc. Natl. Acad. Sci. U.S.A , vol.103 , pp. 13684-13687
    • Ekroos, M.1    Sjögren, T.2
  • 8
    • 0000574406 scopus 로고    scopus 로고
    • Evaluation of atypical cytochrome P450 kinetics with two-substrate models: Evidence that multiple substrates can simultaneously bind to cytochrome P450 active sites
    • Korzekwa, K. R., Krishnamachary, N., Shou, M., Ogai, A., Parise, R. A., Rettie, A. E., Gonzalez, F. J., and Tracy, T. S. (1998) Evaluation of atypical cytochrome P450 kinetics with two-substrate models: Evidence that multiple substrates can simultaneously bind to cytochrome P450 active sites, Biochemistry 37, 4137-4147.
    • (1998) Biochemistry , vol.37 , pp. 4137-4147
    • Korzekwa, K.R.1    Krishnamachary, N.2    Shou, M.3    Ogai, A.4    Parise, R.A.5    Rettie, A.E.6    Gonzalez, F.J.7    Tracy, T.S.8
  • 9
    • 0031028518 scopus 로고    scopus 로고
    • Cooperativity in oxidations catalyzed by cytochrome P450 3A4
    • Ueng, Y. F., Kuwabara, T., Chun, Y. J., and Guengerich, F. P. (1997) Cooperativity in oxidations catalyzed by cytochrome P450 3A4, Biochemistry 36, 370-381.
    • (1997) Biochemistry , vol.36 , pp. 370-381
    • Ueng, Y.F.1    Kuwabara, T.2    Chun, Y.J.3    Guengerich, F.P.4
  • 10
    • 0035059352 scopus 로고    scopus 로고
    • Allosteric behavior in cytochrome P450-dependent in vitro drug-drug interactions: A prospective based on conformational dynamics
    • Atkins, W. M., Wang, R. W., and Lu, A. Y. H. (2001) Allosteric behavior in cytochrome P450-dependent in vitro drug-drug interactions: A prospective based on conformational dynamics, Chem. Res. Toxicol. 14, 338-347.
    • (2001) Chem. Res. Toxicol , vol.14 , pp. 338-347
    • Atkins, W.M.1    Wang, R.W.2    Lu, A.Y.H.3
  • 11
    • 0345689555 scopus 로고    scopus 로고
    • Conformational heterogeneity of cytochrome P450 3A4 revealed by high pressure spectroscopy
    • Davydov, D. R., Halpert, J. R., Renaud, J. P., and Hui Bon Hoa, G. (2003) Conformational heterogeneity of cytochrome P450 3A4 revealed by high pressure spectroscopy, Biochem. Biophys. Res. Commun. 312, 121-130.
    • (2003) Biochem. Biophys. Res. Commun , vol.312 , pp. 121-130
    • Davydov, D.R.1    Halpert, J.R.2    Renaud, J.P.3    Hui Bon Hoa, G.4
  • 12
    • 2542623028 scopus 로고    scopus 로고
    • An electrostatically driven conformational transition is involved in the mechanisms of substrate binding and cooperativity in cytochrome P450eryF
    • Davydov, D. R., Botchkareva, A. E., Kumar, S., He, Y. Q., and Halpert, J. R. (2004) An electrostatically driven conformational transition is involved in the mechanisms of substrate binding and cooperativity in cytochrome P450eryF, Biochemistry 43, 6475-6485.
    • (2004) Biochemistry , vol.43 , pp. 6475-6485
    • Davydov, D.R.1    Botchkareva, A.E.2    Kumar, S.3    He, Y.Q.4    Halpert, J.R.5
  • 13
    • 33645981275 scopus 로고    scopus 로고
    • Conformational fluctuations of proteins revealed by variable pressure NMR
    • Li, H., and Akasaka, K. (2006) Conformational fluctuations of proteins revealed by variable pressure NMR, Biochim. Biophys. Acta 1764, 331-345.
    • (2006) Biochim. Biophys. Acta , vol.1764 , pp. 331-345
    • Li, H.1    Akasaka, K.2
  • 14
    • 33646010631 scopus 로고    scopus 로고
    • Pressure and temperature as tools for investigating the role of individual non-covalent interactions in enzymatic reactions: Sulfolobus solfataricus carboxypeptidase as a model enzyme
    • Occhipinti, E., Bec, N., Gambirasio, B., Baietta, G., Martelli, P. L., Casadio, R., Balny, C., Lange, R., and Tortora, P. (2006) Pressure and temperature as tools for investigating the role of individual non-covalent interactions in enzymatic reactions: Sulfolobus solfataricus carboxypeptidase as a model enzyme, Biochim. Biophys. Acta 1764, 563-572.
    • (2006) Biochim. Biophys. Acta , vol.1764 , pp. 563-572
    • Occhipinti, E.1    Bec, N.2    Gambirasio, B.3    Baietta, G.4    Martelli, P.L.5    Casadio, R.6    Balny, C.7    Lange, R.8    Tortora, P.9
  • 15
    • 0037171146 scopus 로고    scopus 로고
    • The effects of osmotic and hydrostatic pressures on macromolecular systems
    • Kornblatt, J. A., and Kornblatt, M. J. (2002) The effects of osmotic and hydrostatic pressures on macromolecular systems, Biochim. Biophys. Acta 1595, 30-47.
    • (2002) Biochim. Biophys. Acta , vol.1595 , pp. 30-47
    • Kornblatt, J.A.1    Kornblatt, M.J.2
  • 16
    • 0037171133 scopus 로고    scopus 로고
    • The interactions of nucleic acids at elevated hydrostatic pressure
    • Macgregor, R. B. (2002) The interactions of nucleic acids at elevated hydrostatic pressure, Biochim. Biophys. Acta 1595, 266-276.
    • (2002) Biochim. Biophys. Acta , vol.1595 , pp. 266-276
    • Macgregor, R.B.1
  • 17
    • 0031714901 scopus 로고    scopus 로고
    • Protein structure and dynamics at high pressure
    • Heremans, K., and Smeller, L. (1998) Protein structure and dynamics at high pressure, Biochim. Biophys. Acta 1386, 353-370.
    • (1998) Biochim. Biophys. Acta , vol.1386 , pp. 353-370
    • Heremans, K.1    Smeller, L.2
  • 18
    • 0028210538 scopus 로고
    • Hydrostatic pressure reverses osmotic pressure effects on the specificity of EcoRI-DNA interactions
    • Robinson, C. R., and Sligar, S. G. (1994) Hydrostatic pressure reverses osmotic pressure effects on the specificity of EcoRI-DNA interactions, Biochemistry 33, 3787-3792.
    • (1994) Biochemistry , vol.33 , pp. 3787-3792
    • Robinson, C.R.1    Sligar, S.G.2
  • 19
    • 0021832318 scopus 로고
    • High-pressure investigations of cytochrome P-450 spin and substrate binding equilibria
    • Fisher, M. T., Scarlata, S. F., and Sligar, S. G. (1985) High-pressure investigations of cytochrome P-450 spin and substrate binding equilibria, Arch. Biochem. Biophys. 1, 456-463.
    • (1985) Arch. Biochem. Biophys , vol.1 , pp. 456-463
    • Fisher, M.T.1    Scarlata, S.F.2    Sligar, S.G.3
  • 20
    • 0020485740 scopus 로고
    • The pressure dependence of the spin equilibrium in camphor-bound ferric cytochrome P-450
    • Hui Bon Hoa, G., and Marden, M. C. (1982) The pressure dependence of the spin equilibrium in camphor-bound ferric cytochrome P-450, Eur. J. Biochem. 124, 311-315.
    • (1982) Eur. J. Biochem , vol.124 , pp. 311-315
    • Hui Bon Hoa, G.1    Marden, M.C.2
  • 21
    • 0023654056 scopus 로고
    • P-450 binding to substrates camphor and linalool versus pressure
    • Marden, M. C., and Hoa, G. H. (1987) P-450 binding to substrates camphor and linalool versus pressure, Arch. Biochem. Biophys. 253, 100-107.
    • (1987) Arch. Biochem. Biophys , vol.253 , pp. 100-107
    • Marden, M.C.1    Hoa, G.H.2
  • 22
    • 0026686888 scopus 로고
    • Heme-pocket-hydration change during the inactivation of cytochrome P-450camphor by hydrostatic pressure
    • Di Primo, C., Hui Bon Hoa, G., Douzou, P., and Sligar, S. G. (1992) Heme-pocket-hydration change during the inactivation of cytochrome P-450camphor by hydrostatic pressure, Eur. J. Biochem. 2, 583-508.
    • (1992) Eur. J. Biochem , vol.2 , pp. 583-508
    • Di Primo, C.1    Hui Bon Hoa, G.2    Douzou, P.3    Sligar, S.G.4
  • 25
    • 0026492443 scopus 로고
    • High pressure induced inactivation of ferrous cytochrome P-450 LM2 (2B4) CO complex: Evidence for the presence of two conformers in the oligomer
    • Davydov, D. R., Knyushko, T. V., and Hui Bon Hoa, G. (1992) High pressure induced inactivation of ferrous cytochrome P-450 LM2 (2B4) CO complex: Evidence for the presence of two conformers in the oligomer, Biochem. Biophys. Res. Commun. 188, 216-221.
    • (1992) Biochem. Biophys. Res. Commun , vol.188 , pp. 216-221
    • Davydov, D.R.1    Knyushko, T.V.2    Hui Bon Hoa, G.3
  • 26
    • 0029077745 scopus 로고
    • High-pressure induced transitions in microsomal cytochrome P450 2B4 in solution: Evidence for conformational inhomogeneity in the oligomers
    • Davydov, D. R., Deprez, E., Hui Bon Hoa, G., Knyushko, T. V., Kuznetsova, G. P., Koen, Y. M., and Archakov, A. I. (1995) High-pressure induced transitions in microsomal cytochrome P450 2B4 in solution: Evidence for conformational inhomogeneity in the oligomers, Arch. Biochem. Biophys. 320, 330-344.
    • (1995) Arch. Biochem. Biophys , vol.320 , pp. 330-344
    • Davydov, D.R.1    Deprez, E.2    Hui Bon Hoa, G.3    Knyushko, T.V.4    Kuznetsova, G.P.5    Koen, Y.M.6    Archakov, A.I.7
  • 27
    • 0034610011 scopus 로고    scopus 로고
    • Stabilization of P450 2B4 by its association with P450 1A2 revealed by high-pressure spectroscopy
    • Davydov, D. R., Petushkova, N. A., Archakov, A. I., and Hui Bon Hoa, G. (2000) Stabilization of P450 2B4 by its association with P450 1A2 revealed by high-pressure spectroscopy, Biochem. Biophys. Res. Commun. 276, 1005-1012.
    • (2000) Biochem. Biophys. Res. Commun , vol.276 , pp. 1005-1012
    • Davydov, D.R.1    Petushkova, N.A.2    Archakov, A.I.3    Hui Bon Hoa, G.4
  • 28
  • 29
    • 0031438615 scopus 로고    scopus 로고
    • A central role for water in the control of the spin state of cytochrome P-450-(scc)
    • Bancel, F., Bec, N., Ebel, C., and Lange, R. (1997) A central role for water in the control of the spin state of cytochrome P-450-(scc), Eur. J. Biochem. 250, 276-285.
    • (1997) Eur. J. Biochem , vol.250 , pp. 276-285
    • Bancel, F.1    Bec, N.2    Ebel, C.3    Lange, R.4
  • 31
    • 0033547829 scopus 로고    scopus 로고
    • Dynamics of protein-bound water in the heme domain of P450BM3 studied by high-pressure spectroscopy: Comparison with P450cam and P450 2B4
    • Davydov, D. R., Hui Bon Hoa, G., and Peterson, J. A. (1999) Dynamics of protein-bound water in the heme domain of P450BM3 studied by high-pressure spectroscopy: Comparison with P450cam and P450 2B4, Biochemistry 38, 751-761.
    • (1999) Biochemistry , vol.38 , pp. 751-761
    • Davydov, D.R.1    Hui Bon Hoa, G.2    Peterson, J.A.3
  • 32
    • 0032501058 scopus 로고    scopus 로고
    • Characterization of a cytochrome P450 from the acidothermophilic archaea Sulfolobus solfataricus
    • Mclean, M. A., Maves, S. A., Weiss, K. E., Krepich, S., and Sligar, S. G. (1998) Characterization of a cytochrome P450 from the acidothermophilic archaea Sulfolobus solfataricus, Biochem. Biophys. Res. Commun. 252, 166-172.
    • (1998) Biochem. Biophys. Res. Commun , vol.252 , pp. 166-172
    • Mclean, M.A.1    Maves, S.A.2    Weiss, K.E.3    Krepich, S.4    Sligar, S.G.5
  • 33
    • 0034823445 scopus 로고    scopus 로고
    • Reversible pressure deformation of a thermophilic cytochrome P450 enzyme (CYP119) and its active-site mutants
    • Tschirret-Guth, R. A., Koo, L. S., Hoa, G. H. B., and de Montellano, P. R. O. (2001) Reversible pressure deformation of a thermophilic cytochrome P450 enzyme (CYP119) and its active-site mutants, J. Am. Chem. Soc. 123, 3412-3417.
    • (2001) J. Am. Chem. Soc , vol.123 , pp. 3412-3417
    • Tschirret-Guth, R.A.1    Koo, L.S.2    Hoa, G.H.B.3    de Montellano, P.R.O.4
  • 34
    • 0028950935 scopus 로고
    • Antagonistic effects of hydrostatic pressure and osmotic pressure on cytochrome P-450(cam) spin transition
    • Di Primo, C., Deprez, E., Hui Bon Hoa, G., and Douzou, P. (1995) Antagonistic effects of hydrostatic pressure and osmotic pressure on cytochrome P-450(cam) spin transition, Biophys. J. 68, 2056-2061.
    • (1995) Biophys. J , vol.68 , pp. 2056-2061
    • Di Primo, C.1    Deprez, E.2    Hui Bon Hoa, G.3    Douzou, P.4
  • 35
    • 0025092326 scopus 로고
    • Effect of the tyrosine 96 hydrogen bond on the inactivation of cytochrome P-450cam induced by hydrostatic pressure
    • Di Primo, C., Hui Bon Hoa, G., Douzou, P., and Sligar, S. (1990) Effect of the tyrosine 96 hydrogen bond on the inactivation of cytochrome P-450cam induced by hydrostatic pressure, Eur. J. Biochem. 193, 383-386.
    • (1990) Eur. J. Biochem , vol.193 , pp. 383-386
    • Di Primo, C.1    Hui Bon Hoa, G.2    Douzou, P.3    Sligar, S.4
  • 36
    • 4444297536 scopus 로고    scopus 로고
    • Homotropic cooperativity of monomeric cytochrome P450 3A4 in a nanoscale native bilayer environment
    • Baas, B. J., Denisov, I. G., and Sligar, S. G. (2004) Homotropic cooperativity of monomeric cytochrome P450 3A4 in a nanoscale native bilayer environment, Arch. Biochem. Biophys. 430, 218-228.
    • (2004) Arch. Biochem. Biophys , vol.430 , pp. 218-228
    • Baas, B.J.1    Denisov, I.G.2    Sligar, S.G.3
  • 37
    • 0029982945 scopus 로고    scopus 로고
    • Thermodynamic studies of substrate binding and spin transitions in human cytochrome P450 3A4 expressed in yeast microsomes
    • Renaud, J. P., Davydov, D. R., Heirwegh, K. P. M., Mansuy, D., and Hui Bon Hoa, G. (1996) Thermodynamic studies of substrate binding and spin transitions in human cytochrome P450 3A4 expressed in yeast microsomes, Biochem. J. 319, 675-681.
    • (1996) Biochem. J , vol.319 , pp. 675-681
    • Renaud, J.P.1    Davydov, D.R.2    Heirwegh, K.P.M.3    Mansuy, D.4    Hui Bon Hoa, G.5
  • 38
    • 33645536654 scopus 로고    scopus 로고
    • Resolution of multiple substrate binding sites in cytochrome P450 3A4: The stoichiometry of the enzyme-substrate complexes probed by FRET and Job's titration
    • Fernando, H., Halpert, J. R., and Davydov, D. R. (2006) Resolution of multiple substrate binding sites in cytochrome P450 3A4: The stoichiometry of the enzyme-substrate complexes probed by FRET and Job's titration, Biochemistry 45, 4199-4209.
    • (2006) Biochemistry , vol.45 , pp. 4199-4209
    • Fernando, H.1    Halpert, J.R.2    Davydov, D.R.3
  • 39
    • 0037171147 scopus 로고    scopus 로고
    • High pressure, a tool for exploring heme protein active sites
    • Hui Bon Hoa, G., McLean, M. A., and Sligar, S. G. (2002) High pressure, a tool for exploring heme protein active sites, Biochim. Biophys. Acta 1595, 297-308.
    • (2002) Biochim. Biophys. Acta , vol.1595 , pp. 297-308
    • Hui Bon Hoa, G.1    McLean, M.A.2    Sligar, S.G.3
  • 41
    • 33845374715 scopus 로고
    • Microviscosity measurements of phospholipid bilayers using fluorescent dyes that undergo torsional relaxation
    • Kung, C. E., and Reed, J. K. (1986) Microviscosity measurements of phospholipid bilayers using fluorescent dyes that undergo torsional relaxation, Biochemistry 25, 6114-6121.
    • (1986) Biochemistry , vol.25 , pp. 6114-6121
    • Kung, C.E.1    Reed, J.K.2
  • 42
    • 34147112191 scopus 로고    scopus 로고
    • Cooperativity in P450 CYP3A4: Linkages in substrate binding, spin state, uncoupling and product formation
    • Denisov, I. G., Baas, B. J., Grinkova, Y. V., and Sligar, S. G. (2007) Cooperativity in P450 CYP3A4: Linkages in substrate binding, spin state, uncoupling and product formation, J. Biol. Chem. 282, 7066-7076.
    • (2007) J. Biol. Chem , vol.282 , pp. 7066-7076
    • Denisov, I.G.1    Baas, B.J.2    Grinkova, Y.V.3    Sligar, S.G.4


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