메뉴 건너뛰기




Volumn 6, Issue 1, 2010, Pages 1-15

New cytochrome P450 mechanisms: Implications for understanding molecular basis for drug toxicity at the level of the cytochrome

Author keywords

Coupling uncoupling; CYP; Drug toxicity; Product; Substrate

Indexed keywords

CAMPHOR; CYTOCHROME P450; FERRIC ION;

EID: 72949090555     PISSN: 17425255     EISSN: None     Source Type: Journal    
DOI: 10.1517/17425250903329095     Document Type: Review
Times cited : (26)

References (55)
  • 1
    • 0025761693 scopus 로고
    • Crystal structure of P450cam complexed with camphane, thiocamphor & admantane: Factors controlling P450 substrate hydroxylation
    • Raag R, Poulos TL. Crystal structure of P450cam complexed with camphane, thiocamphor & admantane: Factors controlling P450 substrate hydroxylation. Biochemistry 1991;30:2674-2684
    • (1991) Biochemistry , vol.30 , pp. 2674-2684
    • Raag, R.1    Poulos, T.L.2
  • 2
    • 0027113109 scopus 로고
    • Cytochrome P450cam: Crystallography, oxygen activation and electron transfer
    • Poulos TL, Raag R. Cytochrome P450cam: Crystallography, oxygen activation and electron transfer. FASEB J 1992;6:674-679
    • (1992) FASEB J , vol.6 , pp. 674-679
    • Poulos, T.L.1    Raag, R.2
  • 3
    • 0010528530 scopus 로고
    • Uncoupling of oxygen transfer and electron transfer in the oxygenation of camphor analogues by cytochrome P450cam
    • Kadkhodayan S, Coulter ED, Maryniak DM, et al. Uncoupling of oxygen transfer and electron transfer in the oxygenation of camphor analogues by cytochrome P450cam. J Biol Chem 1995;270:1-7
    • (1995) J Biol Chem , vol.270 , pp. 1-7
    • Kadkhodayan, S.1    Coulter, E.D.2    Maryniak, D.M.3
  • 4
    • 0028813639 scopus 로고
    • Crystal structure of cytochrome P450cam complexed with its catalytic product, 5-exo-hydroxycamphor
    • Li H, Narasimhulu S, Havran L, et al. Crystal structure of cytochrome P450cam complexed with its catalytic product, 5-exo-hydroxycamphor. J Am Chem Soc 1995;117:6297-6299
    • (1995) J Am Chem Soc , vol.117 , pp. 6297-6299
    • Li, H.1    Narasimhulu, S.2    Havran, L.3
  • 5
    • 0020478791 scopus 로고    scopus 로고
    • Spectroscopic investigations of ferric cytochrome P-450-CAM ligand complexes
    • Dawson H, Anderson LA, Sono M. Spectroscopic investigations of ferric cytochrome P-450-CAM ligand complexes. J Biol Chem 982;257:3606-3617
    • J Biol Chem , vol.982 , Issue.257 , pp. 3606-3617
    • Dawson, H.1    Anderson, L.A.2    Sono, M.3
  • 6
    • 0020490511 scopus 로고
    • Heme ligand replacement reactions of cytochrome P-450. Characterization of the bonding atom of the axial ligand trans to thiolate as oxygen
    • White RE, Coon MJ. Heme ligand replacement reactions of cytochrome P-450. Characterization of the bonding atom of the axial ligand trans to thiolate as oxygen. J Biol Chem 1982;257:3073-3083
    • (1982) J Biol Chem , vol.257 , pp. 3073-3083
    • White, R.E.1    Coon, M.J.2
  • 7
    • 0015184460 scopus 로고
    • Uncoupling of O2 activation from hydroxylation in the steroid C-21 hydroxylase of bovine adrenocortical microsomes
    • Narasimhulu S, Uncoupling of O2 activation from hydroxylation in the steroid C-21 hydroxylase of bovine adrenocortical microsomes. Arch Biochem Biophys 1971;147:384-390
    • (1971) Arch Biochem Biophys , vol.147 , pp. 384-390
    • Narasimhulu, S.1
  • 8
    • 0017409578 scopus 로고
    • Hydrogen peoxide formation and stoichiometry of hydroxylation reactions catalyzed by highly purified liver microsomal cytochrome p450
    • Nordbloom GD, Coon MJ. Hydrogen peoxide formation and stoichiometry of hydroxylation reactions catalyzed by highly purified liver microsomal cytochrome p450. Arch Biochem Biophys 1977;180:343-347
    • (1977) Arch Biochem Biophys , vol.180 , pp. 343-347
    • Nordbloom, G.D.1    Coon, M.J.2
  • 9
    • 0001541099 scopus 로고
    • Uncoupling of the cytochrome P450cam monooxygenase reaction by a single mutation, threonine 252 to alanine or valine: Possible role of the hydroxyl amino acid in oxygen activation
    • Imai M, Shimada H, Watanabe Y, et al. Uncoupling of the cytochrome P450cam monooxygenase reaction by a single mutation, threonine 252 to alanine or valine: Possible role of the hydroxyl amino acid in oxygen activation. Proc Natl Acad Sci USA 1989;86:7823-7827
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 7823-7827
    • Imai, M.1    Shimada, H.2    Watanabe, Y.3
  • 10
    • 0024832753 scopus 로고
    • A conserved residue of cytochrome P450cam is involved in heme-oxygen stability and activation
    • Martinis SA, Atkins WM, Stayton PS, et al. A conserved residue of cytochrome P450cam is involved in heme-oxygen stability and activation. J Am Chem Soc 1989;20:9252-9253
    • (1989) J Am Chem Soc , vol.20 , pp. 9252-9253
    • Martinis, S.A.1    Atkins, W.M.2    Stayton, P.S.3
  • 11
    • 0001425858 scopus 로고
    • Mechanism of oxygen activation by cytochrome P450cam
    • (Yamamoto SNM and Ishimura Y Eds.), Yamada Sci. Foundation
    • Shimada H, Imai M, Horishi T, et al. Mechanism of oxygen activation by cytochrome P450cam. (1990) in international symposiium on oxygenases and oxygen activation (Yamamoto SNM and Ishimura Y Eds.) pp 135, Yamada Sci. Foundation
    • (1990) International Symposiium on Oxygenases and Oxygen Activation , pp. 135
    • Shimada, H.1    Imai, M.2    Horishi, T.3
  • 12
    • 0027994378 scopus 로고
    • A role for asp-251 in cytochrome P450cam oxygen activation
    • Gerber NC, Sligar SG. A role for asp-251 in cytochrome P450cam oxygen activation. J Biol Chem 1994;269:4260-4266
    • (1994) J Biol Chem , vol.269 , pp. 4260-4266
    • Gerber, N.C.1    Sligar, S.G.2
  • 13
    • 0028986232 scopus 로고
    • Role of the Thr252 in cytochrome P450cam: A study with unnatural amino acid mutagenesis
    • Kimata Y, Shimada H, Hirose T, et al. Role of the Thr252 in cytochrome P450cam: A study with unnatural amino acid mutagenesis. Biochem Biophys Res Comm 1995;208:96-102
    • (1995) Biochem Biophys Res Comm , vol.208 , pp. 96-102
    • Kimata, Y.1    Shimada, H.2    Hirose, T.3
  • 14
    • 0034088779 scopus 로고    scopus 로고
    • The catalytic pathway of cytochrome P450cam at atomic resolution
    • Schlichting I, Berendzen J, Chu K, et al. The catalytic pathway of cytochrome P450cam at atomic resolution. Science 2000;287:1615-1622
    • (2000) Science , vol.287 , pp. 1615-1622
    • Schlichting, I.1    Berendzen, J.2    Chu, K.3
  • 15
    • 24744459452 scopus 로고    scopus 로고
    • Crystallographic study on the dioxygen complex of the wild type and mutant cytochrome P450cam: Implications for the dioxygen activation mechanism
    • Nagano S, Poulos TL. Crystallographic study on the dioxygen complex of the wild type and mutant cytochrome P450cam: Implications for the dioxygen activation mechanism. J Biol Chem 2005;280:31659-31663
    • (2005) J Biol Chem , vol.280 , pp. 31659-31663
    • Nagano, S.1    Poulos, T.L.2
  • 16
    • 34548463769 scopus 로고    scopus 로고
    • Structural biology of P450-oxy complexes
    • Poulos TL. Structural biology of P450-oxy complexes. Drug Metab Rev 2007;39:557-566
    • (2007) Drug Metab Rev , vol.39 , pp. 557-566
    • Poulos, T.L.1
  • 17
    • 37049036930 scopus 로고    scopus 로고
    • Alteration of P450 distal pocket solvent leads to impaired proton delivery and changes in heme geometry
    • Makris TM, Koenig K, Schlicting I, et al. Alteration of P450 distal pocket solvent leads to impaired proton delivery and changes in heme geometry. Biochemistry 2007;46:14129-14140
    • (2007) Biochemistry , vol.46 , pp. 14129-14140
    • Makris, T.M.1    Koenig, K.2    Schlicting, I.3
  • 18
    • 0023583624 scopus 로고
    • Crystal structures of metyrapone- and phenyimidazole-inhibited complexes of cytochrome P450cam
    • Poulos TL, Howard AJ. Crystal structures of metyrapone- and phenyimidazole-inhibited complexes of cytochrome P450cam. Biochemistry 1987;26:8165-8174
    • (1987) Biochemistry , vol.26 , pp. 8165-8174
    • Poulos, T.L.1    Howard, A.J.2
  • 19
    • 0023645035 scopus 로고
    • High resolution crystal structure of cytochrome P450cam
    • Poulos TL, Finzel BC, Howard AJ. High resolution crystal structure of cytochrome P450cam. J Mol Biol 1987;195:687-700
    • (1987) J Mol Biol , vol.195 , pp. 687-700
    • Poulos, T.L.1    Finzel, B.C.2    Howard, A.J.3
  • 20
    • 0022919721 scopus 로고
    • Crystal structure of substrate-free pseudomonas putida cytochrome P450
    • Poulos TL, Finzel BC, Howard AJ. Crystal structure of substrate-free pseudomonas putida cytochrome P450. Biochemistry 1986;25:5314-5322
    • (1986) Biochemistry , vol.25 , pp. 5314-5322
    • Poulos, T.L.1    Finzel, B.C.2    Howard, A.J.3
  • 23
    • 0345687195 scopus 로고    scopus 로고
    • An open conformation of the mammalian P4502B4 at 1.6-A resolution
    • Scott EE, He YA, Wester MR, et al. An open conformation of the mammalian P4502B4 at 1.6-A resolution. Proc Natl Acad Sci USA 2003;100:13196-13201
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 13196-13201
    • Scott, E.E.1    He, Y.A.2    Wester, M.R.3
  • 24
    • 3042553224 scopus 로고    scopus 로고
    • Structure of mammalian cytochrome P450 2B4 complexed with 4-( 4-chlorophenyl imidazole at 1.9A resolution: Insights into the range of P450 conformations and the coordination of the redox partner binding
    • Scott EE, White MA, He YA, et al. Structure of mammalian cytochrome P450 2B4 complexed with 4-(4-chlorophenyl imidazole at 1.9A resolution: Insights into the range of P450 conformations and the coordination of the redox partner binding. J Biol Chem 2004;279:27294-301
    • (2004) J Biol Chem , vol.279 , pp. 27294-27301
    • Scott, E.E.1    White, M.A.2    He, Y.A.3
  • 25
    • 0031013972 scopus 로고    scopus 로고
    • The structure of the cytochrome P450BM-3 haem domain complexed with the fatty acid substrate, palmitoleic acid
    • Li H, Poulos TL. The structure of the cytochrome P450BM-3 haem domain complexed with the fatty acid substrate, palmitoleic acid. Nat Struct Biol 1997;4:140-146
    • (1997) Nat Struct Biol , vol.4 , pp. 140-146
    • Li, H.1    Poulos, T.L.2
  • 26
    • 33846383667 scopus 로고    scopus 로고
    • Differential behavior of the sub-sites of cytochrome P450 active site in binding of substrates, and products (implications for coupling/uncoupling)
    • Narasimhulu S. Differential behavior of the sub-sites of cytochrome P450 active site in binding of substrates, and products (implications for coupling/uncoupling). Biochim Biophys Acta 2007;1770:360-375
    • (2007) Biochim Biophys Acta , vol.1770 , pp. 360-375
    • Narasimhulu, S.1
  • 27
    • 2542520761 scopus 로고    scopus 로고
    • Theoretical study of the ligand-CYP2B4 complexes: Effect of structure on binding free energies and heme spin state
    • Harris DL, Park JY, Gruenge L, et al. Theoretical study of the ligand-CYP2B4 complexes: Effect of structure on binding free energies and heme spin state. Proteins 2004;55:895-914
    • (2004) Proteins , vol.55 , pp. 895-914
    • Harris, D.L.1    Park, J.Y.2    Gruenge, L.3
  • 29
    • 0003436236 scopus 로고    scopus 로고
    • Cytochrome P450 reduction and oxygenation systems
    • Eds. King, TE, Mason, HS, and Morrison, M. University Park Press, Baltimore
    • Gunsalus C, Tyson CA, Lipscomb JD. Cytochrome P450 reduction and oxygenation systems, in oxidases & related redox systems. Vol.2. Eds. King, TE, Mason, HS, and Morrison, M. University Park Press, Baltimore. pp. 583-601
    • Oxidases & Related Redox Systems , vol.2 , pp. 583-601
    • Gunsalus, C.1    Tyson, C.A.2    Lipscomb, J.D.3
  • 30
    • 0031404684 scopus 로고    scopus 로고
    • The dimerization of pseudomonas putida P450cam: Practical consequences and engineering of a monomeric enzyme, protein
    • Nickerson DP, Wong LL. The dimerization of pseudomonas putida P450cam: Practical consequences and engineering of a monomeric enzyme, protein. Engineering 1997;10:1357-1361
    • (1997) Engineering , vol.10 , pp. 1357-1361
    • Nickerson, D.P.1    Wong, L.L.2
  • 31
    • 0015182409 scopus 로고
    • Significance of the steroid-induced type i spectral change in the steroid C-21 hydroxylase system of bovine adrenocortical microsomes
    • Narasimhulu S. Significance of the steroid-induced type I spectral change in the steroid C-21 hydroxylase system of bovine adrenocortical microsomes. Arch Biochem Biophys 1971;147:391-404
    • (1971) Arch Biochem Biophys , vol.147 , pp. 391-404
    • Narasimhulu, S.1
  • 32
    • 0345257913 scopus 로고    scopus 로고
    • Multiple oxidants and multiple mechanisms in cytochrome P450 catalysis
    • Coon MJ. Multiple oxidants and multiple mechanisms in cytochrome P450 catalysis. Biochem Biophys Res Comm 2003;312:163-168
    • (2003) Biochem Biophys Res Comm , vol.312 , pp. 163-168
    • Coon, M.J.1
  • 33
    • 0023074623 scopus 로고
    • P450 Cytochromes: Structure & function
    • Black DS, Coon MJ. P450 Cytochromes: Structure & function. Adv Enzymol 1987;60:35-87
    • (1987) Adv Enzymol , vol.60 , pp. 35-87
    • Black, D.S.1    Coon, M.J.2
  • 34
    • 0017295461 scopus 로고
    • Gunsalus, autooxidation and hydroxylation reactions of oxygentated cytochrome P450cam
    • Lipscomb JD, Sligar SG, Namtvedt MJ, et al. Gunsalus, autooxidation and hydroxylation reactions of oxygentated cytochrome P450cam, J Biol Chem 1976;251:1116-1124
    • (1976) J Biol Chem , vol.251 , pp. 1116-1124
    • Lipscomb, J.D.1    Sligar, S.G.2    Namtvedt, M.J.3
  • 35
    • 0019332509 scopus 로고
    • Studies on the steroid hydroxylation system in adrenal cortex microsomes. Purification and characterization of cytochrome P-450 specific for steroid C-21 hydroxylation
    • Kominami S, Ochi H, Kobayashi Y, et al. Studies on the steroid hydroxylation system in adrenal cortex microsomes. Purification and characterization of cytochrome P-450 specific for steroid C-21 hydroxylation. J Biol Chem 1980;255:3386-3394
    • (1980) J Biol Chem , vol.255 , pp. 3386-3394
    • Kominami, S.1    Ochi, H.2    Kobayashi, Y.3
  • 36
    • 0021096850 scopus 로고
    • Oxidation-reduction properties of rat liver cytochrome P450 and NADPH-cytochrome P450 reductase related to catalysis in reconstituted systems
    • Guengerich PF. Oxidation-reduction properties of rat liver cytochrome P450 and NADPH-cytochrome P450 reductase related to catalysis in reconstituted systems. Biochemistry 1983;22:2811-2820
    • (1983) Biochemistry , vol.22 , pp. 2811-2820
    • Guengerich, P.F.1
  • 37
    • 0030781147 scopus 로고    scopus 로고
    • Kinetics of ferric cytochrome P450 reduction by NADPH-cytochrome P450 reductase
    • Guengerich PF, Johnson WW. Kinetics of ferric cytochrome P450 reduction by NADPH-cytochrome P450 reductase. Biochemistry 1997;36:14741-14750
    • (1997) Biochemistry , vol.36 , pp. 14741-14750
    • Guengerich, P.F.1    Johnson, W.W.2
  • 38
    • 0020147674 scopus 로고
    • One electron photoreduction of bacterial cytochrome P450 by ultraviolet light
    • Pierre J, Bazin M, Debey P, et al. One electron photoreduction of bacterial cytochrome P450 by ultraviolet light. Eur J Biochem 1982;124:533-537
    • (1982) Eur J Biochem , vol.124 , pp. 533-537
    • Pierre, J.1    Bazin, M.2    Debey, P.3
  • 39
    • 0027136008 scopus 로고
    • On the model controversy for substrate-induced spin-state transition in cytochrome P450 (a new perspective)
    • Narasimhulu S. On the model controversy for substrate-induced spin-state transition in cytochrome P450 (a new perspective). Endocr Res 1993;19:233-258
    • (1993) Endocr Res , vol.19 , pp. 233-258
    • Narasimhulu, S.1
  • 40
    • 0000574406 scopus 로고    scopus 로고
    • Evaluation of atypical cytochrome P450 kinetics with two-substrate models: Evidence that multiple substrates can simultaneously bind to cytochromes P450 active sites
    • Korzekwa KR, Krishnamachary M, Shou M, et al. Evaluation of atypical cytochrome P450 kinetics with two-substrate models: Evidence that multiple substrates can simultaneously bind to cytochromes P450 active sites. Biochemistry 1998;37:4137-4147
    • (1998) Biochemistry , vol.37 , pp. 4137-4147
    • Korzekwa, K.R.1    Krishnamachary, M.2    Shou, M.3
  • 41
    • 0028307539 scopus 로고
    • Activation of CYP3A4: Evidence for the simultaneous binding of two substrates in a cytochrome P450 active site
    • Shou M, Grogan J, Mancewics KW, et al. Activation of CYP3A4: Evidence for the simultaneous binding of two substrates in a cytochrome P450 active site. Biochemistry 1994;33:6450-6455
    • (1994) Biochemistry , vol.33 , pp. 6450-6455
    • Shou, M.1    Grogan, J.2    Mancewics, K.W.3
  • 42
    • 13844308070 scopus 로고    scopus 로고
    • Non-michaelis menten kinetics in cytochrome P450-catalyzed reactions
    • Atkins WM. Non-michaelis menten kinetics in cytochrome P450-catalyzed reactions. Annu Rev Pharmacol Toxicol 2005;5:291-310
    • (2005) Annu Rev Pharmacol Toxicol , vol.5 , pp. 291-310
    • Atkins, W.M.1
  • 43
    • 0036201594 scopus 로고    scopus 로고
    • Atypical kinetic profiles in drug metabolism reactions
    • Hutzler JM, Tracy TS. Atypical kinetic profiles in drug metabolism reactions. Drug Metab Dispos 2002;30:355-362
    • (2002) Drug Metab Dispos , vol.30 , pp. 355-362
    • Hutzler, J.M.1    Tracy, T.S.2
  • 44
    • 1842866515 scopus 로고    scopus 로고
    • Quinidine and haloperidol as modifiers of CYP3A4 activity: Multisite kinetic model approach
    • Galetin A, Clark SE, Houston JB. Quinidine and haloperidol as modifiers of CYP3A4 activity: Multisite kinetic model approach. Drug Metab Dispos 2002;30:1512-1522
    • (2002) Drug Metab Dispos , vol.30 , pp. 1512-1522
    • Galetin, A.1    Clark, S.E.2    Houston, J.B.3
  • 45
    • 0034976635 scopus 로고    scopus 로고
    • Heterotropic cooperativity of cytochrome P450 3A4 and potential drug-drug interactions
    • Tang W. Stearns R.A. Heterotropic cooperativity of cytochrome P450 3A4 and potential drug-drug interactions. Curr Drug Metab 2001 2 185-198.
    • (2001) Curr Drug Metab , vol.2 , pp. 185-198
    • Tang, W.1    Stearns, R.A.2
  • 46
    • 4644301430 scopus 로고    scopus 로고
    • The structure of human microsomal cytochrome P4503A4 determined by X-ray crystallography to 2.05-A resolution
    • Tang W, Stearns RA. Heterotropic cooperativity of cytochrome P450 3A4 and potential drug-drug interactions. Curr Drug Metab 2001;2:185-98, 46. Yano JK, Wester MR, Schock GA, et al. The structure of human microsomal cytochrome P4503A4 determined by X-ray crystallography to 2.05-A resolution. J Biol Chem 2004;279:38091-38094
    • (2004) J Biol Chem , vol.279 , pp. 38091-38094
    • Yano, J.K.1    Wester, M.R.2    Schock, G.A.3
  • 47
    • 0031005752 scopus 로고    scopus 로고
    • Human cytochrome P450 3A4-catalyzed testosterone 6 beta hydroxylation and erythromycin demethylation. Competition during catalysis
    • Wang RW, Newton DJ, Scheri TD, et al. Human cytochrome P450 3A4-catalyzed testosterone 6 beta hydroxylation and erythromycin demethylation. Competition during catalysis. Drug Metab Dispos 1997;25:502-507
    • (1997) Drug Metab Dispos , vol.25 , pp. 502-507
    • Wang, R.W.1    Newton, D.J.2    Scheri, T.D.3
  • 49
    • 0042357511 scopus 로고    scopus 로고
    • Multisite kinetic analysis of interactions between prototypical CYP3A4 substrates: Midazolam, testosterone, and nifedipine
    • Galetin A, Clarke SE, Houston JB. Multisite kinetic analysis of interactions between prototypical CYP3A4 substrates: Midazolam, testosterone, and nifedipine. Drug Metab Dispos 2003;31:1108-1116
    • (2003) Drug Metab Dispos , vol.31 , pp. 1108-1116
    • Galetin, A.1    Clarke, S.E.2    Houston, J.B.3
  • 50
    • 0031028518 scopus 로고    scopus 로고
    • Cooperativity in oxidation catalyzed by cytochrome P450 3A4
    • Ueng YF, Kuwabara T, Chun YJ, et al. Cooperativity in oxidation catalyzed by cytochrome P450 3A4. Biochemistry 36:370-381
    • Biochemistry , vol.36 , pp. 370-381
    • Ueng, Y.F.1    Kuwabara, T.2    Chun, Y.J.3
  • 51
    • 0037325958 scopus 로고    scopus 로고
    • Activation of cytochrome P450 2C9-mediated metabolism: Mechanistic evidence in support of kinetic observations
    • Hutzler JM, Wienkers LC, Wahlstrom JL, et al. Activation of cytochrome P450 2C9-mediated metabolism: Mechanistic evidence in support of kinetic observations. Arch Biochem Biophys 2002;410:16-24
    • (2002) Arch Biochem Biophys , vol.410 , pp. 16-24
    • Hutzler, J.M.1    Wienkers, L.C.2    Wahlstrom, J.L.3
  • 52
    • 0034613190 scopus 로고    scopus 로고
    • Crystal structure of a thermophilic cytochrome P450 from the archaeon sulfolobus solfataricus
    • Yano JK, Koo LS, Schuler DJ, et al. Crystal structure of a thermophilic cytochrome P450 from the archaeon sulfolobus solfataricus. J Biol Chem 2000;275:31086-31092
    • (2000) J Biol Chem , vol.275 , pp. 31086-31092
    • Yano, J.K.1    Koo, L.S.2    Schuler, D.J.3
  • 53
    • 0037145075 scopus 로고    scopus 로고
    • Thermophilic cytochrome P450: High resolution structure and functional properties
    • Park SY, Yamane K, Adachi S, et al. Thermophilic cytochrome P450: High resolution structure and functional properties. J Inorg Biochem 2002;91:491-501
    • (2002) J Inorg Biochem , vol.91 , pp. 491-501
    • Park, S.Y.1    Yamane, K.2    Adachi, S.3
  • 54
    • 0028357263 scopus 로고
    • Characterization of recombinant plant cinnamate 4-hydroxylaze produced in yeast ( Kinetic and spectral properties of the major plant P450 of the phenylpropanoid pathway
    • Urban P, Werck-Reichhart D, Teutsch HG, et al. Characterization of recombinant plant cinnamate 4-hydroxylaze produced in yeast (Kinetic and spectral properties of the major plant P450 of the phenylpropanoid pathway. Eur J Biochem 1994;222:843-50
    • (1994) Eur J Biochem , vol.222 , pp. 843-850
    • Urban, P.1    Werck-Reichhart, D.2    Teutsch, H.G.3
  • 55
    • 0032524698 scopus 로고    scopus 로고
    • Interactions of substrate and product with cytochrome P450: P4502B4 vs. P450cam
    • Narasimhulu S, Havran LM, Axelsen PH, et al. Interactions of substrate and product with cytochrome P450: P4502B4 vs. P450cam. ABB 1998;353:228-238
    • (1998) ABB , vol.353 , pp. 228-238
    • Narasimhulu, S.1    Havran, L.M.2    Axelsen, P.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.