메뉴 건너뛰기




Volumn 50, Issue 22, 2011, Pages 4903-4911

Structural analysis of mammalian cytochrome P450 2B4 covalently bound to the mechanism-based inactivator tert-butylphenylacetylene: Insight into partial enzymatic activity

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; ACTIVE SITE RESIDUES; COMPUTATIONAL ANALYSIS; COVALENTLY BOUND; CYTOCHROME P450; ENZYMATIC ACTIVITIES; IN-SILICO; PLASTIC REGIONS; RESIDUAL ACTIVITY;

EID: 79958024314     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi200482g     Document Type: Article
Times cited : (36)

References (46)
  • 1
    • 38949099990 scopus 로고    scopus 로고
    • Mechanism-based inactivation of human cytochromes P450s: Experimental characterization, reactive intermediates, and clinical implications
    • DOI 10.1021/tx7002504
    • Hollenberg, P. F., Kent, U. M., and Bumpus, N. N. (2008) Mechanism-based inactivation of human cytochromes P450s: Experimental characterization, reactive intermediates, and clinical implications Chem. Res. Toxicol. 21, 189-205 (Pubitemid 351219719)
    • (2008) Chemical Research in Toxicology , vol.21 , Issue.1 , pp. 189-205
    • Hollenberg, P.F.1    Kent, U.M.2    Bumpus, N.N.3
  • 2
    • 63849160781 scopus 로고    scopus 로고
    • Mechanistic analysis of the inactivation of cytochrome P450 2B6 by phencyclidine: Effects on substrate binding, electron transfer, and uncoupling
    • Shebley, M., Kent, U. M., Ballou, D. P., and Hollenberg, P. F. (2009) Mechanistic analysis of the inactivation of cytochrome P450 2B6 by phencyclidine: Effects on substrate binding, electron transfer, and uncoupling Drug Metab. Dispos. 37, 745-752
    • (2009) Drug Metab. Dispos. , vol.37 , pp. 745-752
    • Shebley, M.1    Kent, U.M.2    Ballou, D.P.3    Hollenberg, P.F.4
  • 3
    • 0036151664 scopus 로고    scopus 로고
    • Effect of 17-α-ethynylestradiol on activities of cytochrome P450 2B (P450 2B) enzymes: Characterization of inactivation of P450s 2B1 and 2B6 and identification of metabolites
    • Kent, U. M., Mills, D. E., Rajnarayanan, R. V., Alworth, W. L., and Hollenberg, P. F. (2002) Effect of 17-α-ethynylestradiol on activities of cytochrome P450 2B (P450 2B) enzymes: Characterization of inactivation of P450s 2B1 and 2B6 and identification of metabolites J. Pharmacol. Exp. Ther. 300, 549-558
    • (2002) J. Pharmacol. Exp. Ther. , vol.300 , pp. 549-558
    • Kent, U.M.1    Mills, D.E.2    Rajnarayanan, R.V.3    Alworth, W.L.4    Hollenberg, P.F.5
  • 4
    • 0022253108 scopus 로고
    • On the mechanism of the inactivation of the major phenobarbital-inducible isozyme of rat liver cytochrome P-450 by chloramphenicol
    • Halpert, J. R., Miller, N., and Gorsky, L. (1985) On the mechanism of the inactivation of the major phenobarbital-inducible isozyme of rat liver cytochrome P450 by chloramphenicol J. Biol. Chem. 260, 8397-8403 (Pubitemid 15249848)
    • (1985) Journal of Biological Chemistry , vol.260 , Issue.14 , pp. 8397-8403
    • Halpert, J.R.1    Miller, N.E.2    Gorsky, L.D.3
  • 6
    • 0032527044 scopus 로고    scopus 로고
    • Mechanism-based inactivation of cytochromes P450 2E1 and 2B1 by 5- phenyl-1-pentyne
    • DOI 10.1006/abbi.1998.0679
    • Roberts, E. S., Alworth, W. L., and Hollenberg, P. F. (1998) Mechanism-based inactivation of cytochromes P450 2E1 and 2B1 by 5-phenyl-1-pentyne Arch. Biochem. Biophys. 354, 295-302 (Pubitemid 28373980)
    • (1998) Archives of Biochemistry and Biophysics , vol.354 , Issue.2 , pp. 295-302
    • Roberts, E.S.1    Alworth, W.L.2    Hollenberg, P.F.3
  • 7
    • 0027275796 scopus 로고
    • Mechanism-based inactivation of cytochrome P450 2B1 by 2- ethynylnaphthalene: Identification of an active-site peptide
    • Roberts, E. S., N.E., H., Alworth, W. L., and Hollenberg, P. F. (1993) Mechanism-based inactivation of cytochrome P450 2B1 by 2-ethynylnaphthalene: Identification of an active-site peptide Chem. Res. Toxicol. 6, 470-479 (Pubitemid 23212515)
    • (1993) Chemical Research in Toxicology , vol.6 , Issue.4 , pp. 470-479
    • Roberts, E.S.1    Hopkins, N.E.2    Alworth, W.L.3    Hollenberg, P.F.4
  • 9
    • 0034055362 scopus 로고    scopus 로고
    • Mechanism-based inactivation of cytochrome P450 2B1 by 7- ethynylcoumarin: Verification of apo-P450 adduction by electrospray ion trap mass spectrometry
    • DOI 10.1021/tx990195s
    • Regal, K. A., Schrag, M. L., Kent, U. M., Wienkers, L. C., and Hollenberg, P. F. (2000) Mechanism-based inactivation of cytochrome P450 2B1 by 7-ethynylcoumarin: Verification of apo-P450 adduction by electrospray ion trap mass spectrometry Chem. Res. Toxicol. 13, 262-270 (Pubitemid 30241653)
    • (2000) Chemical Research in Toxicology , vol.13 , Issue.4 , pp. 262-270
    • Regal, K.A.1    Schrag, M.L.2    Kent, U.M.3    Wienkers, L.C.4    Hollenberg, P.F.5
  • 10
    • 14844347491 scopus 로고    scopus 로고
    • P450 active site architecture and reversibility: Inactivation of cytochromes P450 2B4 and 2B4 T302A by tert-butyl acetylenes
    • DOI 10.1021/bi0478953
    • Blobaum, A. L., Harris, D. L., and Hollenberg, P. F. (2005) P450 active site architecture and reversibility: Inactivation of cytochromes P450 2B4 and 2B4 T302A by tert -butyl acetylenes Biochemistry 44, 3831-3844 (Pubitemid 40358035)
    • (2005) Biochemistry , vol.44 , Issue.10 , pp. 3831-3844
    • Blobaum, A.L.1    Harris, D.L.2    Hollenberg, P.F.3
  • 11
    • 70350443423 scopus 로고    scopus 로고
    • Mechanism-based inactivation of CYP2B1 and its F-helix mutant by two tert -butyl acetylenic compounds: Covalent modification of prosthetic heme versus apoprotein
    • Lin, H. L., Zhang, H., Noon, K. R., and Hollenberg, P. F. (2009) Mechanism-based inactivation of CYP2B1 and its F-helix mutant by two tert -butyl acetylenic compounds: Covalent modification of prosthetic heme versus apoprotein J. Pharmacol. Exp. Ther. 331, 392-403
    • (2009) J. Pharmacol. Exp. Ther. , vol.331 , pp. 392-403
    • Lin, H.L.1    Zhang, H.2    Noon, K.R.3    Hollenberg, P.F.4
  • 12
    • 77952389208 scopus 로고    scopus 로고
    • Covalent modification of Thr302 in cytochrome P450 2B1 by the mechanism-based inactivator 4- tert -butylphenylacetylene
    • Lin, H. L., Zhang, H., Jushchyshyn, M., and Hollenberg, P. F. (2010) Covalent modification of Thr302 in cytochrome P450 2B1 by the mechanism-based inactivator 4- tert -butylphenylacetylene J. Pharmacol. Exp. Ther. 333, 663-669
    • (2010) J. Pharmacol. Exp. Ther. , vol.333 , pp. 663-669
    • Lin, H.L.1    Zhang, H.2    Jushchyshyn, M.3    Hollenberg, P.F.4
  • 13
    • 70350457938 scopus 로고    scopus 로고
    • Tert -Butylphenylacetylene is a potent mechanism-based inactivator of cytochrome P450 2B4: Inhibition of cytochrome P450 catalysis by steric hinderance
    • Zhang, H., Lin, H.-L., Walker, V. J., Hamdane, D., and Hollenberg, P. F. (2009) tert -Butylphenylacetylene is a potent mechanism-based inactivator of cytochrome P450 2B4: Inhibition of cytochrome P450 catalysis by steric hinderance Mol. Pharmacol. 76, 1011-1018
    • (2009) Mol. Pharmacol. , vol.76 , pp. 1011-1018
    • Zhang, H.1    Lin, H.-L.2    Walker, V.J.3    Hamdane, D.4    Hollenberg, P.F.5
  • 14
    • 0034869034 scopus 로고    scopus 로고
    • Mechanism-based inactivators as probes of cytochrome P450 structure and function
    • DOI 10.2174/1389200013338478
    • Kent, U. M., Juschyshyn, M. I., and Hollenberg, P. F. (2001) Mechanism-based inactivators as probes of cytochrome P450 structure and function Curr. Drug Metab. 2, 215-243 (Pubitemid 32782795)
    • (2001) Current Drug Metabolism , vol.2 , Issue.3 , pp. 215-243
    • Kent, U.M.1    Jushchyshyn, M.I.2    Hollenberg, P.F.3
  • 15
    • 24744459452 scopus 로고    scopus 로고
    • Crystallographic study on the dioxygen complex of wild-type and mutant cytochrome P450cam: Implications for the dioxygen activation mechanism
    • DOI 10.1074/jbc.M505261200
    • Nagano, S. and Poulos, T. L. (2005) Crystallographic study on the dioxygen complex of wild-type and mutant cytochrome P450cam. Implications for the dioxygen activation mechanism J. Biol. Chem. 280, 31659-31663 (Pubitemid 41291912)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.36 , pp. 31659-31663
    • Nagano, S.1    Poulos, T.L.2
  • 17
    • 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
    • DOI 10.1073/pnas.93.10.4644
    • Vaz, A. D. N., Pernecky, S. J., Raner, G. M., and Coon, M. J. (1996) Peroxo-iron and oxenoid-iron species as alternative oxyegenating agents in cytochrome P450-catalyzed reactions: Switching by threonine-302 to alanine mutagenesis of cytochrome P450 2B4 Proc. Natl. Acad. Sci. U.S.A. 93, 4644-4648 (Pubitemid 26163496)
    • (1996) Proceedings of the National Academy of Sciences of the United States of America , vol.93 , Issue.10 , pp. 4644-4648
    • Vaz, A.D.N.1    Pernecky, S.J.2    Raner, G.M.3    Coon, M.J.4
  • 19
    • 0027537089 scopus 로고
    • Replacement of Thr-303 of P450 2E1 with serine modifies the regioselectivity of its fatty acid hydroxylase activity
    • Fukuda, T., Imai, Y., Komori, M., Nakamura, M., Kusunose, E., Satouchi, K., and Kusunose, M. (1993) Replacement of Thr-303 of P450 2E1 with serine modifies the regioselectivity of its fatty acid hydroxylase activity J. Biochem. 113, 7-12 (Pubitemid 23068834)
    • (1993) Journal of Biochemistry , vol.113 , Issue.1 , pp. 7-12
    • Fukuda, T.1    Imai, Y.2    Komori, M.3    Nakamura, M.4    Kusunose, E.5    Satouchi, K.6    Kusunose, M.7
  • 20
    • 76149134076 scopus 로고    scopus 로고
    • Defining the structural consequences of mechanism-based inactivation of mammalian cytochrome P450 2B4 using resonance Raman spectroscopy
    • Mak, P. J., Zhang, H., Hollenberg, P. F., and Kincaid, J. R. (2010) Defining the structural consequences of mechanism-based inactivation of mammalian cytochrome P450 2B4 using resonance Raman spectroscopy J. Am. Chem. Soc. 132, 1494-1495
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 1494-1495
    • Mak, P.J.1    Zhang, H.2    Hollenberg, P.F.3    Kincaid, J.R.4
  • 23
    • 70350028665 scopus 로고    scopus 로고
    • Effect of conformational dynamics on substrate recognition and specificity as probed by the introduction of a de novo disulfide bond into cytochrome P450 2B1
    • Zhang, H., Kenaan, C., Hamdane, D., Hoa, G. H., and Hollenberg, P. F. (2009) Effect of conformational dynamics on substrate recognition and specificity as probed by the introduction of a de novo disulfide bond into cytochrome P450 2B1 J. Biol. Chem. 284, 25678-25686
    • (2009) J. Biol. Chem. , vol.284 , pp. 25678-25686
    • Zhang, H.1    Kenaan, C.2    Hamdane, D.3    Hoa, G.H.4    Hollenberg, P.F.5
  • 25
    • 85046526624 scopus 로고
    • Evaluation of single-crystal X-ray diffraction data from a position-sensitive detector
    • Kabsch, W. (1988) Evaluation of single-crystal X-ray diffraction data from a position-sensitive detector J. Appl. Crystallogr. 21, 916-924
    • (1988) J. Appl. Crystallogr. , vol.21 , pp. 916-924
    • Kabsch, W.1
  • 29
    • 76149120388 scopus 로고    scopus 로고
    • AutoDock Vina: Improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading
    • Trott, O. and Olson, A. J. (2010) AutoDock Vina: Improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading J. Comput. Chem. 31, 455-461
    • (2010) J. Comput. Chem. , vol.31 , pp. 455-461
    • Trott, O.1    Olson, A.J.2
  • 31
    • 0029160249 scopus 로고
    • Thermodynamics of water mediating protein-ligand interactions in cytochrome P450cam: A molecular dynamics study
    • Helms, V. and Wade, R. C. (1995) Thermodynamics of water mediating protein-ligand interactions in cytochrome P450cam: A molecular dynamics study Biophys. J. 69, 810-824
    • (1995) Biophys. J. , vol.69 , pp. 810-824
    • Helms, V.1    Wade, R.C.2
  • 34
    • 3042553224 scopus 로고    scopus 로고
    • Structure of mammalian cytochrome P450 2B4 complexed with 4-(4-chlorophenyl)imidazole at 1.9-A resolution: Insight into the range of P450 conformations and the coordination of redox partner binding
    • DOI 10.1074/jbc.M403349200
    • 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 coordination of redox partner binding J. Biol. Chem. 279, 27294-27301 (Pubitemid 38812569)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.26 , 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
  • 35
    • 34548423359 scopus 로고    scopus 로고
    • Structural and thermodynamic consequences of 1-(4-chlorophenyl)imidazole binding to cytochrome P450 2B4
    • DOI 10.1021/bi7011614
    • Zhao, Y., Sun, L., Muralidhara, B. K., Kumar, S., White, M. A., Stout, C. D., and Halpert, J. R. (2007) Structural and thermodynamic consequences of 1-(4-chlorophenyl)imidazole binding to cytochrome P450 2B4 Biochemistry 46, 11559-11567 (Pubitemid 47585501)
    • (2007) Biochemistry , vol.46 , Issue.41 , pp. 11559-11567
    • Zhao, Y.1    Sun, L.2    Muralidhara, B.K.3    Kumar, S.4    White, M.A.5    Stout, C.D.6    Halpert, J.R.7
  • 36
    • 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
    • DOI 10.1074/jbc.M511464200
    • 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 (Pubitemid 43847698)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.9 , 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
  • 37
    • 66649125786 scopus 로고    scopus 로고
    • Crystal structures of cytochrome P450 2B4 in complex with the inhibitor 1-biphenyl-4-methyl-1 H -imidazole: Ligand induced structural response through α-helical repositioning
    • Gay, S. C., Sun, L., Maekawa, K., Halpert, J. R., and Stout, C. D. (2009) Crystal structures of cytochrome P450 2B4 in complex with the inhibitor 1-biphenyl-4-methyl-1 H -imidazole: Ligand induced structural response through α-helical repositioning Biochemistry 48, 4762-4771
    • (2009) Biochemistry , vol.48 , pp. 4762-4771
    • Gay, S.C.1    Sun, L.2    Maekawa, K.3    Halpert, J.R.4    Stout, C.D.5
  • 38
    • 33646357912 scopus 로고    scopus 로고
    • Conformational flexibility of mammalian cytochrome P450 2B4 in binding imidazole inhibitors with different ring chemistry and side chains: Solution thermodynamics and molecular modeling
    • DOI 10.1074/jbc.M509696200
    • Muralidhara, B. K., Negi, S., Chin, C. C., Braun, W., and Halpert, J. R. (2006) Conformational flexibility of mammalian cytochrome P450 2B4 in binding imidazole inhibitors with different ring chemistry and side chains. Solution thermodynamics and molecular modeling J. Biol. Chem. 281, 8051-8061 (Pubitemid 43847423)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.12 , pp. 8051-8061
    • Muralidhara, B.K.1    Negi, S.2    Chin, C.C.3    Braun, W.4    Halpert, J.R.5
  • 39
    • 0019509069 scopus 로고
    • Covalent modification of lysine during the suicide inactivation of rat liver cytochrome P-450 by chloramphenicol
    • DOI 10.1016/S0006-2952(81)80010-X
    • Halpert, J. (1981) Covalent modification of lysine during the suicide inactivation of rat liver cytochrome P-450 by chloramphenicol Biochem. Pharmacol. 30, 875-881 (Pubitemid 11096139)
    • (1981) Biochemical Pharmacology , vol.30 , Issue.8 , pp. 875-881
    • Halpert, J.1
  • 40
    • 79951566203 scopus 로고    scopus 로고
    • Targeting of the highly conserved threonine 302 residue of cytochromes P450 2B family during mechanism-based inactivation by aryl acetylenes
    • Zhang, H., Lin, H. L., Kenaan, C., and Hollenberg, P. F. (2011) Targeting of the highly conserved threonine 302 residue of cytochromes P450 2B family during mechanism-based inactivation by aryl acetylenes Arch. Biochem. Biophys. 507, 135-143
    • (2011) Arch. Biochem. Biophys. , vol.507 , pp. 135-143
    • Zhang, H.1    Lin, H.L.2    Kenaan, C.3    Hollenberg, P.F.4
  • 41
    • 77951247090 scopus 로고    scopus 로고
    • P450cam visits an open conformation in the absence of substrate
    • Lee, Y. T., Wilson, R. F., Rupniewski, I., and Goodin, D. B. (2010) P450cam visits an open conformation in the absence of substrate Biochemistry 49, 3412-3419
    • (2010) Biochemistry , vol.49 , pp. 3412-3419
    • Lee, Y.T.1    Wilson, R.F.2    Rupniewski, I.3    Goodin, D.B.4
  • 43
    • 79551473016 scopus 로고    scopus 로고
    • The structure of CYP101D2 unveils a potential path for substrate entry into the active site
    • Yang, W., Bell, S. G., Wang, H., Zhou, W., Bartlam, M., Wong, L. L., and Rao, Z. (2010) The structure of CYP101D2 unveils a potential path for substrate entry into the active site Biochem. J. 433, 85-93
    • (2010) Biochem. J. , vol.433 , pp. 85-93
    • Yang, W.1    Bell, S.G.2    Wang, H.3    Zhou, W.4    Bartlam, M.5    Wong, L.L.6    Rao, Z.7
  • 44
    • 33751038821 scopus 로고    scopus 로고
    • Investigation of the role of cytochrome P450 2B4 active site residues in substrate metabolism based on crystal structures of the ligand-bound enzyme
    • DOI 10.1016/j.abb.2006.08.024, PII S000398610600333X
    • Hernandez, C. E., Kumar, S., Liu, H., and Halpert, J. R. (2006) Investigation of the role of cytochrome P450 2B4 active site residues in substrate metabolism based on crystal structures of the ligand-bound enzyme Arch. Biochem. Biophys. 455, 61-67 (Pubitemid 44754700)
    • (2006) Archives of Biochemistry and Biophysics , vol.455 , Issue.1 , pp. 61-67
    • Hernandez, C.E.1    Kumar, S.2    Liu, H.3    Halpert, J.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.