276
Views
31
CrossRef citations to date
0
Altmetric
Reviews

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

Pages 1-15 | Published online: 30 Nov 2009

Bibliography

  • Raag R, Poulos TL. Crystal structure of P450cam complexed with camphane, thiocamphor & admantane: factors controlling P450 substrate hydroxylation. Biochemistry 1991;30:2674-84
  • Poulos TL, Raag R. Cytochrome P450cam: crystallography, oxygen activation and electron transfer. FASEB J 1992;6:674-79
  • Kadkhodayan S, Coulter ED, Maryniak DM, Uncoupling of oxygen transfer and electron transfer in the oxygenation of camphor analogues by cytochrome P450cam. J Biol Chem 1995;270:1-7
  • Li H, Narasimhulu S, Havran L, Crystal structure of cytochrome P450cam complexed with its catalytic product, 5-exo-hydroxycamphor. J Am Chem Soc 1995;117:6297-99
  • Dawson H, Anderson LA, Sono M. Spectroscopic investigations of ferric cytochrome P-450-CAM ligand complexes. J Biol Chem 982;257:3606-17
  • 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;257:3073-83
  • Narasimhulu S, Uncoupling of O2 activation from hydroxylation in the steroid C-21 hydroxylase of bovine adrenocortical microsomes. Arch Biochem Biophys 1971;147:384-90
  • Nordbloom GD, Coon MJ. Hydrogen peoxide formation and stoichiometry of hydroxylation reactions catalyzed by highly purified liver microsomal cytochrome p450. Arch Biochem Biophys 1977;180:343-47
  • Imai M, Shimada H, Watanabe Y, 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;86:7823-7
  • Martinis SA, Atkins WM, Stayton PS, A conserved residue of cytochrome P450cam is involved in heme-oxygen stability and activation. J Am Chem Soc 1989;20:9252-3
  • Shimada H, Imai M, Horishi T, 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
  • Gerber NC, Sligar SG. A role for asp-251 in cytochrome P450cam oxygen activation. J Biol Chem 1994;269:4260-66
  • Kimata Y, Shimada H, Hirose T, Role of the Thr252 in cytochrome P450cam: a study with unnatural amino acid mutagenesis. Biochem Biophys Res Comm 1995;208:96-102
  • Schlichting I, Berendzen J, Chu K, The catalytic pathway of cytochrome P450cam at atomic resolution. Science 2000;287:1615-22
  • 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;280:31659-63
  • Poulos TL. Structural biology of P450-oxy complexes. Drug Metab Rev 2007;39:557-66
  • Makris TM, Koenig K, Schlicting I, . Alteration of P450 distal pocket solvent leads to impaired proton delivery and changes in heme geometry. Biochemistry 2007;46:14129-40
  • Poulos TL, Howard AJ. Crystal structures of metyrapone- and phenyimidazole-inhibited complexes of cytochrome P450cam. Biochemistry 1987;26:8165-74
  • Poulos TL, Finzel BC, Howard AJ. High resolution crystal structure of cytochrome P450cam. J Mol Biol 1987;195:687-700
  • Poulos TL, Finzel BC, Howard AJ. Crystal structure of substrate-free pseudomonas putida cytochrome P450. Biochemistry 1986;25:5314-22
  • Poulos TL. Structural biology of heme monooxygenases. Biochem Biophys Res Commun Struct Biol 2005;338:337-45
  • Poulos TL, Johnson EF. Structures of cytochrome P450 enzymes, in cytochrome P450, structure, mechanism & biochemistry, 3rd Edition, Ed: Paul R Ortiz de Montellano, (2005) pp. 85-113
  • Scott EE, He YA, Wester MR, An open conformation of the mammalian P4502B4 at 1.6-A resolution. Proc Natl Acad Sci USA 2003;100:13196-201
  • Scott EE, White MA, He YA, 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
  • 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;4:140-6
  • 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;1770:360-75
  • Harris DL, Park JY, Gruenge L, Theoretical study of the ligand-CYP2B4 complexes: effect of structure on binding free energies and heme spin state. Proteins 2004;55:895-914
  • Lipscomb JD, Harrison JE, Dus KM, “Cytochrome P450cam: SS-dimer and –SH derivative reactivities. Biochem Biophys Res Commun 1978;83:771-8
  • 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
  • Nickerson DP, Wong LL. The dimerization of pseudomonas putida P450cam: practical consequences and engineering of a monomeric enzyme, protein. Engineering 1997;10:1357-61
  • 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
  • Coon MJ. Multiple oxidants and multiple mechanisms in cytochrome P450 catalysis. Biochem Biophys Res Comm 2003;312:163-68
  • Black DS, Coon MJ. P450 Cytochromes: structure & function. Adv Enzymol 1987;60:35-87
  • Lipscomb JD, Sligar SG, Namtvedt MJ, Gunsalus, autooxidation and hydroxylation reactions of oxygentated cytochrome P450cam, J Biol Chem 1976;251:1116-24
  • Kominami S, Ochi H, Kobayashi Y, 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;255:3386-94
  • Guengerich PF. Oxidation-reduction properties of rat liver cytochrome P450 and NADPH-cytochrome P450 reductase related to catalysis in reconstituted systems. Biochemistry 1983;22:2811-0
  • Guengerich PF, Johnson WW. Kinetics of ferric cytochrome P450 reduction by NADPH-cytochrome P450 reductase. Biochemistry 1997;36:14741-50
  • Pierre J, Bazin M, Debey P, One electron photoreduction of bacterial cytochrome P450 by ultraviolet light. Eur J Biochem 1982;124:533-7
  • Narasimhulu S. On the model controversy for substrate-induced spin-state transition in cytochrome P450 (a new perspective). Endocr Res 1993;19:233-58
  • Korzekwa KR, Krishnamachary M, Shou M, Evaluation of atypical cytochrome P450 kinetics with two-substrate models: evidence that multiple substrates can simultaneously bind to cytochromes P450 active sites. Biochemistry 1998;37:4137-47
  • Shou M, Grogan J, Mancewics KW, Activation of CYP3A4: evidence for the simultaneous binding of two substrates in a cytochrome P450 active site. Biochemistry 1994;33:6450-5
  • Atkins WM. Non-michaelis menten kinetics in cytochrome P450-catalyzed reactions. Annu Rev Pharmacol Toxicol 2005;5:291-310
  • Hutzler JM, Tracy TS. Atypical kinetic profiles in drug metabolism reactions. Drug Metab Dispos 2002;30:355-62
  • Galetin A, Clark SE, Houston JB. Quinidine and haloperidol as modifiers of CYP3A4 activity: multisite kinetic model approach. Drug Metab Dispos 2002;30:1512-22
  • Tang W, Stearns RA. Heterotropic cooperativity of cytochrome P450 3A4 and potential drug-drug interactions. Curr Drug Metab 2001;2:185-98,
  • Yano JK, Wester MR, Schock GA, The structure of human microsomal cytochrome P4503A4 determined by X-ray crystallography to 2.05-A resolution. J Biol Chem 2004;279:38091-94
  • Wang RW, Newton DJ, Scheri TD, Human cytochrome P450 3A4-catalyzed testosterone 6 beta hydroxylation and erythromycin demethylation. Competition during catalysis. Drug Metab Dispos 1997;25:502-7
  • Wang RW, Newton DJ, Liu N, Human cytochrome P450 3A4: in vitro drug-drug interaction patterns are substrate dependent. 2000;28:360-6
  • Galetin A, Clarke SE, Houston JB. Multisite kinetic analysis of interactions between prototypical CYP3A4 substrates: midazolam, testosterone, and nifedipine. Drug Metab Dispos 2003;31:1108-16
  • Ueng YF, Kuwabara T, Chun YJ, Cooperativity in oxidation catalyzed by cytochrome P450 3A4. Biochemistry 36:370-81
  • Hutzler JM, Wienkers LC, Wahlstrom JL, Activation of cytochrome P450 2C9-mediated metabolism: mechanistic evidence in support of kinetic observations. Arch Biochem Biophys 2002;410:16-24
  • Yano JK, Koo LS, Schuler DJ, Crystal structure of a thermophilic cytochrome P450 from the archaeon sulfolobus solfataricus. J Biol Chem 2000;275:31086-92
  • Park SY, Yamane K, Adachi S, Thermophilic cytochrome P450: high resolution structure and functional properties. J Inorg Biochem 2002;91:491-501
  • Urban P, Werck-Reichhart D, Teutsch HG, 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
  • Narasimhulu S, Havran LM, Axelsen PH, Interactions of substrate and product with cytochrome P450: P4502B4 vs. P450cam. ABB 1998;353:228-38

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.