318
Views
61
CrossRef citations to date
0
Altmetric
Research Article

MECHANISTIC ENZYMOLOGY OF OXYGEN ACTIVATION BY THE CYTOCHROMES P450

, , , &
Pages 691-708 | Published online: 27 Nov 2002

REFERENCES

  • Sligar S.G. Nature's Universal Oxygenases: The Cytochromes P450. Essays Biochem. 1999; 34: 71–83
  • Guengerich F.P. Common and Uncommon Cytochrome P450 Reactions Related to Metabolism and Chemical Toxicity. Chem. Res. Toxicol. 2001; 14: 611–650
  • Brewer C.B., Peterson J.A. Single Turnover Kinetics of the Reaction Between Oxycytochrome P-450cam and Reduced Putidaredoxin. J. Biol. Chem. 1988; 263: 791–798
  • Tsai R., Yu C.-A., Gunsalus I.C., Peisach J., Blumberg W.E., Orme-Johnson W.H., Beinert H. Spin-State Changes in Cytochrome P-450cam on Binding of Specific Substrates. Proc. Natl Acad. Sci. USA 1970; 66: 1157–1163
  • Sligar S.G. Coupling of Spin, Substrate, and Redox Equilibria in Cytochrome P-450. Biochemistry 1976; 15: 5399–5406
  • Fisher M.T., Sligar S.G. Control of Heme Protein Redox Potential and Reduction Rates: Linear Free Energy Relationships Between Potential and Ferric Spin State Equilibrium. J. Am. Chem. Soc. 1985; 107: 5018–5019
  • Sibbeson O., Zhang Z., Ortiz de Montellano P.R. Cytochrome P450cam Substrate Specificity: Relationship Between Structure and Catalytic Oxidation of Alkylbenzenes. Arch. Biochem. Biophys. 1998; 353: 285–296
  • Gould P., Gelb M.H., Sligar S.G. Interaction of 5-Bromocamphor with Cytochrome P-450cam. J. Biol. Chem. 1981; 256: 6686–6691
  • Sharrock M., Debrunner P.G., Schulz C., Lipscomb J.D., Marshall V., Gunsalus I.C. Cytochrome P450cam and Its Complexes. Mossbauer Parameters of the Heme Iron. Biochim. Biophys. Acta 1976; 420: 8–26
  • Champion P.M., Gunsalus I.C., Wagner G.C. Resonance Raman Investigations of Cytochrome P450cam from Pseudomonas putida. J. Am. Chem. Soc. 1978; 100: 3743–3751
  • Macdonald I.D.G., Sligar S.G., Christian J.F., Unno M., Champion P.M. Identification of the Fe–O–O Bending Mode in Oxycytochrome P450cam by Resonance Raman Spectroscopy. J. Am. Chem. Soc. 1999; 121: 376–380
  • Katagiri M., Ganguli B.N., Gunsalus I.C. A Soluble Cytochrome P-450 Functional in Methylene Hydroxylation. J. Biol. Chem. 1968; 243: 3543–3546
  • Schulz C.E., Rutter R., Sage J.T., Debrunner P.G., Hager L.P. Mossbauer and Electron Paramagnetic Resonance Studies of Horseradish Peroxidase and Its Catalytic Intermediates. Biochemistry 1984; 23: 4743–4754
  • Poulos T.L., Kraut J. The Stereochemistry of Peroxidase Catalysis. J. Biol. Chem. 1980; 255: 8199–8205
  • Harris D.L., Loew G.H. Investigation of the Proton-Assisted Pathway to Formation of the Catalytically Active, Ferryl Species of P450s by Molecular Dynamics Studies of P450eryF. J. Am. Chem. Soc. 1996; 118(27)6377–6387
  • Groves J.T., McClusky G.A. Aliphatic Hydroxylation via Oxygen Rebound. Oxygen Transfer Catalyzed by Iron. J. Am. Chem. Soc. 1976; 98: 859–861
  • Dolphin D., James B.R., Welborn H.C. Proton Activities for Three States of Cytochrome P-450cam. Biochem. Biophys. Res. Commun. 1979; 88: 415–421
  • Finzel B.C., Poulos T.L., Kraut J. Crystal Structure of Yeast Cytochrome c Peroxidase Refined at 1.7-Angstrom Resolution. J. Biol. Chem. 1984; 259: 13027–13036
  • Poulos T.L., Edwards S.L., Wariishi H., Gold M.G. Crystallographic Refinement of Lignin Peroxidase at 2A. J. Biol. Chem. 1993; 268: 4429–4440
  • Poulos T.L., Finzel B.C., Gunsalus I.C., Wagner G.C., Kraut J. The 2.6-Angstrom Crystal Structure of Pseudomonas putida Cytochrome P-450. J. Biol. Chem. 1985; 260: 16122–16130
  • Okamoto N., Imai Y., Shoun H., Shiro Y. Site-Directed Mutagenesis of the Conserved Threonine (Thr243) at Distal Helix of Fungal Cytochrome P450nor. Biochemistry 1998; 37: 8839–8847
  • Yeom H., Sligar S.G., Poulos T., Fulco A. The Role of Thr268 in the Oxygen Activation of Cytochrome BM-3. Biochemistry 1995; 34: 14733–14740
  • Yanagita K., Sagami I., Daff S., Shimizu T. Marked Enhancement in the Reductive Dehalogenation of Hexachloroethane by a Thr319Ala Mutation of Cytochrome P450 1A2. Biochem. Biophys. Res. Commun. 1998; 249: 678–682
  • Nitahara Y., Kishimoto K., Yabusaki Y., Gotoh O., Yoshida Y., Horiuchi Y., Aoyama Y. The Amino Acid Residues Affecting the Activity and Azole Susceptibility of Rat cyp51. J. Biochem. 2001; 129: 761–768
  • Kao Y.C., Korzekwa K.R., Laughton C.A., Chen S. Evaluation of the Mechanism of Aromatase cytP450. Eur. J. Biochem. 2001; 268: 243–251
  • Roussel F., Khan K.K., Halpert J.R. The Importance of srs-1 Residues in Catalytic Specificity of Cytochrome P450 3A4. Arch. Biochem. Biophys. 2000; 374: 269–278
  • Coon M.J., Vaz A.D.N., McGinnity D.F., Peng H.M. Multiple Oxygen Species in P450 Catalysis. Drug Metab. Dispos. 1998; 26: 1190–1193
  • Imai Y., Nakamura M. Point Mutations at Threonine-301 Modify Substrate Specificity of Rabbit liver Microsomal Cytochromes P-450 (Laurate (Omega-1)-Hydroxylase and Testosterone 16 Alpha-Hydroxylase). Biochem. Biophys. Res. Commun. 1989; 158: 717–722
  • Imai M., Shimada H., Watanabe Y., Matsushima-Hibiya Y., Makino R., Koga H., Horiuchi T., Ishimura Y. Uncoupling of the Cytochrome P-450cam Monooxygenase Reaction by a Single Mutation, Threonine-252 to Alanine or Valine: A Possible Role of the Hydroxy Amino Acid in Oxygen Activation. Proc. Natl Acad. Sci. USA 1989; 86: 7823–7827
  • Martinis S.A., Atkins W.M., Stayton P.S., Sligar S.G. A Conserved Residue of Cytochrome P-450 Is Involved in Heme-Oxygen Stability and Activation. J. Am. Chem. Soc. 1989; 111: 9252–9253
  • Raag R., Martinis S.A., Sligar S.G., Poulos T.L. Crystal Structure of the Cytochrome P-450cam Active Site Mutant Thr252Ala. Biochemistry 1991; 30: 11420–11429
  • Shimada H., Watanabe Y., Imai M., Makino R., Koga H., Horiuchi T., Ishimura Y. The Role of Threonine 252 in Oxygen Activation by Cytochrome P-450cam: Mechanistic Studies by Site-Directed Mutagenesis. Dioxygen Activation and Homogeneous Catalytic Oxidation, L.I. Simandi. Elsevier Science Publishers, Amsterdam 1991; 313–319
  • Shimada, H.; Makino, R.; Unno, M.; Horiuchi, T.; Ishimura, Y. Proton and Electron Transfer Mechanism in Dioxygen Activation by Cytochrome P450cam. 8th Cytochrome P450 Int. Conf., Paris, France, 1993; Lechner, M.C., Eds.; Libbey: Montrouge, 1994; 299–306.
  • Kimata Y., Shimada H., Hirose T., Ishimura Y. Role of Thr-252 in Cytochrome P-450cam: A Study with Unnatural Amino Acids. Biochem. Biophys. Res. Commun. 1995; 208: 96–102
  • Shafiee A., Hutchinson C.R. Macrolide Antibiotic Biosynthesis: Isolation and Properties of Two Forms of 6-Deoxyerythronolide B Hydroxylase from Saccharopolyspora erythraea (Streptomyces erythreus). Biochemistry 1987; 26: 6204–6210
  • Shafiee A., Hutchinson C.R. Purification and Reconstitution of the Electron Transport Components for 6-Deoxyerythronolide B Hydroxylase, a Cytochrome P-450 Enzyme of Macrolide Antibiotic (Erythromycin) Biosynthesis. J. Bacteriol. 1988; 170: 1548–1553
  • Cupp-Vickery J.R., Poulos T.L. Structure of Cytochrome P450eryF Involved in Erythromycin Biosynthesis. Nat. Struct. Biol. 1995; 2: 144–153
  • Cupp-Vickery J.R., Han O., Hutchinson C.R., Poulos T.L. Substrate-Assisted Catalysis in Cytochrome P450eryF. Nat. Struct. Biol. 1996; 3: 632–637
  • Andersen J.F., Tatsuta K., Gunji H., Ishiyama T., Hutchinson C.R. Substrate Specificity of 6-Deoxyerythronolide B Hydroxylase, a Bacteria Cytochrome P450 of Erythromycin A Biosynthesis. Biochemistry 1993; 32: 1905–1913
  • Xiang, H.; Tschirret-Guth, R.A.; de Montellano, P.R.O. An A245T Mutation Conveys the P450eryf to Oxidize Alternative Substrates. 2000, 275, 35999–36006.
  • Ishigooka M., Shimizu T., Hiroya K., Hatano M. Role of Glu318 at the Putative Distal Site in the Catalytic Function of Cytochrome P450d. Biochemistry 1992; 31: 1528–1531
  • Amarneh B., Corbin C.J., Peterson J.A., Simpson E.R., Graham-Lorence S. Functional Domains of Human Aromatase Cytochrome P450 Characterized by Linear Alignment and Site-Directed Mutagenesis. Mol. Endocrinol. 1993; 7: 1617–1624
  • Gerber N.C., Sligar S.G. Catalytic Mechanism of Cytochrome P-450: Evidence for a Distal Charge Relay. J. Am. Chem. Soc. 1992; 114: 8742–8743
  • Benson D.E., Suslick K.S., Sligar S.G. Reduced Oxy Intermediate Observed in D251N Cytochrome P450cam. Biochemistry 1997; 36: 5104–5107
  • Vidakovic M., Sligar S.G., Li H., Poulos T.L. Understanding the Role of the Essential Asp251 in Cytochrome P450cam Using Site-Directed Mutagenesis, Crystallography, and Kinetic Solvent Isotope Effect. Biochemistry 1998; 37: 9211–9219
  • Gerber N.C., Sligar S.G. A Role for Asp-251 in Cytochrome P-450cam Oxygen Activation. J. Biol. Chem. 1994; 269: 4260–4266
  • Aikens J., Sligar S.G. Kinetic Solvent Isotope Effects During Oxygen Activation by Cytochrome P-450cam. J. Am. Chem. Soc. 1994; 116: 1143–1144
  • Schowen R.L. Solvent Isotope Effects on Enzymic Reactions. Isotope Effects on Enzyme-Catalyzed Reactions, W.W. Cleland, M.H. O' Leary, D.B. Northrop. University Park Press, Baltimore 1977; 64–99
  • Turner J.J., Pimentel G.C. Krypton Fluoride: Preparation by the Matrix Isolation Technique. Science 1963; 140: 974–975
  • Symons M.C.R., Petersen R.L. Electron Capture by Oxyhemoglobin: An ESR Study. Proc. R. Soc. London B 1978; 201: 285–300
  • Davydov R.M. Optical and ESR Spectroscopic Studies of Electron Adducts of Oxymyoglobin and Oxyhemoglobin. Biofizika 1980; 25: 203–207
  • Kappl R., Hohn-Berlage M., Huttermann J., Bartlett N., Symons M.C.R. Electron Spin and Electron Nuclear Couble Resonance of the [FeO2]-[Ferrite] Center from Irradiated Oxyhemo- and Oxymyoglobin. Biochim. Biophys. Acta 1985; 827: 327–343
  • Davydov R., Kuprin S., Graslund A., Ehrenberg A. Electron Paramagnetic Resonance Study of the Mixed-Valent Diiron Center in Escherichia coli Ribonucleotide Reductase Produced by Reduction of Radical-Free Protein R2 at 77K. J. Am. Chem. Soc. 1994; 116: 11120–11128
  • Davydov R., Kappl R., Hutterman R., Peterson J.A. EPR-Spectroscopy of Reduced Oxyferrous-P450cam. FEBS Lett. 1991; 295: 113–115
  • Davydov R., Macdonald I.D.G., Makris T.M., Sligar S.G., Hoffman B.M. EPR and ENDOR of Catalytic Intermediates in Cryoreduced Native and Mutant Oxy-Cytochromes P450cam: Mutation-Induced Changes in the Proton Delivery System. J. Am. Chem. Soc. 1999; 121: 10654–10655
  • Burstyn J.N., Roe J.A., Miksztal A.R., Shaevitz B.A., Lang G., Valentine J.S. Magnetic and Spectroscopic Characterization of an Iron Porphyrin Peroxide Complex. Peroxoferrioctaethylporphyrin(1-). J. Am. Chem. Soc. 1988; 110: 1382–1388
  • Hoffman B.M., Diemente D.L., Basolo F. Electron Paramagnetic Resonance Studies of Some Cobalt(II) Schiff Base Compounds and Their Monomeric Oxygen Adducts. J. Am. Chem. Soc. 1970; 92: 61–65
  • Davydov R., Makris T.M., Kofman V., Werst D.E., Sligar S.G., Hoffman B.M. Hydroxylation of Camphor by Reduced Oxy-Cytochrome P450cam: Mechanistic Implications of EPR and ENDOR Studies of Catalytic Intermediates in Native and Mutant Enzymes. J. Am. Chem. Soc. 2001; 123: 1403–1415
  • Lipscomb J.D. Electron Paramagnetic Resonance Detectable States of Cytochrome P-450cam. Biochemistry 1980; 19: 3590–3599
  • White R.E., McCarthy M.B., Egeberg K.D., Sligar S.G. Regioselectivity in the Cytochromes P-450: Control by Protein Constraints and by Chemical Reactivities. Arch. Biochem. Biophys. 1984; 228: 493–502
  • Newcomb M., Shen R., Choi S.Y., Toy P.H., Hollenberg P.F., Vaz A.D.N., Coon M.J. Cytochrome P450-Catalyzed Hydroxylation of Mechanistic Probes That Distinguish Between Radicals and Cations. Evidence for Cationic But Not for Radical Intermediates. J. Am. Chem. Soc. 2000; 122: 2677–2686
  • Pratt J.M., Ridd T.I., King L.J. Activation of H2O2 by P450: Evidence That the Hydroxylating Intermediate Is Iron(III)-Coordinated H2O2 and Not the Ferryl FeO3+ Complex. J. Chem. Soc., Chem. Commun. 1995; 22: 2297–2298
  • Denisov, I.G.; Makris, T.M.; Sligar, S.G. Methods in Enzymology. In press.
  • Denisov I.G., Makris T.M., Sligar S.G. Cryotrapped Reaction Intermediates of Cytochrome P450 Studied by Radiolytic Reduction with Phosphorus-32. J. Biol. Chem. 2001; 276: 11648–11652
  • Harris D., Loew G., Waskell L. Structure and Spectra of Ferrous Dioxygen and Reduced Ferrous Dioxygen Model Cytochrome P450. J. Am. Chem. Soc. 1998; 120: 4308–4318
  • Kobayashi K., Amano M., Kanbara Y., Hayashi K. One-Electron Reduction of the Oxyform of 2,4-Diacetyldeuterocytochrome P-450cam. J. Biol. Chem. 1987; 262: 5445–5447
  • Schlichting I., Berendzen J., Chu K., Stock A.M., Maves S.A., Benson D.E., Sweet R.M., Ringe D., Petsko G.A., Sligar S.G. The Catalytic Pathway of Cytochrome P450cam at Atomic Resolution. Science 2000; 287: 1615–1622
  • Yeom H., Sligar S.G. Oxygen Activation by Cytochrome P450BM-3: Effects of Mutating an Active Site Acidic Residue. Arch. Biochem. Biophys. 1997; 337: 209–216

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.