The structure of heme proteins compounds I and II: Some misconceptions

Free Radical Biology and Medicine

Volumn 24, Issue 7-8, 1998, Pages 1338-1346

  Everse, Johannes ^a  

^a TEXAS TECH UNIVERSITY HEALTH SCIENCES CENTER SCHOOL OF MEDICINE   (United States)

Author keywords

Compound I; Compound II; Cytochrome P450; Enzyme mechanisms; Free radical; Heme proteins; Oxo ferryl bond; Peroxidases

Indexed keywords

FREE RADICAL; HEME; HEMOPROTEIN; PEROXIDASE;

CHEMICAL BOND; CHEMICAL MODIFICATION; CHEMICAL REACTION; CHEMICAL STRUCTURE; ELECTRICITY; ENZYME MECHANISM; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PROTEIN STRUCTURE; REVIEW;

ARMORACIA RUSTICANA;

EID: 0032076871     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0891-5849(97)00451-6     Document Type: Review

References (64)

1. Ortiz de Montellano P. R., Catalano C. E. Epoxidation of styrene by hemoglobin and myoglobin. Transfer of oxygen equivalents to the protein surface. J. Biol. Chem. 260:1985;9265-9271.
2. 2-mediated cross-linking of sperm whale myoglobin . J. Biol. Chem. 263:1988;17880-17886.
3. Davies M. J. Identification of a globin free radical in equine myoglobin treated with peroxides. Biochim. Biophys. Acta. 1077:1991;86-90.
4. McArthur K. M., Davies M. J. Detection and reactions of the globin radical in haemoglobin. Biochim. Biophys. Acta. 1202:1993;173-181.
5. Grisham M. B. Myoglobin-catalyzed hydrogen peroxide dependent arachidonic acid peroxidation. J. Free Rad. Biol. Med. 1:1985;227-232.
6. Kobayashi S., Nakano M., Kimura T., Schaap A. P. On the mechanism of the peroxidase-catalyzed oxygen transfer reaction. Biochemistry. 26:1987;5019-5022.
7. Guengerich F. P., Macdonald T. L. Mechanisms of cytochrome P-450 catalysis. FASEB J. 4:1990;2453-2459.
8. 2 activated metmyoglobin. Lipids. 20:1985;625-628.
9. Kanner J., Harel S. Initiation of membranal lipid peroxidation by activated metmyoglobin and methemoglobin. Arch. Biochem. Biophys. 237:1985;314-321.
10. Cashon R. E., Alayash A. I. Reaction of human hemoglobin HbAo and two cross-linked derivatives with hydrogen peroxide Differential behavior of the ferryl intermediate . Arch. Biochem. Biophys. 316:1995;461-469.
11. Gorbunov N. V., Osipov A. N., Day B. W., Zayas-Rivera B., Kagan V. E., Elsayed N. M. Reduction of ferrylmyoglobin and ferrylhemoglobin by nitric oxide a protective mechanism against hemoprotein-induced oxidations . Biochemistry. 34:1995;6689-6699.
12. Cadenas E. Thiyl radical formation during thiol oxidation by ferrylmyoglobin. Meth. Enzymol. 251:1995;106-120.
13. Laranjinha J., Almeida L., Madeira V. Reduction of ferrylmyoglobin by dietary phenolic acid derivatives of cinnamic acid. Free Rad. Biol. Med. 19:1995;329-337.
14. Everse J., Hsia N. The toxicities of native and modified hemoglobins. Free Rad. Biol. Med. 22:1997;1075-1099.
15. Ortiz de Montellano P. R. Cytochrome P450; Structure, Mechanism, and Biochemistry. 2nd ed. 1995;Plenum Press, New York.
16. Pauling L. C. The Nature of the Chemical Bond. 3rd ed. 1960;Cornell University Press, Ithaca, NY.
17. Sawyer, D. T. Oxygen Chemistry, New York: Oxford University Press; 1991: Chapter 3.
18. Peisach J., Blumberg W. E., Wittenberg B. A., Wittenberg J. B. Electronic structure of protoheme proteins. III. configuration of the heme and its ligands. J. Biol. Chem. 243:1968;1871-1880.
19. Dolphin D., Forman A., Borg D. C., Fajer J., Felton R. H. Compounds I of catalase and horseradish peroxidase π cation radicals . Proc. Natl. Acad. Sci. USA. 68:1971;614-618.
20. Dolphin D., Felton R. H. Biochemical significance of porphyrin π cation radicals. Acc. Chem. Res. 7:1974;26-32.
21. LaMar G., De Ropp J. S., Smith K. M., Langry K. C. Proton nuclear magnetic resonance investigation of the electronic structure of Compound I of horseradish peroxidase. J. Biol. Chem. 256:1981;237-243.
22. Roberts J. E., Hoffman B. M., Rutter R., Hager L. P. Electron-nuclear double resonance of horseradish peroxidase Compound I. J. Biol. Chem. 256:1981;2118-2121.
23. 17O ENDOR of horseradish peroxidase Compound I. J. Am. Chem. Soc. 103:1981;7654-7656.
24. Bosshard H. R., Anni H., Yonetani T. Yeast cytochrome C peroxidase. Everse J., Everse K. E., Grisham M. B. Peroxidases in Chemistry and Biology. Vol. II:1991;51-84 CRC Press, Boca Raton.
25. 2 compounds by ferrocyanide indirect evidence of an apoprotein site for one of the two oxidizing equivalents . Biochem. Biophys. Res. Commun. 121:1984;463-470.
26. CAM from Pseudomonas putida. J. Am. Chem. Soc. 100:1978;3743-3751.
27. CAM. J. Am. Chem. Soc. 104:1982;5469-5472.
28. Karthein R., Dietz R., Nastainczyk W., Ruf H. H. Higher oxidation states of prostaglandin H synthase. EPR study of a transient tyrosyl radical in the enzyme during the peroxidase reaction. Eur. J. Biochem. 171:1988;313-320.
29. 2. Eur. J. Biochem. 171:1988;321-328.
30. Penner-Hahn J. E., Eble K. S., McMurry T. J., Renner M., Balch A. L., Groves J. T., Dawson J. H., Hodgson K. O. Structural characterization of horseradish peroxidase using EXAFS spectroscopy. Evidence for a FeO ligation in Compounds I and II. J. Am. Chem. Soc. 108:1986;7819-7825.
31. Chance M., Powers L., Poulos T., Chance B. Cytochrome c peroxidase compound ES is identical with horseradish peroxidase compound I in iron-ligand distances. Biochemistry. 25:1986;1266-1270.
32. Chance M., Powers L., Kumar C., Chance B. X-ray absorption studies of myoglobin peroxide reveal functional differences between globins and heme enzymes. Biochemistry. 25:1986;1259-1265.
33. Chance B., Powers L., Ching Y., Poulos T., Schonbaum G. R., Yamazaki I., Paul K. G. X-ray absorption studies of intermediates in peroxidase activity. Arch. Biochem. Biophys. 235:1984;596-611.
34. Baek H. K., Van Wart H. E. Elementary steps in the formation of horseradish peroxidase Compound I direct observation of Compound 0, a new intermediate with a hyperporphyrin spectrum . Biochemistry. 28:1989;5714-5719.
35. Baek H. K., Van Wart H. E. Elementary steps in the reaction of horseradish peroxidase with several peroxides kinetics and thermodynamics of formation of Compound 0 and Compound I . J. Am. Chem. Soc. 114:1992;718-725.
36. Schonbaum G. R., Lo S. Interaction of peroxidases with aromatic peracids and alkyl peroxides. J. Biol. Chem. 247:1972;3353-3360.
37. Adediran S. A., Dunford H. B. Structure of horseradish peroxidase Compound I. kinetic evidence for the incorporation of one oxygen atom from the oxidizing substrate into the enzyme. Eur. J. Biochem. 132:1983;147-150.
38. Groves J. T., Haushalter R. C., Nakamura M., Nemo T. E., Evans B. J. High-valent iron-porphyrin complexes related to peroxidase and cytochrome P450. J. Am. Chem. Soc. 103:1981;2884-2886.
39. Groves J. T., Watanabe Y. Oxygen activation by metalloporphyrins related to peroxidase and cytochrome P450. Direct observation of the O - O bond cleavage step. J. Am. Chem. Soc. 108:1986;7834-7836.
40. Traylor, P. S.; Dolphin, D.; Traylor, T. G. Sterically protected hemins with electronegative substituents: efficient catalysts for hydroxylation and epoxidation. J. Chem. Soc., Chem. Commun. 1984:279-280.
41. Traylor T. G., Nakano T., Dunlap B. E., Traylor P. S. Mechanisms of hemin-catalyzed alkene epoxidation. The effect of catalyst on the regiochemistry of epoxidation. J. Am. Chem. Soc. 108:1986;2782-2784.
42. 2 as hydroxylating agents in steroid hydroxylation reactions catalyzed by partially purified cytochrome P450. Biochem. Biophys. Res. Commun. 66:1975;209-216.
43. Hrycay E. G., Gustaffson J. A., Ingelman-Sundberg M., Ernster L. The involvement of cytochrome P450 in hepatic microsomal steroid hydroxylation reactions supported by sodium periodate, sodium chlorite, and organic peroxides. Eur. J. Biochem. 61:1976;43-52.
44. 4 to support microsomal hydroxylations in biosynthesis and metabolism of bile acids. FEBS Lett. 66:1976;299-302.
45. Gustafsson J. A., Hrycay E. G., Ernster L. Sodium periodate, sodium chlorite, and organic peroxides as hydroxylating agents in steroid hydroxylation reactions catalyzed by adrenocortical microsomal and mitochondrial cytochrome P450. Arch. Biochem. Biophys. 174:1976;440-453.
46. Calderwood T. S., Bruice T. C. Electrochemical generation of iron(IV)-oxo porphyrins and iron(IV)-oxo porphyrin π-cation radicals. Inorg. Chem. 25:1986;3722-3724.
47. Calderwood T. S., Lee W. A., Bruice T. C. Spectral and electrochemical identification of iron(IV)-oxo porphyrin and iron(IV)-oxo porphyrin π-cation species. J. Am. Chem. Soc. 107:1985;8272-8273.
48. III chloride. J. Am. Chem. Soc. 108:1986;1636-1643.
49. Collman J. P., Kodadek T., Brauman J. I. Oxygenation of styrene by cytochrome P450 model systems a mechanistic study . J. Am. Chem. Soc. 108:1986;2588-2594.
50. Ortiz de Montellano P. R. Oxygen activation and reactivity. Ortiz de Montellano P. R. Cytochrome P450. Structure, Mechanism, and Biochemistry. 1995;245-303 Plenum Press, New York.
51. Sugimoto H., Tung H-C., Sawyer D. T. Formation, characterization, and reactivity of the oxene adduct of [tetrakis(2,6-dichlorophenyl)porphinato]iron(III) perchlorate in acetonitrile. Model for the reactive intermediate of cytochrome P-450. J. Am. Chem. Soc. 110:1988;2465-2470.
52. Pauling L., Coryell C. D. The magnetic properties and structure of hemoglobin, oxyhemoglobin and carbonmonoxyhemoglobin. Proc. Natl. Acad. Sci. USA. 22:1936;210-216.
53. Pauling, L. Haemoglobin. London: Butterworths Scientific Publications; 1949; 57-65.
54. Griffith J. S. The magnetic properties of some hemoglobin complexes. Proc. Roy. Soc. Ser. A. 235:1956;23-36.
55. Weiss J. J. Nature of the iron-oxygen bond in oxyhaemoglobin. Nature. 202:1964;83-84.
56. Gray H. B. Structural models for iron and copper proteins based on spectroscopic and magnetic properties. Adv. Chem. Ser. 100:1971;365-389.
57. 2 to heme in oxyhemoglobin. Proc. Natl. Acad. Sci. USA. 72:1975;2335-2339.
58. Sadrzadeh S. M. H., Graf E., Panter S. S., Hallaway P. E., Eaton J. W. Hemoglobin a biologic Fenton reagent . J. Biol. Chem. 259:1984;14354-14356.
59. Gutteridge J. M. C. Iron promotors of the Fenton reaction and lipid peroxidation can be released from haemoglobin by peroxides. FEBS Lett. 201:1986;291-295.
60. Faassen A. E., Sundby S. R., Panter S. S., Condie P. M., Hedlund B. E. Hemoglobin; a lifesaver and an oxidant; how to tip the balance. Biomat. Art. Cells Art. Org. 16:1988;93-108.
61. Alayash A. I., Fratantoni J. C., Bonaventura C., Bonaventura J., Bucci E. Consequences of chemical modifications on the free radical reactions of human hemoglobin. Arch. Biochem. Biophys. 298:1992;114-120.
62. Marnett L. J., Kennedy T. A. Comparison of the peroxidase activity of hemoproteins and cytochrome P450. Ortiz de Montellano P. R. Cytochrome P450. Structure, Mechanism, and Biochemistry. 1995;49-80 Plenum Press, New York.
63. IVO group in ferryl myoglobin and Compound II of horseradish peroxidase . J. Am. Chem. Soc. 105:1983;782-787.
64. IVO stretching vibration of Compound II. Biochim. Biophys. Acta. 828:1985;73-80.