Reactions of heme proteins with carbonate radical anion

Research on Chemical Intermediates

Volumn 35, Issue 4, 2009, Pages 401-409

  Gebicka, L ^a   Didik, J ^a   Gebicki, J L ^a  

^a LODZ UNIVERSITY OF TECHNOLOGY   (Poland)

Author keywords

Carbonate radical anion; Catalase; Cytochrome c; Horseradish peroxidase; Radiolysis

Indexed keywords

AMINO ACID RESIDUES; CARBONATE RADICAL ANION; CYTOCHROME C; HEME IRON; HEME PROTEINS; HORSE-RADISH PEROXIDASE; PULSE RADIOLYSIS METHOD;

AMINO ACIDS; CARBONATION; HEMOGLOBIN; IONS; ORGANIC ACIDS; PETROLEUM TAR; PORPHYRINS; RADIATION CHEMISTRY; RATE CONSTANTS;

RADIOLYSIS;

EID: 70349415929     PISSN: 09226168     EISSN: 15685675     Source Type: Journal    
DOI: 10.1007/s11164-009-0042-8     Document Type: Article

References (33)

1. D.B. Medinas, G. Cerchiaro, D.F. Trindade, O. Augusto, The carbonate radical and related oxidants derived from bicarbonate buffer. IUBMB Life 59, 255-262 (2007)
2. O. Augusto, M.G. Bonini, A.M. Amanso, E. Linares, C.C.X. Santos, S.L. De Menezes, Nitrogen dioxide and carbonate radical anion: two emerging radicals in biology. Free Radic. Biol. Med. 32, 841-859 (2002)
3. 2. J. Biol. Chem. 277, 34674-34678 (2002)
4. H. Zhang, C. Andrekopoulos, J. Joseph, K. Chandran, H. Karoui, J.P. Crow, B. Kalyanaraman, Bicarbonate-dependent peroxidase activity of human Cu,Zn-superoxide dismutase induces covalent aggregation of protein: intermediacy of tryptophan-derived oxidation products. J. Biol. Chem. 278, 24078-24089 (2003)
5. 2. Proc. Natl. Acad. Sci. USA 101, 743-744 (2004)
6. M.G. Bonini, D.C. Fernandes, O. Augusto, Albumin oxidation to diverse radicals by the peroxidase activity of Cu,Zn-superoxide dismutase in the presence of bicarbonate or nitrite: diffusible radicals produce cysteinyl and solvent-exposed and -unexposed tyrosyl radicals. Biochemistry 42, 344-351 (2004)
7. M.G. Bonini, S. Miyamoto, P. Di Mascio, O. Augusto, Production of the carbonate radical anion during xanthine oxidase turnover in the presence of bicarbonate. J. Biol. Chem. 279, 51836-51843 (2004)
8. A.S. Domazou, W.H. Koppenol, Oxidation-state-dependent reactions of cytochrome c with the trioxidocarbonate(•1-) radical: a pulse radiolysis study. J. Biol. Inorg. Chem. 12, 118-125 (2007)
9. F. Boccini, A.S. Domazou, S. Herold, Pulse radiolysis studies of the reactions of carbonate radical anion with myoglobin and hemoglobin. J. Phys. Chem. A 108, 5800-5805 (2004)
10. S. Goldstein, A. Samuni, Intra- and intermolecular oxidation of oxymyoglobin and oxyhemoglobin induced by hydroxyl and carbonate radicals. Free Radic. Biol. Med. 39, 511-519 (2005)
11. L. Gebicka, J. Didik, Mechanism of peroxynitrite interaction with cytochrome c. Acta Biochim. Pol. 50, 815-823 (2003)
12. T. Samejima, J.T. Yang, Reconstitution of acid-denatured catalase. J. Biol. Chem. 238, 3256-3261 (1963)
13. 2O. Biochemistry 32, 11878-11885 (1993)
14. P.J. Ohlsson, K.G. Paul, The molar absorptivity of horseradish peroxidase. Acta Chem. Scand. B 30, 373-375 (1976)
15. R.F. Beers Jr., I.W. Sizer, A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase. J. Biol. Chem. 195, 133-140 (1952)
16. R.E. Childs, W.G. Bardsley, The steady-state kinetics of peroxidase with 2,20-azino-di-(3-ethylbenzthiazoline- 6-sulphonic acid) as chromogen. Biochem. J. 145, 93-103 (1975)
17. -) in aqueous solution. J. Phys. Chem. Ref. Data 17, 513-886 (1988)
18. S. Prajapati, V. Bhakuni, K.R. Babu, S.K. Jain, Alkaline unfolding and salt-induced folding of bovine liver catalase at high pH. Eur. J. Biochem. 255, 178-184 (1998)
19. J.L. Weeks, J. Rabani, D. Behar, The pulse radiolysis of deaerated aqueous carbonate solutions I. Transient optical spectrum and mechanism. II. pK for OH radicals. J. Phys. Chem. 70, 2100-2106 (1966)
20. N.C. Veith, A.T. Smith, Horseradish peroxidase. Adv. Inorg. Chem. 51, 107-162 (2001)
21. B. Chance, H. Sies, A. Boveris, Hydroperoxide metabolism in mammalian organs. Physiol. Rev. 59, 527-605 (1979)
22. P. Neta, R.E. Huie, A.B. Ross, Rate constants for reactions of inorganic radicals in aqueous solution. J Phys. Chem. Ref. Data 17, 1027-1284 (1988)
23. I. Hamachi, A. Fujita, T. Kunitake, Enhanced N-demethylase activity of cytochrome c bound to a phosphate-bearing synthetic bilayer membrane. J. Am. Chem. Soc. 116, 8811-8812 (1994)
24. L. Gebicka, Peroxidase-like activity of cytochrome c in the presence of anionic surfactants. Res. Chem. Intermed. 27, 717-723 (2001)
25. R.E.M. Diederix, M. Ubbink, G.W. Canters, Peroxidase activity as a tool for studying the folding of c-type cytochromes. Biochemistry 41, 13067-13077 (2002)
26. Y.-R. Chen, L.J. Deterding, B.E. Sturgeon, K.B. Tomer, R.P. Mason, Protein oxidation of cytochrome c by reactive halogen species enhances its peroxidase activity. J. Biol. Chem. 277, 29781-29791 (2002)
27. M.G. Simic, I.A. Taub, Mechanisms of inter- and intra-molecular electron transfer in cytochromes. Faraday Discuss. Chem. Soc. 63, 270-278 (1977)
28. L. Gebicka, J.L. Gebicki, Pulse radiolysis of catalase in solution-II. Reactions of primary products from water radiolysis with catalase. Radiat. Phys. Chem. 36, 161-163 (1990)
29. L. Gebicka, J.L. Gebicki, Redox transformations in peroxidases studied by pulse radiolysis technique. Radiat. Phys. Chem. 39, 113-116 (1992)
30. R. Joshi, T. Mukherjee, Carbonate radical anion-induced electron transfer in bovine serum albumin. Radiat. Phys. Chem. 75, 760-767 (2006)
31. E. Margoliash, E.L. Smith, G. Kreil, H. Tuppy, Amino acid sequence of horse heart cytochrome c. The complete amino-acid sequence. Nature 192, 1125-1127 (1961)
32. K.G. Welinder, Amino acid sequence studies of horseradish peroxidase. Amino and carboxyl termini, cyanogen bromide and tryptic fragments, the complete sequence, and some structural characteristics of horseradish peroxidase c. Eur. J. Biochem. 96, 483-502 (1979)
33. M.R.N. Murthy, T.J. Reid III, A. Sicignano, N. Tanaka, M.G. Rossmann, Structure of beef liver catalase. J. Mol. Biol. 152, 465-499 (1981)