Collect. Czech. Chem. Commun.
2006, 71, 1588-1610
https://doi.org/10.1135/cccc20061588
A Kinetic Study of the Cytochrome c-Hydrogen Peroxide Reaction
Joaquin F. Perez-Benito
Departamento de Quimica Fisica, Facultad de Quimica, Universidad de Barcelona, Marti i Franques, 1, 08028 Barcelona, Spain
References
1. Science 1996, 273, 59.
< R. S., Weindruch R.: https://doi.org/10.1126/science.273.5271.59>
2. Inorg. Chem. 1993, 32, 3162.
< A. M., Espenson J. H., Bakac A.: https://doi.org/10.1021/ic00066a030>
3. J. Am. Chem. Soc. 2000, 122, 10714.
< E., Holland P. L., Tolman W. B., Romesberg F. E., Schultz P. G.: https://doi.org/10.1021/ja0025806>
4. Free Radical Biol. Med. 1996, 20, 553.
< S.: https://doi.org/10.1016/0891-5849(95)02111-6>
5. Proc. Natl. Acad. Sci. U.S.A. 1975, 72, 140.
< C., Partch R. E., Weil T.: https://doi.org/10.1073/pnas.72.1.140>
6. Acc. Chem. Res. 1999, 32, 547.
< S., Meyerstein D.: https://doi.org/10.1021/ar9800789>
7. Acc. Chem. Res. 1996, 29, 409.
< D. T., Sobkowiak A., Matsushita T.: https://doi.org/10.1021/ar950031c>
8. Eur. J. Inorg. Chem. 2005, 2875.
< S., Masarwa A., Meyerstein N., Meyerstein D.: https://doi.org/10.1002/ejic.200500097>
9. J. Phys. Chem. A 2004, 108, 4853.
< J. F.: https://doi.org/10.1021/jp031339l>
10. Biochem. Biophys. Res. Commun. 1995, 216, 483.
< H., Takatori T., Aono K., Iwadate K., Takahashi M., Nakajima M., Nagao M.: https://doi.org/10.1006/bbrc.1995.2648>
11. Cell. Mol. Life Sci. 2001, 58, 485.
< K., Ikeda K., Kuroi R., Hashimoto R., Tokumaru S., Kojo S.: https://doi.org/10.1007/PL00000872>
12. BioFactors 1998, 8, 195.
< G., Cavazzoni M., Genova M. L., D’Aurelio M., Pich M. M., Pallotti F., Formiggini G., Marchetti M., Castelli G. P., Bovina C.: https://doi.org/10.1002/biof.5520080305>
13. Agents Actions 1991, 34, 393.
< E., Uhrich S., Bethke P.: https://doi.org/10.1007/BF01988734>
14. Arch. Biochem. Biophys. 1993, 306, 70.
< N., Shah M. M., Grover T. A., Aust S. D.: https://doi.org/10.1006/abbi.1993.1482>
15. Chem. Biol. 2000, 7, 237.
< J. A., Mauk A. G., Vazquez-Duhalt R.: https://doi.org/10.1016/S1074-5521(00)00098-3>
16. FEBS Lett. 1988, 227, 43.
< J. F., McCord J. M.: https://doi.org/10.1016/0014-5793(88)81410-8>
17. Biochemistry 2005, 44, 8652.
< S., Chevance S., Bouyer P., Garnier L., Montillet J. L., Bondon A., Berthornieu C.: https://doi.org/10.1021/bi050322l>
18. Free Radical Biol. Med. 2004, 37, 1963.
< V. E., Borisenko G. G., Tyurina Y. Y., Tyurin V. A., Jiang J., Potapovich A. I., Kini V., Amoscato A. A., Fujii Y.: https://doi.org/10.1016/j.freeradbiomed.2004.08.016>
19. Biochem. J. 1959, 71, 570.
< E., Frohwirt N.: https://doi.org/10.1042/bj0710570>
20. Eur. J. Biochem. 1971, 22, 5.
< C., Wilson M. T.: https://doi.org/10.1111/j.1432-1033.1971.tb01507.x>
21. Eur. J. Biochem. 1971, 22, 11.
< M. T., Greenwood C.: https://doi.org/10.1111/j.1432-1033.1971.tb01508.x>
22. Biochem. J. 1987, 243, 379.
< A. J., Brittain T.: https://doi.org/10.1042/bj2430379>
23. J. Colloid Interface Sci. 1992, 152, 70.
< J. F., Arias C.: https://doi.org/10.1016/0021-9797(92)90009-B>
24. Barrow G. M.: Physical Chemistry, p. 803. McGraw–Hill, New York 1966.
25. J. Inorg. Biochem. 2004, 98, 430.
< J. F.: https://doi.org/10.1016/j.jinorgbio.2003.10.025>
26. J. Biochem. 1995, 117, 780.
< M., Nakamura M., Suzuki T., Kawai K., Horitsu H., Takamizawa K.: https://doi.org/10.1093/oxfordjournals.jbchem.a124776>
27. Acc. Chem. Res. 1981, 14, 393.
< D. T., Valentine J. S.: https://doi.org/10.1021/ar00072a005>
28. Biochim. Biophys. Acta 1988, 967, 267.
< T., Matsugo S.: https://doi.org/10.1016/0304-4165(88)90019-0>
29. J. Biol. Chem. 1966, 241, 4180.
K. G., Parks P. C., Czerlinski G. H., Hess G. P.:
30. Gazz. Chim. Ital. 1991, 121, 139.
J. F., Arias C., Brillas E.:
31. J. Biochem. Biophys. Methods 1994, 28, 205.
< M. L., Scarpa M., Rigo A.: https://doi.org/10.1016/0165-022X(94)90017-5>
32. Biochem. Biophys. Res. Commun. 1991, 181, 197.
F., Hultquist E. D.:
33. Prog. Inorg. Chem. 1995, 43, 267.
< A.: https://doi.org/10.1002/9780470166444.ch3>
34. Biochim. Biophys. Acta 1978, 503, 1.
< J. W., Raap A., Koppenol W. H., Nauta H.: https://doi.org/10.1016/0005-2728(78)90157-3>
35. Biochim. Biophys. Acta 1976, 449, 157.
< W. H., Van Buuren K. J. H., Butler J., Braams R.: https://doi.org/10.1016/0005-2728(76)90130-4>
36. J. Biol. Chem. 1982, 257, 10747.
J., Koppenol W. H., Margoliash E.:
37. Biochim. Biophys. Acta 1993, 1161, 73.
< J., Hoey B. M.: https://doi.org/10.1016/0167-4838(93)90198-Z>
38. Bull. Chem. Soc. Jpn. 1994, 67, 529.
< K., Hiramatsu M., Ohya-Nishiguchi H., Kamada H., Fujii K.: https://doi.org/10.1246/bcsj.67.529>
39. J. Biol. Chem. 1982, 257, 4426.
W. H., Margoliash E.:
40. J. Biol. Chem. 1988, 263, 11652.
D., Wilson G. S., Earl R. A., Cusanovich M. A.:
41. J. Biol. Inorg. Chem. 2003, 8, 527.
< S. G., Mabrouk P. A.: https://doi.org/10.1007/s00775-002-0437-0>
42. Isr. J. Chem. 1984, 24, 11.
< W. H., Butler J.: https://doi.org/10.1002/ijch.198400002>
43. Free Radical Biol. Med. 1985, 1, 281.
< W. H.: https://doi.org/10.1016/0748-5514(85)90132-1>
44. Isr. J. Chem. 1972, 10, 1011.
< K.: https://doi.org/10.1002/ijch.197200111>
45. Coetzee J. F., Ritchie C. D.: Solute–Solvent Interactions, p. 20. Dekker, New York 1969.
46. Int. J. Biochem. 1985, 17, 119.
< J. P., Carrier T. L.: https://doi.org/10.1016/0020-711X(85)90095-3>
47. Eur. J. Biochem. 1973, 32 , 492.
< R., Schejter A.: https://doi.org/10.1111/j.1432-1033.1973.tb02633.x>
48. Photochem. Photobiol. 1994, 60, 415.
< S., Kayamori-Sato N., Konishi T.: https://doi.org/10.1111/j.1751-1097.1994.tb05126.x>
49. J. Inorg. Biochem. 1987, 31, 133.
< M. M., Lakshmaiah N.: https://doi.org/10.1016/0162-0134(87)80058-2>
50. Monatsh. Chem. 2001, 132, 1477.
< J. F.: https://doi.org/10.1007/s007060170004>
51. Arch. Biochem. Biophys. 2001, 389, 110.
< W. A., Kissner R., Nauser T., Koppenol W. H.: https://doi.org/10.1006/abbi.2001.2321>
52. Can. J. Chem. 1982, 60, 848.
< Y., Tanaka K.: https://doi.org/10.1139/v82-128>
53. Electrochim. Acta 1999, 44, 3341.
< E., Luciano P., Nitsche S., Bianco P.: https://doi.org/10.1016/S0013-4686(99)00053-5>
54. Bard A. J.: Encyclopedia of Electrochemistry of the Elements, Vol. IX, Part B, p. 263. Marcel Dekker, New York 1986.
55. New J. Chem. 1999, 23, 945.
< J. F., Arias C.: https://doi.org/10.1039/a903797g>
56. Weast R. C.: Handbook of Chemistry and Physics, p. D-141. CRC Press, Cleveland 1977.
57. J. Phys. Chem. A 1997, 101, 4726.
< J. F., Arias C.: https://doi.org/10.1021/jp963868d>
58. Anal. Biochem. 1987, 160, 184.
< D., Kruppa J.: https://doi.org/10.1016/0003-2697(87)90629-4>
59. J. Chem. Soc., Faraday Trans. 1990, 86, 1539.
< A. J., McCracken D. R., Buxton G. V., Wood N. D.: https://doi.org/10.1039/ft9908601539>
60. Free Radical Res. 1994, 20, 345.
< M. J., Jung L., Tanielian C., Mechin R.: https://doi.org/10.3109/10715769409145635>
61. Chem. Pharm. Bull. 1993, 41, 1842.
< N., Saito Y.: https://doi.org/10.1248/cpb.41.1842>
62. J. Phys. Chem. Ref. Data 1988, 17, 513.
< G. V., Greenstock C. L., Helman W. P., Ross A. B.: https://doi.org/10.1063/1.555805>
63. Biochem. Pharmacol. 1988, 37, 4574.
< E., Vegh M., Kramer M., Horvath I.: https://doi.org/10.1016/0006-2952(88)90675-2>
64. Anal. Chem. 1997, 69, 4295.
< B., Gutierrez P. L., Blough N. V.: https://doi.org/10.1021/ac970622b>