Bulletin of the Korean Chemical Society

Korean Chemical Society (대한화학회)
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Peroxidase Activity of Cytochrome c

  • Kim, Nam-Hoon (Department of Genetic Engineering, Cheongju University) ;
  • Jeong, Moon-Sik (Department of Genetic Engineering, Cheongju University) ;
  • Choi, Soo-Young (Department of Genetic Engineering, Division of Life Sciences, Hallym University) ;
  • Kang, Jung-Hoon (Department of Genetic Engineering, Cheongju University)
  • Published : 2004.12.20
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Abstract

The peroxidase activity of cytochrome c was studied by using a chromogen, 2,2'-azinobis-(2-ethylbenzthiazoline-6-sulfonate) (ABTS). Initial rate of ABTS oxidation formation was linear with respect to the concentration of cytochrome c between 2.5-10 ${\mu}$M and $H_2O_2$ between 0.1-0.5 mM. The optimal pH for the peroxidase activity of cytochrome c was 7.0-8.5. The peroxidase activity retained about 40% of the maximum activity when exposed at 60 $^{\circ}C$. for 10 min. The peroxidase activity showed a typical Michaelis-Menten kinetics for $H_2O_2$ which Km value was 29.6 mM. Radical scavengers inhibited the peroxidase activity of cytochrome c. The peroxidase activity was significantly inhibited by the low concentration of iron chelator, deferoxamine. The results suggested that the peroxidase activity was associated with iron in the heme of cytochrome c.

Keywords

References

  1. Moore, G. R.; Pettigrew, G. W. Cytochrome c: Evolution,Structure, and Physicochemical Aspects; Springer-Verlag: Berlin,1990.
  2. Dumont, M. E.; Cardillo, T. S.; Hayes, M. K.; Sherman, F. Mol.Cell Biol. 1991, 11, 5487.
  3. Liu, X.; Kim, C. N.; Yan, J.; Jemmerson, R.; Wang, X. Cell 1996,86, 147. https://doi.org/10.1016/S0092-8674(00)80085-9
  4. Olteanu, A.; Patel, C. N.; Demon, M. M.; Kennedy, S.; Linhoff,M. W.; Minder, C. M.; Potts, P. R.; Deshmukh, M.; Pielak, G. J. Biochem. Biophys. Res. Commun. 2003, 312, 733. https://doi.org/10.1016/j.bbrc.2003.10.182
  5. Hashimoto, M.; Takeda, A.; Hsu, L. J.; Takenouchi, T.; Masliah,E. J. Biol. Chem. 1999, 274, 28849. https://doi.org/10.1074/jbc.274.41.28849
  6. Radi, R.; Thomson, L.; Rubbo, H.; Prodanov, E. Arch. Biochem.Biophys. 1991, 288, 112. https://doi.org/10.1016/0003-9861(91)90171-E
  7. Radi, R.; Sims, S.; Cassina, A.; Turrens, J. F. Free Rad. Biol. Med.1993, 15, 653. https://doi.org/10.1016/0891-5849(93)90169-U
  8. Lawrence, A.; Jomes, C. M.; Wardman, P.; Burkitt, M. J. J. Biol.Chem. 2003, 278, 29410. https://doi.org/10.1074/jbc.M300054200
  9. Rush, J. D.; Koppenol, W. H. J. Am. Chem. Soc. 1988, 110, 4957. https://doi.org/10.1021/ja00223a013
  10. Childs, R. E.; Bardsley, W. G. Biochem. J. 1975, 145, 93.
  11. Wolfenden, B. S.; Wilson, R. L. J. Chem. Soc. Perkin Trans. 1982,II, 805.
  12. Prasad, S.; Maiti, N. C.; Mazumdar, S.; Mitra, S. Biochim. Biophys.Acta 2002, 1596, 63. https://doi.org/10.1016/S0167-4838(02)00205-4
  13. Boveries, A.; Oshino, N.; Chance, B. Biochem. J. 1972, 128, 617.
  14. Yim, M. B.; Chock, P. B.; Stadtman, E. R. J. Biol. Chem. 1993,268, 4099.
  15. Kang, J. H. Bull. Korean Chem. Soc. 2004, 25, 625. https://doi.org/10.5012/bkcs.2004.25.5.625
  16. Kamp, D. W.; Graceffa, P.; Pryor, W. A.; Weitzmn, S. A. FreeRadic. Biol. Med. 1992, 12, 293. https://doi.org/10.1016/0891-5849(92)90117-Y
  17. DeBore, D. A.; Clark, R. E. Ann. Thorac. Surg. 1992, 53, 412. https://doi.org/10.1016/0003-4975(92)90260-B
  18. Lee, C. T.; Liao, S. C.; Hsu, K. T.; Lam, K. K.; Chen, J. B. Ren.Fail. 1999, 21, 665. https://doi.org/10.3109/08860229909094160

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