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Oxidative Modification of Cytochrome c by Hydrogen Peroxide  

Kim, Nam Hoon (Department of Genetic Engineering, Cheongju University)
Jeong, Moon Sik (Department of Genetic Engineering, Cheongju University)
Choi, Soo Young (Department of Biomedical Science, Division of Life Sciences, Hallym University)
Kang, Jung Hoon (Department of Genetic Engineering, Cheongju University)
Publication Information
Molecules and Cells / v.22, no.2, 2006 , pp. 220-227 More about this Journal
Abstract
Oxidative alteration of mitochondrial cytochrome c has been linked to disease and is one of the causes of proapoptotic events. We have investigated the modification of cytochrome c by $H_2O_2$. When cytochrome c was incubated with $H_2O_2$, oligomerization of the protein increased and the formation of carbonyl derivatives and dityrosine was stimulated. Radical scavengers prevented these effects suggesting that free radicals are implicated in the $H_2O_2$-mediated oligomerization. Oligomerization was significantly inhibited by the iron chelator, deferoxamine. During incubation of deoxyribose with cytochrome c and $H_2O_2$, damage to the deoxyribose occurred in parallel with the release of iron from cytochrome c. When cytochrome c that had been exposed to $H_2O_2$ was analyzed by amino acid analysis, the tyrosine, histidine and methionine residues proved to be particularly sensitive. These results suggest that $H_2O_2$-mediated cytochrome c oligomerization is due to oxidative damage resulting from free radicals generated by a combination of the peroxidase activity of cytochrome c and the Fenton reaction of free iron released from the oxidatively-damaged protein.
Keywords
Cytochrome c; Fenton Reaction; Free Radical; Oligomerization;
Citations & Related Records
Times Cited By KSCI : 2  (Citation Analysis)
Times Cited By Web Of Science : 13  (Related Records In Web of Science)
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