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Abstracts
The peroxidase-like activity of cytochrome c is considerably increased by unfolding of the protein. The enhancement of the activity is due to the higher reaction rate of unfolded cytochrome c with hydrogen peroxide, which is the rate-determining step in the peroxidase cycle of cytochrome c (Gębicka, L., 2001, Res Chem Intermed 27, 717-23). In this study we checked whether combined action of two unfolding factors, SDS and peroxynitrite or radiation (hydroxyl radicals), increases the peroxidase-like activity of cytochrome c more than any single treatment alone. Peroxynitrite reacts with SDS-modified cytochrome c in the same way as with native cytochrome c, via intermediate radical products, •OH/•NO2, arising from peroxynitrite homolysis. We found that SDS-modified cytochrome c is much more sensitive to oxidative damage than the native protein. Partial unfolding of cytochrome c by SDS causes the peroxide substrate to have a better access to the heme center. On the other hand, the amino acids located in the vicinity of the active site and/or heme group become accessible for oxidizing radicals. The overall effect observed is that the peroxidase-like activity of SDS-modified cytochrome c decreases with an increase of the concentration of the oxidizing species (peroxynitrite or radiolytically generated hydroxyl radicals). The damage of SDS-modified cytochrome c caused by irradiation is much more significant than that observed after peroxynitrite treatment.
Journal
Year
Volume
Issue
Pages
551-555
Physical description
Dates
published
2005
received
2004-12-10
revised
2005-01-12
accepted
2005-02-03
(unknown)
2005-05-15
Contributors
author
- Institute of Applied Radiation Chemistry, Technical University of Łódź, Łódź, Poland
author
- Institute of Applied Radiation Chemistry, Technical University of Łódź, Łódź, Poland
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Document Type
Publication order reference
Identifiers
YADDA identifier
bwmeta1.element.bwnjournal-article-abpv52i2p551kz