Does the peroxidase-like activity of sodium dodecyl sulphate-modified cytochrome c increase after peroxynitrite or radiation treatment?

• Autorzy: Gebicka L. , Didik J.
• Języki publikacji: EN

Abstrakty

EN

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.

Słowa kluczowe

EN

peroxidase-like activity; cytochrome c; sodium dodecyl sulphate; radiation; treatment; peroxynitrite; protein

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2005
• Tom: 52
• Numer: 2
• Opis fizyczny: p.551-555,fig.,ref.

Twórcy

autor

Gebicka L.

• Technical University of Lodz, Lodz, Poland

autor

Didik J.

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