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• W2005772531 endingPage "849" @default.
• W2005772531 startingPage "841" @default.
• W2005772531 abstract "The effects of nitrosative species on cyt c structure and peroxidase activity were investigated here in the presence of O(2)(*-) and anionic and zwitterionic vesicles. Nitrosative species were generated by 3-morpholinesydnonymine (SIN1) decomposition, using cyt c heme iron and/or molecular oxygen as electron acceptor. Far- and near-UV CD spectra of SIN1-treated cyt c revealed respectively a slight decrease of alpha-helix content (from 39 to 34%) and changes in the tryptophan structure accompanied by increased fluorescence. The Soret CD spectra displayed a significant decrease of the positive signal at 403 nm. EPR spectra revealed the presence of a low-spin cyt c form (S=1/2) with g(1)=2.736, g(2)=2.465, and g(3)=2.058 after incubation with SIN1. These data suggest that the concomitant presence of NO(*) and O(2)(*-) generated from dissolved oxygen, in a system containing cyt c and liposomes, promotes chemical and conformational modifications in cyt c, resulting in a hypothetical bis-histidine hexacoordinated heme iron. We also show that, paradoxically, O(2)(*-) prevents not only membrane lipoperoxidation by peroxide-derived radicals but also oxidation of cyt c itself due to the ability of O(2)(*-) to reduce heme iron. Finally, lipoperoxidation measurements showed that, although it is a more efficient peroxidase, SIN1-treated cyt c is not more effective than native cyt c in promoting damage to anionic liposomes in the presence of tert-ButylOOH, probably due to loss of affinity with negatively charged lipids." @default.
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• W2005772531 date "2009-09-01" @default.
• W2005772531 modified "2023-10-03" @default.
• W2005772531 title "Superoxide radical protects liposome-contained cytochrome c against oxidative damage promoted by peroxynitrite and free radicals" @default.
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• W2005772531 doi "https://doi.org/10.1016/j.freeradbiomed.2009.06.028" @default.
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