Please use this identifier to cite or link to this item: https://repositorio.unifesp.br/handle/11600/31817
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dc.contributor.authorMano, Camila M.
dc.contributor.authorBarros, Marcelo P.
dc.contributor.authorFaria, Priscila A.
dc.contributor.authorPrieto, Tatiana
dc.contributor.authorDyszy, Fabio H.
dc.contributor.authorNascimento, Otaciro R.
dc.contributor.authorNantes, Iseli L.
dc.contributor.authorBechara, Etelvino J. H. [UNIFESP]
dc.date.accessioned2016-01-24T13:58:45Z-
dc.date.available2016-01-24T13:58:45Z-
dc.date.issued2009-09-15
dc.identifierhttp://dx.doi.org/10.1016/j.freeradbiomed.2009.06.028
dc.identifier.citationFree Radical Biology and Medicine. New York: Elsevier B.V., v. 47, n. 6, p. 841-849, 2009.
dc.identifier.issn0891-5849
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/31817-
dc.description.abstractThe effects of nitrosative species on cyt c structure and peroxidase activity were investigated here in the presence of O(2)(center dot-) 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 a-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(center dot) and O(2)(center dot-) generated from dissolved oxygen, in a system containing cyt c and liposomes, promotes chemical and conformational modi. cations in cyt c, resulting in a hypothetical bis-histidine hexacoordinated heme iron. We also show that, paradoxically, O(2)(center dot-) prevents not only membrane lipoperoxidation by peroxide-derived radicals but also oxidation of cyt c itself due to the ability of O(2)(center dot-) 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. (C) 2009 Elsevier Inc. All rights reserved.en
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.description.sponsorshipInternational Foundation for Science
dc.format.extent841-849
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofFree Radical Biology and Medicine
dc.rightsAcesso restrito
dc.subjectCytochrome cen
dc.subjectSuperoxideen
dc.subjectNitric oxideen
dc.subjectPeroxynitriteen
dc.subjectPeroxidase activityen
dc.subjectPhosphatidylcholineen
dc.subjectPhosphatidylglycerolen
dc.titleSuperoxide radical protects liposome-contained cytochrome c against oxidative damage promoted by peroxynitrite and free radicalsen
dc.typeArtigo
dc.rights.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.contributor.institutionUniv Cruzeiro Sul
dc.contributor.institutionUniv Mogi das Cruzes
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.description.affiliationUniv São Paulo, Inst Quim, Dept Bioquim, BR-05508900 São Paulo, Brazil
dc.description.affiliationUniv Cruzeiro Sul, Programa Quim Ambiental Ciencias Biol & Saude, São Paulo, Brazil
dc.description.affiliationUniv Mogi das Cruzes, Ctr Interdisciplinar Invest Bioquim, Mogi Das Cruzes, Brazil
dc.description.affiliationUniv São Paulo, Dept Fis & Informat, Inst Fis Sao Carlos, Sao Carlos, SP, Brazil
dc.description.affiliationUniversidade Federal de São Paulo, Dept Ciencias Exatas & Terra, Diadema, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Dept Ciencias Exatas & Terra, Diadema, Brazil
dc.identifier.doi10.1016/j.freeradbiomed.2009.06.028
dc.description.sourceWeb of Science
dc.identifier.wosWOS:000273494300018
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