The effect of pH on horseradish peroxidase-catalyzed oxidation of melatonin: production of N-1-acetyl-N-2-formyl-5-methoxykynuramine versus radical-mediated degradation

Página do item simplificado
dc.contributor.authorXimenes, Valdecir Farias [UNESP]
dc.contributor.authorFernandes, João Roberto [UNESP]
dc.contributor.authorBueno, Vania B.
dc.contributor.authorCatalani, Luiz H.
dc.contributor.authorde Oliveira, Georgino H.
dc.contributor.authorMachado, Rosangela G. P.
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.date.accessioned2014-05-20T13:24:26Z
dc.date.available2014-05-20T13:24:26Z
dc.date.issued2007-04-01
dc.description.abstractThere is a g-rowing body of evidence that melatonin and its oxidation product, N-1-acetyl-N-2-formyl-5-methoxykynuramine (AFMK), have anti-inflammatory properties. From a nutritional point of view, the discovery of melatonin in plant tissues emphasizes the importance of its relationship with plant peroxidases. Here we found that the pH of the reaction mixture has a profound influence in the reaction rate and products distribution when melatonin is oxidized by the plant enzyme horseradish peroxidase. At pH 5.5. 1 mm of melatonin was almost completely oxidized within 2 min, whereas only about 3% was consumed at pH 7.4. However, the relative yield of AFMK was higher in physiological pH. Radical-mediated oxidation products, including 2-hydroxymelatonin a dimer of, 2-hydroxymelatonin and O-demethylated dimer of melatonin account for the fast consumption of melatonin at pH 5.5. The higher production of AFMK at pH 7.4 was explained by the involvement of compound III of peroxidases as evidenced by spectral studies. on the other hand, the fast oxidative degradation at pH 5.5 was explained by the classic peroxidase cycle.en
dc.description.affiliationUniv Estadual Paulista, Dept Quim, Fac Ciências, Bauru, Brazil
dc.description.affiliationUniv São Paulo, Inst Quim, São Paulo, Brazil
dc.description.affiliationUniv Estadual Paulista, Fac Ciências Farmaceut, Dept Principios At & Nat, Araraquara, SP, Brazil
dc.description.affiliationUnespUniv Estadual Paulista, Dept Quim, Fac Ciências, Bauru, Brazil
dc.description.affiliationUnespUniv Estadual Paulista, Fac Ciências Farmaceut, Dept Principios At & Nat, Araraquara, SP, Brazil
dc.format.extent291-296
dc.identifierhttp://dx.doi.org/10.1111/j.1600-076X.2007.00419.x
dc.identifier.citationJournal of Pineal Research. Oxford: Blackwell Publishing, v. 42, n. 3, p. 291-296, 2007.
dc.identifier.doi10.1111/j.1600-076X.2007.00419.x
dc.identifier.issn0742-3098
dc.identifier.lattes4066413997908572
dc.identifier.lattes8540599256820672
dc.identifier.urihttp://hdl.handle.net/11449/7570
dc.identifier.wosWOS:000245405200011
dc.language.isoeng
dc.publisherBlackwell Publishing
dc.relation.ispartofJournal of Pineal Research
dc.relation.ispartofjcr11.613
dc.relation.ispartofsjr3,945
dc.rights.accessRightsAcesso restrito
dc.sourceWeb of Science
dc.subject2-hydroxymelatoninpt
dc.subjecthorseradish peroxidasept
dc.subjectmelatoninpt
dc.subjectmelatonin dimerpt
dc.subjectN-1-acetyl-N-2-formyl-5-methoxykynuraminept
dc.titleThe effect of pH on horseradish peroxidase-catalyzed oxidation of melatonin: production of N-1-acetyl-N-2-formyl-5-methoxykynuramine versus radical-mediated degradationen
dc.typeArtigo
dcterms.licensehttp://olabout.wiley.com/WileyCDA/Section/id-406071.html
dcterms.rightsHolderBlackwell Publishing
unesp.author.lattes4066413997908572
unesp.author.lattes8540599256820672
unesp.campusUniversidade Estadual Paulista (Unesp), Faculdade de Ciências, Baurupt
unesp.departmentQuímica - FCpt

Arquivos

Licença do Pacote
Agora exibindo 1 - 1 de 1
Nenhuma Miniatura disponível
Nome:
license.txt
Tamanho:
1.71 KB
Formato:
Item-specific license agreed upon to submission
Descrição:

Coleções

Bauru - FC - Faculdade de Ciências