The Water Effect on the Kinetics of the Bovine Liver Catalase

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dc.contributor.authorVicente Seixas, Flavio Augusto
dc.contributor.authorda Silva, Milene Ribeiro
dc.contributor.authorMurakami, Mario Tyago
dc.contributor.authorTosqui, Priscilla [UNESP]
dc.contributor.authorColombo, Marcio Francisco [UNESP]
dc.contributor.institutionUniversidade Estadual de Maringá (UEM)
dc.contributor.institutionNatl Res Ctr Energy & Mat
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.date.accessioned2014-05-20T14:02:38Z
dc.date.available2014-05-20T14:02:38Z
dc.date.issued2011-09-01
dc.description.abstractCatalase is an enzyme that occurs in almost all aerobic organisms. Its main metabolic function is to prevent oxidative damage to tissues induced by hydrogen peroxide which is a strong oxidizing agent. Catalase is very effective in performing this task, since it has the highest turnover rate among all the enzymes. The properties of catalase have been investigated extensively for many years; however, the role of the solvent molecules in the catalytic reaction of this enzyme has not yet been investigated. Therefore, the objective of this work was to investigate the contribution of the solvent molecules on the catalytic reaction of bovine liver catalase with its substrate H(2)O(2) by the osmotic stress method. As a probe for protein structural changes in solution, the differential number of water molecules released during the transition from free to bound form of the enzyme was measured. These assays were correlated with protein structural data provided by the SAXS technique and crystallographic structures of free and CN(-) bonded enzymes. The results showed that the difference in surface accessible area of the crystal structures does not reflect the variation that is observed in solution. Moreover, catalase is not influenced by the solvent during the catalytic reaction, which represents a lower energy barrier to be crossed in the overall energetics of the reaction, a fact that contributes to the high turnover rate of catalase.en
dc.description.affiliationUniversidade Estadual de Maringá (UEM), DBQ, Dept Biochem, BR-87020900 Maringa, Parana, Brazil
dc.description.affiliationUniversidade Estadual de Maringá (UEM), Dept Technol, BR-87506370 Umuarama, PR, Brazil
dc.description.affiliationNatl Res Ctr Energy & Mat, Natl Lab Biosci, BR-13083970 Campinas, SP, Brazil
dc.description.affiliationUniv Estadual Paulista, Dept Phys, BR-15054000 Sao Jose do Rio Preto, SP, Brazil
dc.description.affiliationUnespUniv Estadual Paulista, Dept Phys, BR-15054000 Sao Jose do Rio Preto, SP, Brazil
dc.description.sponsorshipUEM
dc.description.sponsorshipFundação Araucária de Apoio ao Desenvolvimento Científico e Tecnológico do Paraná (FAADCT/PR)
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.format.extent879-885
dc.identifierhttp://eurekaselect.com/88018/article
dc.identifier.citationProtein and Peptide Letters. Sharjah: Bentham Science Publ Ltd, v. 18, n. 9, p. 879-885, 2011.
dc.identifier.issn0929-8665
dc.identifier.lattes3425817209646054
dc.identifier.urihttp://hdl.handle.net/11449/22081
dc.identifier.wosWOS:000295409800004
dc.language.isoeng
dc.publisherBentham Science Publ Ltd
dc.relation.ispartofProtein and Peptide Letters
dc.relation.ispartofjcr1.039
dc.relation.ispartofsjr0,429
dc.rights.accessRightsAcesso restrito
dc.sourceWeb of Science
dc.subjectCatalaseen
dc.subjectosmotic stress methoden
dc.subjectenzyme kineticsen
dc.subjectwater effecten
dc.subjectprotein allosteryen
dc.titleThe Water Effect on the Kinetics of the Bovine Liver Catalaseen
dc.typeArtigo
dcterms.licensehttp://www.benthamscience.com/permission.php
dcterms.rightsHolderBentham Science Publ Ltd
unesp.author.lattes3425817209646054
unesp.campusUniversidade Estadual Paulista (Unesp), Instituto de Biociências Letras e Ciências Exatas, São José do Rio Pretopt

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Artigos - Física - IBILCE