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dc.contributor.authorViviani, V. R.-
dc.contributor.authorArnoldi, F. G C-
dc.contributor.authorNeto, A. J S-
dc.contributor.authorOehlmeyer, T. L.-
dc.contributor.authorBechara, E. J H-
dc.contributor.authorOhmiya, Y.-
dc.identifier.citationPhotochemical and Photobiological Sciences, v. 7, n. 2, p. 159-169, 2008.-
dc.description.abstractFirefly luciferases are called pH-sensitive because their bioluminescence spectra display a typical red-shift at acidic pH, higher temperatures, and in the presence of heavy metal cations, whereas other beetle luciferases (click beetles and railroadworms) do not, and for this reason they are called pH-insensitive. Despite many studies on firefly luciferases, the origin of pH-sensitivity is far from being understood. This subject is revised in view of recent results. Some substitutions of amino-acid residues influencing pH-sensitivity in firefly luciferases have been identified. Sequence comparison, site-directed mutagenesis and modeling studies have shown a set of residues differing between pH-sensitive and pH-insensitive luciferases which affect bioluminescence colors. Some substitutions dramatically affecting bioluminescence colors in both groups of luciferases are clustered in the loop between residues 223-235 (Photinus pyralis sequence). A network of hydrogen bonds and salt bridges involving the residues N229-S284-E311-R337 was found to be important for affecting bioluminescence colors. It is suggested that these structural elements may affect the benzothiazolyl side of the luciferin-binding site affecting bioluminescence colors. Experimental evidence suggest that the residual red light emission in pH-sensitive luciferases could be a vestige that may have biological importance in some firefly species. Furthermore, the potential utility of pH-sensitivity for intracellular biosensing applications is considered. © The Royal Society of Chemistry and Owner Societies.en
dc.subjectbenzothiazole derivative-
dc.subjectfirefly luciferase-
dc.subjectheavy metal-
dc.subjectamino acid sequence-
dc.subjectamino acid substitution-
dc.subjectbinding site-
dc.subjectenzyme structure-
dc.subjecthigh temperature-
dc.subjecthydrogen bond-
dc.subjectmolecular model-
dc.subjectpriority journal-
dc.subjectred light-
dc.subjectsite directed mutagenesis-
dc.subjectAmino Acid Sequence-
dc.subjectHydrogen-Ion Concentration-
dc.subjectModels, Molecular-
dc.subjectMolecular Sequence Data-
dc.subjectProtein Conformation-
dc.subjectSequence Homology, Amino Acid-
dc.subjectPhotinus pyralis-
dc.titleThe structural origin and biological function of pH-sensitivity in firefly luciferasesen
dc.contributor.institutionUniversidade Federal de São Carlos (UFSCar)-
dc.contributor.institutionUniversidade de Sorocaba, Sorocaba (UNISO)-
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)-
dc.contributor.institutionUniversidade de São Paulo (USP)-
dc.contributor.institutionHokkaido Graduate School of Medicine-
dc.description.affiliationUniversidade Federal de São Carlos (UFSCAR) Campus de Sorocaba, Av. Darcí Dafferner, 200, Alto da Boa Vista, Sorocaba, 18043-970, Sorocaba SP-
dc.description.affiliationLaboratório de Biotecnologia e Bioluminescência Universidade de Sorocaba, Sorocaba (UNISO), SP-
dc.description.affiliationDepartamento de Genética e Evolução Universidade Federal de São Carlos, São Carlos, SP-
dc.description.affiliationDepartamento de Biologia Universidade Estadual de São Paulo, Rio Claro, SP-
dc.description.affiliationDepartamento de Bioquímica Instituto de Química Universidade de São Paulo, São Paulo, SP-
dc.description.affiliationDepartment of Photobiology Hokkaido Graduate School of Medicine, Sapporo-
dc.description.affiliationUnespDepartamento de Biologia Universidade Estadual de São Paulo, Rio Claro, SP-
dc.rights.accessRightsAcesso restrito-
dc.relation.ispartofPhotochemical and Photobiological Sciences-
Appears in Collections:Artigos, TCCs, Teses e Dissertações da Unesp

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