The structural origin and biological function of pH-sensitivity in firefly luciferases

dc.contributorUniversidade Estadual Paulista (UNESP)
dc.creatorViviani, V. R.
dc.creatorArnoldi, F. G C
dc.creatorNeto, A. J S
dc.creatorOehlmeyer, T. L.
dc.creatorBechara, E. J H
dc.creatorOhmiya, Y.
dc.date2014-05-27T11:22:48Z
dc.date2016-10-25T18:25:14Z
dc.date2014-05-27T11:22:48Z
dc.date2016-10-25T18:25:14Z
dc.date2008-02-19
dc.date.accessioned2017-04-06T01:30:02Z
dc.date.available2017-04-06T01:30:02Z
dc.identifierPhotochemical and Photobiological Sciences, v. 7, n. 2, p. 159-169, 2008.
dc.identifier1474-905X
dc.identifier1474-9092
dc.identifierhttp://hdl.handle.net/11449/70307
dc.identifierhttp://acervodigital.unesp.br/handle/11449/70307
dc.identifier10.1039/b714392c
dc.identifier2-s2.0-39049088105
dc.identifierhttp://dx.doi.org/10.1039/b714392c
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/891430
dc.descriptionFirefly 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.
dc.languageeng
dc.relationPhotochemical and Photobiological Sciences
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.subjectbenzothiazole derivative
dc.subjectfirefly luciferase
dc.subjectheavy metal
dc.subjectluciferase
dc.subjectluciferin
dc.subjectamino acid sequence
dc.subjectamino acid substitution
dc.subjectbeetle
dc.subjectbinding site
dc.subjectbioluminescence
dc.subjectenzyme structure
dc.subjecthigh temperature
dc.subjecthydrogen bond
dc.subjectmolecular model
dc.subjectpH
dc.subjectpriority journal
dc.subjectred light
dc.subjectreview
dc.subjectsite directed mutagenesis
dc.subjectAmino Acid Sequence
dc.subjectAnimals
dc.subjectEvolution
dc.subjectFireflies
dc.subjectHydrogen-Ion Concentration
dc.subjectLuciferases
dc.subjectLuminescence
dc.subjectModels, Molecular
dc.subjectMolecular Sequence Data
dc.subjectProtein Conformation
dc.subjectSequence Homology, Amino Acid
dc.subjectColeoptera
dc.subjectElateridae
dc.subjectPhotinus pyralis
dc.titleThe structural origin and biological function of pH-sensitivity in firefly luciferases
dc.typeOtro


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