Active-site properties of Phrixotrix railroad worm green and red bioluminescence-eliciting luciferases

dc.contributorUniversidade Estadual Paulista (UNESP)
dc.creatorViviani, V. R.
dc.creatorArnoldi, F. G. C.
dc.creatorVenkatesh, B.
dc.creatorNeto, A. J. S.
dc.creatorOgawa, F. G. T.
dc.creatorOehlmeyer, A. T. L.
dc.creatorOhmiya, Y.
dc.date2014-05-20T13:54:39Z
dc.date2014-05-20T13:54:39Z
dc.date2006-10-01
dc.date.accessioned2017-04-05T21:11:17Z
dc.date.available2017-04-05T21:11:17Z
dc.identifierJournal of Biochemistry. Tokyo: Japanese Biochemical Soc, v. 140, n. 4, p. 467-474, 2006.
dc.identifier0021-924X
dc.identifierhttp://hdl.handle.net/11449/19562
dc.identifier10.1093/jb/mvj190
dc.identifierWOS:000241798200001
dc.identifierWOS000241798200001.pdf
dc.identifierhttp://dx.doi.org/10.1093/jb/mvj190
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/865395
dc.descriptionThe luciferases of the railroad worm Phrixotrix (Coleoptera: Phengodidae) are the only beetle luciferases that naturally produce true red bioluminescence. Previously, we cloned the green- (PxGR) and red-emitting (PxRE) luciferases of railroad worms Phrixotrix viviani and P. hirtus[OLE1]. These luciferases were expressed and purified, and their active-site properties were determined. The red-emitting PxRE luciferase displays flash-like kinetics, whereas PxGR luciferase displays slow-type kinetics. The substrate affinities and catalytic efficiency of PxRE luciferase are also higher than those of PxGR luciferase. Fluorescence studies with 8-anilino-1-naphthalene sulfonic acid and 6-p-toluidino-2-naphthalene sulfonic acid showed that the PxRE luciferase luciferin-binding site is more polar than that of PxGR luciferase, and it is sensitive to guanidine. Alutagenesis and modelling studies suggest that several invariant residues in the putative luciferin-binding site of PxRE luciferase cannot interact with excited oxyluciferin. These results suggest that one portion of the luciferin-binding site of the red-emitting luciferase is tighter than that of PxGR luciferase, whereas the other portion could be more open and polar.
dc.languageeng
dc.publisherJapanese Biochemical Soc
dc.relationJournal of Biochemistry
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.subjectbioluminescence
dc.subjectluciferases
dc.subjectPhrixotrix
dc.subjectrailroad worms
dc.titleActive-site properties of Phrixotrix railroad worm green and red bioluminescence-eliciting luciferases
dc.typeOtro


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