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dc.contributor.authorMorillo Cazorla, Margarita
dc.contributor.authorToledo Gonzalez, Darwin
dc.contributor.authorPérez González, Juan Jesús
dc.contributor.authorRamon Portés, Eva
dc.contributor.authorGarriga Solé, Pere
dc.contributor.otherUniversitat Politècnica de Catalunya. Departament d'Enginyeria Química
dc.date.accessioned2014-10-07T11:40:47Z
dc.date.created2014-07-01
dc.date.issued2014-07-01
dc.identifier.citationMorillo, M. [et al.]. Mercury-induced dark-state instability and photobleaching alterations of the visual G-protein coupled receptor rhodopsin. "Chemical research in toxicology", 01 Juliol 2014, vol. 27, núm. 7, p. 1219-1226.
dc.identifier.issn0893-228X
dc.identifier.urihttp://hdl.handle.net/2117/24291
dc.description.abstractMercuric compounds were previously shown to affect the visual phototransduction cascade, and this could result in vision impairment. We have analyzed the effect of mercuric chloride on the structure and stability of the dim light vision photoreceptor rhodopsin. For this purpose, we have used both native rhodopsin imrnunopurified from bovine retinas and a recombinant mutant rhodopsin carrying several Cys to Ser substitutions in order to investigate the potential binding site of mercury on the receptor. Our results show that mercuric chloride dramatically reduces the stability of dark-state rhodopsin and alters the molecular features of the photoactived conformation obtained upon illumination by eliciting the formation of an altered photointermediate. The thermal bleaching kinetics of native and mutant rhodopsin is markedly accelerated by mercury in a concentration-dependent manner, and its chromophore regeneration ability is severely reduced without significantly affecting its G-protein activation capacity. Furthermore, fluorescence spectroscopic measurements on the retinal release process, ensuing illumination, suggest that mercury impairs complete retinal release from the receptor binding pocket. Our results provide further support for the capacity of mercury as a hazardous metal ion with reported deleterious effect on vision and provide a molecular explanation for such an effect at the rhodopsin photoreceptor level. We suggest that mercury could alter vision by acting in a specific manner on the molecular components of the retinoid cycle, particularly by modifying the ability of the visual photoreceptor protein rhodopsin to be regenerated and to be normally photoactivated by light.
dc.format.extent8 p.
dc.language.isoeng
dc.subjectÀrees temàtiques de la UPC::Ciències de la visió::Biologia ocular
dc.subject.lcshRetinitis pigmentosa -- Etiology
dc.subject.lcshG proteins -- Receptors
dc.subject.otherRetinitis-pigmentosa
dc.subject.otherCrystal-structure
dc.subject.otherConformational stability
dc.subject.otherMolecular-mechanisms
dc.subject.otherThermal-stability
dc.subject.otherOrganic mercurial
dc.subject.otherColor-vision
dc.subject.otherAccumulation
dc.subject.otherActivation
dc.subject.otherWorkers
dc.titleMercury-induced dark-state instability and photobleaching alterations of the visual G-protein coupled receptor rhodopsin
dc.typeArticle
dc.subject.lemacRetina -- Malalties
dc.subject.lemacRetinosi pigmentària
dc.subject.lemacRodopsina
dc.contributor.groupUniversitat Politècnica de Catalunya. GBMI - Grup de Biotecnologia Molecular i Industrial
dc.contributor.groupUniversitat Politècnica de Catalunya. ENGMOL - Enginyeria Molecular
dc.identifier.doi10.1021/tx500114s
dc.description.peerreviewedPeer Reviewed
dc.relation.publisherversionhttp://pubs.acs.org/doi/pdf/10.1021/tx500114s
dc.rights.accessRestricted access - publisher's policy
local.identifier.drac15112572
dc.description.versionPostprint (published version)
dc.date.lift10000-01-01
local.citation.authorMorillo, M.; Toledo, D.; Perez, J.; Ramon, E.; Garriga, P.
local.citation.publicationNameChemical research in toxicology
local.citation.volume27
local.citation.number7
local.citation.startingPage1219
local.citation.endingPage1226


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