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Probing a polar cluster in the retinal binding pocket of bacteriorhodopsin by a chemical design approach

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Probing a polar cluster in the retinal binding pocket of bacteriorhodopsin by a chemical design approach

dc.contributor.author	Simón-Vázquez, R.
dc.contributor.author	Domínguez, M.
dc.contributor.author	Lórenz Fonfría, Victor Armando
dc.contributor.author	Alvarez, S.
dc.contributor.author	Bourdelande, J.L.
dc.contributor.author	de Lera, A.R.
dc.contributor.author	Padrós, E.
dc.contributor.author	Perálvarez-Marín, A.
dc.date.accessioned	2015-12-22T13:24:07Z
dc.date.available	2015-12-22T13:24:07Z
dc.date.issued	2012
dc.identifier.citation	Simón-Vázquez, R. Domínguez, M. Lórenz Fonfría, Victor Armando Alvarez, S. Bourdelande, J.L. de Lera, A.R. Padrós, E. Perálvarez-Marín, A. 2012 Probing a polar cluster in the retinal binding pocket of bacteriorhodopsin by a chemical design approach Plos One 7 8 e42447
dc.identifier.uri	http://hdl.handle.net/10550/49734
dc.description.abstract	Bacteriorhodopsin has a polar cluster of amino acids surrounding the retinal molecule, which is responsible for light harvesting to fuel proton pumping. From our previous studies, we have shown that threonine 90 is the pivotal amino acid in this polar cluster, both functionally and structurally. In an attempt to perform a phenotype rescue, we have chemically designed a retinal analogue molecule to compensate the drastic effects of the T90A mutation in bacteriorhodopsin. This analogue substitutes the methyl group at position C(13) of the retinal hydrocarbon chain by and ethyl group (20-methyl retinal). We have analyzed the effect of reconstituting the wild-type and the T90A mutant apoproteins with all-trans-retinal and its 20-methyl derivative (hereafter, 13-ethyl retinal). Biophysical characterization indicates that recovering the steric interaction between the residue 90 and retinal, eases the accommodation of the chromophore, however it is not enough for a complete phenotype rescue. The characterization of these chemically engineered chromoproteins provides further insight into the role of the hydrogen bond network and the steric interactions involving the retinal binding pocket in bacteriorhodopsin and other microbial sensory rhodopsins.
dc.language.iso	eng
dc.relation.ispartof	Plos One, 2012, vol. 7, num. 8, p. e42447
dc.subject	Bioquímica
dc.subject	Biotecnologia
dc.title	Probing a polar cluster in the retinal binding pocket of bacteriorhodopsin by a chemical design approach
dc.type	journal article	es_ES
dc.date.updated	2015-12-22T13:24:07Z
dc.identifier.doi	10.1371/journal.pone.0042447
dc.identifier.idgrec	107594
dc.rights.accessRights	open access	es_ES