Mostrar el registro sencillo del ítem

Artículo

dc.creatorSánchez Azqueta, Anaes
dc.creatorMartínez Júlvez, Martaes
dc.creatorHervás Morón, Manueles
dc.creatorNavarro Carruesco, José Antonioes
dc.creatorMedina, Milagroses
dc.date.accessioned2018-01-08T17:19:51Z
dc.date.available2018-01-08T17:19:51Z
dc.date.issued2014
dc.identifier.citationSánchez Azqueta, A., Martínez Júlvez, M., Hervás Morón, M., Navarro Carruesco, J.A. y Medina, M. (2014). External loops at the ferredoxin-NADP+ reductase protein-partner binding cavity contribute to substrates allocation. Biochimica et Biophysica Acta - Bioenergetics, 1837, 296-305.
dc.identifier.issn0005-2728es
dc.identifier.urihttp://hdl.handle.net/11441/68398
dc.description.abstractFerredoxin-NADP+ reductase (FNR) is the structural prototype of a family of FAD-containing reductases that catalyze electron transfer between low potential proteins and NAD(P)+/H, and that display a two-domain arrangement with an open cavity at their interface. The inner part of this cavity accommodates the reacting atoms during catalysis. Loops at its edge are highly conserved among plastidic FNRs, suggesting that they might contribute to both flavin stabilization and competent disposition of substrates. Here we pay attention to two of these loops in Anabaena FNR. The first is a sheet-loop-sheet motif, loop102-114, that allocates the FAD adenosine. It was thought to determine the extended FAD conformation, and, indirectly, to modulate isoalloxazine electronic properties, partners binding, catalytic efficiency and even coenzyme specificity. The second, loop261-269, contains key residues for the allocation of partners and coenzyme, including two glutamates, Glu267 and Glu268, proposed as candidates to facilitate the key displacement of the C-terminal tyrosine (Tyr303) from its stacking against the isoalloxazine ring during the catalytic cycle. Our data indicate that the main function of loop102-114 is to provide the inter-domain cavity with flexibility to accommodate protein partners and to guide the coenzyme to the catalytic site, while the extended conformation of FAD must be induced by other protein determinants. Glu267 and Glu268 appear to assist the conformational changes that occur in the loop261-269 during productive coenzyme binding, but their contribution to Tyr303 displacement is minor than expected. Additionally, loop261-269 appears a determinant to ensure reversibility in photosynthetic FNRses
dc.description.sponsorshipMinisterio de Economía, Industria y Competitividad BIO2010-14983es
dc.description.sponsorshipJunta de Andalucía PAIDI BIO-022es
dc.formatapplication/pdfes
dc.language.isoenges
dc.publisherElsevieres
dc.relation.ispartofBiochimica et Biophysica Acta - Bioenergetics, 1837, 296-305.
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 Internacional*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/*
dc.subjectFerredoxin-NADP+ reductasees
dc.subjectElectron and hydride transferes
dc.subjectIsoalloxazine:nicotinamide interactiones
dc.subjectCatalytically competent interactiones
dc.subjectCharge-transfer complexes
dc.titleExternal loops at the ferredoxin-NADP+ reductase protein-partner binding cavity contribute to substrates allocationes
dc.typeinfo:eu-repo/semantics/articlees
dc.type.versioninfo:eu-repo/semantics/acceptedVersiones
dc.rights.accessRightsinfo:eu-repo/semantics/openAccesses
dc.contributor.affiliationUniversidad de Sevilla. Departamento de Bioquímica Vegetal y Biología Moleculares
dc.relation.projectIDBIO2010-14983es
dc.relation.projectIDPAIDI BIO-022es
dc.relation.publisherversionhttp://dx.doi.org/10.1016/j.bbabio.2013.11.016es
dc.identifier.doi10.1016/j.bbabio.2013.11.016es
idus.format.extent59 p.es
dc.journaltitleBiochimica et Biophysica Acta - Bioenergeticses
dc.publication.volumen1837es
dc.publication.initialPage296es
dc.publication.endPage305es
dc.contributor.funderMinisterio de Economia, Industria y Competitividad (MINECO). España
dc.contributor.funderJunta de Andalucía

FicherosTamañoFormatoVerDescripción
External loops at the ferredox ...1.747MbIcon   [PDF] Ver/Abrir  

Este registro aparece en las siguientes colecciones

Mostrar el registro sencillo del ítem

Attribution-NonCommercial-NoDerivatives 4.0 Internacional
Excepto si se señala otra cosa, la licencia del ítem se describe como: Attribution-NonCommercial-NoDerivatives 4.0 Internacional