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dc.creatorAntonini, Lara V.es
dc.creatorPeregrina, José R.es
dc.creatorAngulo Álvarez, Jesúses
dc.creatorMedina, Milagroses
dc.creatorNieto, Pedro M.es
dc.date.accessioned2020-06-12T07:18:10Z
dc.date.available2020-06-12T07:18:10Z
dc.date.issued2014
dc.identifier.citationAntonini, L.V., Peregrina, J.R., Angulo Álvarez, J., Medina, M. y Nieto, P.M. (2014). A STD-NMR Study of the Interaction of the Anabaena Ferredoxin-NADP+ Reductase with the Coenzyme. Molecules, 19 (1), 672-685.
dc.identifier.issn1420-3049es
dc.identifier.urihttps://hdl.handle.net/11441/97715
dc.description.abstractFerredoxin-NADP+ reductase (FNR) catalyzes the electron transfer from ferredoxin to NADP+ via its flavin FAD cofactor. To get further insights in the architecture of the transient complexes produced during the hydride transfer event between the enzyme and the NADP+ coenzyme we have applied NMR spectroscopy using Saturation Transfer Difference (STD) techniques to analyze the interaction between FNRox and the oxidized state of its NADP+ coenzyme. We have found that STD NMR, together with the use of selected mutations on FNR and of the non-FNR reacting coenzyme analogue NAD+, are appropriate tools to provide further information about the the interaction epitope.es
dc.formatapplication/pdfes
dc.format.extent14 p.es
dc.language.isoenges
dc.publisherMDPIes
dc.relation.ispartofMolecules, 19 (1), 672-685.
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 Internacional*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/*
dc.subjectSaturation transfer difference NMR spectroscopyes
dc.subjectFlavoenzymeses
dc.subjectHydride transferes
dc.subjectIsoalloxazine-nicotinamide interactionses
dc.subjectCORCEMA-STes
dc.titleA STD-NMR Study of the Interaction of the Anabaena Ferredoxin-NADP+ Reductase with the Coenzymees
dc.typeinfo:eu-repo/semantics/articlees
dc.type.versioninfo:eu-repo/semantics/publishedVersiones
dc.rights.accessrightsinfo:eu-repo/semantics/openAccesses
dc.contributor.affiliationUniversidad de Sevilla. Departamento de Química orgánicaes
dc.relation.publisherversionhttps://doi.org/10.3390/molecules19010672es
dc.identifier.doi/10.3390/molecules19010672es
dc.journaltitleMoleculeses
dc.publication.volumen19es
dc.publication.issue1es
dc.publication.initialPage672es
dc.publication.endPage685es

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Except where otherwise noted, this item's license is described as: Attribution-NonCommercial-NoDerivatives 4.0 Internacional