Antonini, Lara V.Peregrina, José R.Angulo Álvarez, JesúsMedina, MilagrosNieto, Pedro M.2020-06-122020-06-122014Antonini, 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), 672-685.1420-3049https://hdl.handle.net/11441/97715Ferredoxin-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.application/pdf14 p.engAttribution-NonCommercial-NoDerivatives 4.0 Internacionalhttp://creativecommons.org/licenses/by-nc-nd/4.0/Saturation transfer difference NMR spectroscopyFlavoenzymesHydride transferIsoalloxazine-nicotinamide interactionsCORCEMA-STA STD-NMR Study of the Interaction of the Anabaena Ferredoxin-NADP+ Reductase with the Coenzymeinfo:eu-repo/semantics/articleinfo:eu-repo/semantics/openAccesshttps://doi.org//10.3390/molecules19010672