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A STD-NMR Study of the Interaction of the Anabaena Ferredoxin-NADP+ Reductase with the Coenzyme

AutorAntonini, Lara V.; Peregrina, José R.; Angulo, Jesús ; Medina, Milagros; Nieto, Pedro M.
Fecha de publicación7-ene-2014
EditorMultidisciplinary Digital Publishing Institute
CitaciónMolecules 19 (1): 672-685 (2014)
ResumenFerredoxin-NADP<sup>+</sup> reductase (FNR) catalyzes the electron transfer from ferredoxin to NADP<sup>+</sup> 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<sup>+</sup> coenzyme we have applied NMR spectroscopy using Saturation Transfer Difference (STD) techniques to analyze the interaction between FNR<sub>ox</sub> and the oxidized state of its NADP<sup>+</sup> 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<sup>+</sup>, are appropriate tools to provide further information about the the interaction epitope.
URIhttp://hdl.handle.net/10261/164185
Identificadoresdoi: 10.3390/molecules19010672
Aparece en las colecciones: Colección MDPI
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