Article
A STD-NMR Study of the Interaction of the Anabaena Ferredoxin-NADP+ Reductase with the Coenzyme
Author/s | Antonini, Lara V.
Peregrina, José R. Angulo Álvarez, Jesús Medina, Milagros Nieto, Pedro M. |
Department | Universidad de Sevilla. Departamento de Química orgánica |
Publication Date | 2014 |
Deposit Date | 2020-06-12 |
Published in |
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Abstract | Ferredoxin-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 ... Ferredoxin-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. |
Citation | Antonini, 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. |
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