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Molecules 2014, 19(1), 672-685; doi:10.3390/molecules19010672

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

1
Instituto de Investigaciones Químicas, CSIC, Americo Vespucio, 49, Sevilla 41092, Spain
2
Departamento de Bioquimica y Biologia Molecular y Celular, Facultad de Ciencias and Institute of Biocomputation and Physics of Complex Systems (BIFI), Universidad de Zaragoza, Zaragoza 50009, Spain
*
Author to whom correspondence should be addressed.
Received: 24 September 2013 / Revised: 17 December 2013 / Accepted: 18 December 2013 / Published: 7 January 2014
(This article belongs to the Special Issue NMR of Proteins and Small Biomolecules)
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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 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. View Full-Text
Keywords: saturation transfer difference NMR spectroscopy; flavoenzymes; hydride transfer; isoalloxazine-nicotinamide interactions; CORCEMA-ST saturation transfer difference NMR spectroscopy; flavoenzymes; hydride transfer; isoalloxazine-nicotinamide interactions; CORCEMA-ST
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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Antonini, L.V.; Peregrina, J.R.; Angulo, J.; Medina, M.; Nieto, P.M. A STD-NMR Study of the Interaction of the Anabaena Ferredoxin-NADP+ Reductase with the Coenzyme. Molecules 2014, 19, 672-685.

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