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A STD-NMR study of the interaction of the anabaena ferredoxin-NAD P+ reductase with the coenzyme

AuthorsAntonini, Lara V.; Peregrina, José R.; Angulo, Jesús ; Medina, Milagros; Nieto, Pedro M.
KeywordsIsoalloxazine-nicotinamide interactions
Hydride transfer
Difference NMR spectroscopy
Saturation transfer
Issue Date2014
PublisherMultidisciplinary Digital Publishing Institute
CitationMolecules 19(1): 672-685 (2014)
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.
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