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Título

A STD-NMR study of the interaction of the Anabaena Ferredoxin-NAD P+ reductase with the Coenzyme

AutorAntonini, L.V.; Peregrina, José R.; Angulo, Javier; Medina, Milagros; Nieto, Pedro M.
Palabras claveIsoalloxazine-nicotinamide interactions
CORCEMA-ST
Hydride transfer
Flavoenzymes
Difference NMR spectroscopy
Saturation transfer
Fecha de publicación2014
EditorMultidisciplinary Digital Publishing Institute
CitaciónMolecules 19: 672- 685 (2014)
ResumenFerredoxin-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.© 2014 by the authors licensee MDPI Basel Switzerland.
URIhttp://hdl.handle.net/10261/98810
DOI10.3390/molecules19010672
Identificadoresdoi: 10.3390/molecules19010672
issn: 1420-3049
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