Thread: NMR paper A STD-NMR study of the interaction of the Anabaena ferredoxin-NADP+ reductase with the coenzyme.
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Default A STD-NMR study of the interaction of the Anabaena ferredoxin-NADP+ reductase with the coenzyme.
A STD-NMR study of the interaction of the Anabaena ferredoxin-NADP+ reductase with the coenzyme.

Related Articles A STD-NMR study of the interaction of the Anabaena ferredoxin-NADP+ reductase with the coenzyme.

Molecules. 2014;19(1):672-85

Authors: Antonini LV, Peregrina JR, Angulo J, Medina M, Nieto PM

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.


PMID: 24402199 [PubMed - indexed for MEDLINE]



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