%0 Journal Article
%T A STD-NMR Study of the Interaction of the Anabaena Ferredoxin-NADP+ Reductase with the Coenzyme
%A Lara V. Antonini
%A Jos¨¦ R. Peregrina
%A Jes¨˛s Angulo
%A Milagros Medina
%A Pedro M. Nieto
%J Molecules
%D 2014
%I MDPI AG
%R 10.3390/molecules19010672
%X 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 FNR ox 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.
%K saturation transfer difference NMR spectroscopy
%K flavoenzymes
%K hydride transfer
%K isoalloxazine-nicotinamide interactions
%K CORCEMA-ST
%U http://www.mdpi.com/1420-3049/19/1/672