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

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.

SUBMITTER: Antonini LV 

PROVIDER: S-EPMC6272016 | biostudies-literature | 2014 Jan

REPOSITORIES: biostudies-literature