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.
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