A STD-NMR Study of the Interaction of the Anabaena Ferredoxin-NADP+ Reductase with the Coenzyme

Molecules

Lara V. Antonini¹  José R. Peregrina²  Jesús Angulo¹  Milagros Medina² 

[1] Instituto de Investigaciones Químicas, CSIC, Americo Vespucio, 49, Sevilla 41092, Spain; E-Mail:;Departamento de Bioquimica y Biologia Molecular y Celular, Facultad de Ciencias and Institute of Biocomputation and Physics of Complex Systems (BIFI), Universidad de Zaragoza, Zaragoza 50009, Spain; E-Mails:

关键词: saturation transfer difference NMR spectroscopy;    flavoenzymes;    hydride transfer;    isoalloxazine-nicotinamide interactions;    CORCEMA-ST;   

DOI  :  10.3390/molecules19010672

来源: mdpi

【 摘 要 】

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.

【 授权许可】

CC BY   
© 2014 by the authors; licensee MDPI, Basel, Switzerland.