Resumen: 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. Idioma: Inglés DOI: 10.3390/molecules19010672 Año: 2014 Publicado en: MOLECULES 19, 1 (2014), 672-685 ISSN: 1420-3049 Factor impacto JCR: 2.416 (2014) Categ. JCR: CHEMISTRY, ORGANIC rank: 22 / 58 = 0.379 (2014) - Q2 - T2 Financiación: info:eu-repo/grantAgreement/ES/MICINN/BIO2010-14983 Financiación: info:eu-repo/grantAgreement/ES/MICINN/CTQ2012-32605 Tipo y forma: Article (Published version) Área (Departamento): Bioquímica y Biología Molecular (Departamento de Bioquímica y Biología Molecular y Celular)