32460 20171130135647.0 doi 10.3390/molecules19010672 sideral 85181 ART-2014-85181 eng Antonini, L.V. A STD-NMR study of the interaction of the Anabaena Ferredoxin-NAD P+ reductase with the Coenzyme 2014 Access copy available to the general public Unrestricted 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. info:eu-repo/grantAgreement/ES/MICINN/BIO2010-14983 info:eu-repo/grantAgreement/ES/MICINN/CTQ2012-32605 info:eu-repo/semantics/openAccess by http://creativecommons.org/licenses/by/3.0/es/ 2.416 2014 CHEMISTRY, ORGANIC 22 / 58 = 0.379 2014 Q2 T2 info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion Peregrina, J.R. Angulo, J. (orcid)0000-0001-8743-0182 Medina, M. Universidad de Zaragoza Nieto, P.M. 1002 060 Universidad de Zaragoza Departamento de Bioquímica y Biología Molecular y Celular Bioquímica y Biología Molecular 19, 1 (2014), 672-685 Molecules MOLECULES 1420-3049 702701 http://zaguan.unizar.es/record/32460/files/texto_completo.pdf Versión publicada 84446 http://zaguan.unizar.es/record/32460/files/texto_completo.jpg?subformat=icon icon Versión publicada oai:zaguan.unizar.es:32460 articulos driver 2017-11-30-13:53:32 ARTICLE