147115 20260217205534.0 doi 10.1016/j.abb.2024.110204 sideral 140975 ART-2024-140975 eng Moreno, Andrea Universidad de Zaragoza New insights into the function and molecular mechanisms of Ferredoxin-NADP+ reductase from Brucella ovis 2024 Access copy available to the general public Unrestricted Bacterial ferredoxin(flavodoxin)-NADP+ reductases (FPR) primarily catalyze the transfer of reducing equivalents from NADPH to ferredoxin (or flavodoxin) to provide low potential reducing equivalents for the oxidoreductive metabolism. In addition, they can be implicated in regulating reactive oxygen species levels. Here we assess the functionality of FPR from B. ovis to understand its potential roles in the bacteria physiology. We prove that this FPR is active with the endogenous [2Fe–2S] Fdx ferredoxin, exhibiting a KMFdx in the low micromolar range. At the molecular level, this study provides with the first structures of an FPR at room temperature obtained by serial femtosecond crystallography, envisaging increase in flexibility at both the adenine nucleotide moiety of FAD and the C-terminal tail. The produced microcrystals are in addition suitable for future mix-and-inject time-resolved studies with the NADP+/H coenzyme either at synchrotrons or XFELs. Furthermore, the study also predicts the ability of FPR to simultaneously interact with Fdx and NADP+/H. info:eu-repo/grantAgreement/ES/DGA/E35-23R info:eu-repo/grantAgreement/ES/DGA/LMP13_21 info:eu-repo/grantAgreement/ES/MICINN/CNS2022-135713 info:eu-repo/grantAgreement/ES/MICINN/PID2022-136369NB-I00 info:eu-repo/semantics/openAccess by-nc-nd https://creativecommons.org/licenses/by-nc-nd/4.0/deed.es 3.0 2024 BIOPHYSICS 27 / 79 = 0.342 2024 Q2 T2 BIOCHEMISTRY & MOLECULAR BIOLOGY 169 / 320 = 0.528 2024 Q3 T2 0.912 2024 Biophysics 2024 Q1 Molecular Biology 2024 Q2 Biochemistry 2024 Q2 6.4 2024 info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion Quereda-Moraleda, Isabel Lozano-Vallhonrat, Celia Buñuel-Escudero, María Universidad de Zaragoza (orcid)0009-0008-1503-5739 Botha, Sabine Kupitz, Christopher Lisova, Stella Sierra, Ray Mariani, Valerio Schleissner, Pamela Gee, Leland B. Dörner, Katerina Schmidt, Christina Han, Huijong Kloos, Marco Smyth, Peter Valerio, Joana Schulz, Joachim de Wijn, Raphael Melo, Diogo V.M. Round, Adam Trost, Fabian Sobolev, Egor Juncheng, E. Sikorski, Marcin Bean, Richard Martínez-Júlvez, Marta Universidad de Zaragoza (orcid)0000-0001-9047-0046 Martin-Garcia, Jose Manuel Medina, Milagros Universidad de Zaragoza (orcid)0000-0001-8743-0182 2009 750 Universidad de Zaragoza Dpto. Química Analítica Área Química Analítica 1002 060 Universidad de Zaragoza Dpto. Bioq.Biolog.Mol. Celular Área Bioquímica y Biolog.Mole. 762 (2024), 110204 [12 pp.] Arch. biochem. biophys. ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS 0003-9861 7950887 http://zaguan.unizar.es/record/147115/files/texto_completo.pdf Versión publicada 2538864 http://zaguan.unizar.es/record/147115/files/texto_completo.jpg?subformat=icon icon Versión publicada oai:zaguan.unizar.es:147115 articulos driver 2026-02-17-20:33:47 ARTICLE