000147115 001__ 147115
000147115 005__ 20241212141912.0
000147115 0247_ $$2doi$$a10.1016/j.abb.2024.110204
000147115 0248_ $$2sideral$$a140975
000147115 037__ $$aART-2024-140975
000147115 041__ $$aeng
000147115 100__ $$aMoreno, Andrea$$uUniversidad de Zaragoza
000147115 245__ $$aNew insights into the function and molecular mechanisms of Ferredoxin-NADP+ reductase from Brucella ovis
000147115 260__ $$c2024
000147115 5060_ $$aAccess copy available to the general public$$fUnrestricted
000147115 5203_ $$aBacterial ferredoxin(flavodoxin)-NADP+ reductases (FPR) primarily catalyze the transfer of reducing equivalents from NADPH to ferredoxin (or flavodoxin) to provide low potential reducing equivalents for the oxidoreductive metabolism. In addition, they can be implicated in regulating reactive oxygen species levels. Here we assess the functionality of FPR from B. ovis to understand its potential roles in the bacteria physiology. We prove that this FPR is active with the endogenous [2Fe–2S] Fdx ferredoxin, exhibiting a KMFdx in the low micromolar range. At the molecular level, this study provides with the first structures of an FPR at room temperature obtained by serial femtosecond crystallography, envisaging increase in flexibility at both the adenine nucleotide moiety of FAD and the C-terminal tail. The produced microcrystals are in addition suitable for future mix-and-inject time-resolved studies with the NADP+/H coenzyme either at synchrotrons or XFELs. Furthermore, the study also predicts the ability of FPR to simultaneously interact with Fdx and NADP+/H.
000147115 536__ $$9info:eu-repo/grantAgreement/ES/DGA/E35-23R$$9info:eu-repo/grantAgreement/ES/DGA/LMP13_21$$9info:eu-repo/grantAgreement/ES/MICINN/CNS2022-135713$$9info:eu-repo/grantAgreement/ES/MICINN/PID2022-136369NB-I00
000147115 540__ $$9info:eu-repo/semantics/openAccess$$aby-nc-nd$$uhttp://creativecommons.org/licenses/by-nc-nd/3.0/es/
000147115 655_4 $$ainfo:eu-repo/semantics/article$$vinfo:eu-repo/semantics/publishedVersion
000147115 700__ $$aQuereda-Moraleda, Isabel
000147115 700__ $$aLozano-Vallhonrat, Celia
000147115 700__ $$aBuñuel-Escudero, María$$uUniversidad de Zaragoza
000147115 700__ $$aBotha, Sabine
000147115 700__ $$aKupitz, Christopher
000147115 700__ $$aLisova, Stella
000147115 700__ $$aSierra, Ray
000147115 700__ $$aMariani, Valerio
000147115 700__ $$aSchleissner, Pamela
000147115 700__ $$aGee, Leland B.
000147115 700__ $$aDörner, Katerina
000147115 700__ $$aSchmidt, Christina
000147115 700__ $$aHan, Huijong
000147115 700__ $$aKloos, Marco
000147115 700__ $$aSmyth, Peter
000147115 700__ $$aValerio, Joana
000147115 700__ $$aSchulz, Joachim
000147115 700__ $$ade Wijn, Raphael
000147115 700__ $$aMelo, Diogo V.M.
000147115 700__ $$aRound, Adam
000147115 700__ $$aTrost, Fabian
000147115 700__ $$aSobolev, Egor
000147115 700__ $$aJuncheng, E.
000147115 700__ $$aSikorski, Marcin
000147115 700__ $$aBean, Richard
000147115 700__ $$0(orcid)0000-0001-9047-0046$$aMartínez-Júlvez, Marta$$uUniversidad de Zaragoza
000147115 700__ $$aMartin-Garcia, Jose Manuel
000147115 700__ $$0(orcid)0000-0001-8743-0182$$aMedina, Milagros$$uUniversidad de Zaragoza
000147115 7102_ $$12009$$2750$$aUniversidad de Zaragoza$$bDpto. Química Analítica$$cÁrea Química Analítica
000147115 7102_ $$11002$$2060$$aUniversidad de Zaragoza$$bDpto. Bioq.Biolog.Mol. Celular$$cÁrea Bioquímica y Biolog.Mole.
000147115 773__ $$g762 (2024), 110204 [12 pp.]$$pArch. biochem. biophys.$$tARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS$$x0003-9861
000147115 8564_ $$s7950887$$uhttps://zaguan.unizar.es/record/147115/files/texto_completo.pdf$$yVersión publicada
000147115 8564_ $$s2538864$$uhttps://zaguan.unizar.es/record/147115/files/texto_completo.jpg?subformat=icon$$xicon$$yVersión publicada
000147115 909CO $$ooai:zaguan.unizar.es:147115$$particulos$$pdriver
000147115 951__ $$a2024-12-12-12:43:15
000147115 980__ $$aARTICLE