000167981 001__ 167981
000167981 005__ 20260127151100.0
000167981 0247_ $$2doi$$a10.1111/ppl.12621
000167981 0248_ $$2sideral$$a104602
000167981 037__ $$aART-2018-104602
000167981 041__ $$aeng
000167981 100__ $$aKoskela, M.M.
000167981 245__ $$aArabidopsis FNRL protein is an NADPH-dependent chloroplast oxidoreductase resembling bacterial ferredoxin-NADP+ reductases
000167981 260__ $$c2018
000167981 5060_ $$aAccess copy available to the general public$$fUnrestricted
000167981 5203_ $$aPlastidic ferredoxin-NADP+ oxidoreductases (FNRs; EC:1.18.1.2) together with bacterial type FNRs (FPRs) form the plant-type FNR family. Members of this group contain a two-domain scaffold that forms the basis of an extended superfamily of flavin adenine dinucleotide (FAD) dependent oxidoreductases. In this study, we show that the Arabidopsis thaliana At1g15140 [Ferredoxin-NADP+ oxidoreductase-like (FNRL)] is an FAD-containing NADPH dependent oxidoreductase present in the chloroplast stroma. Determination of the kinetic parameters using the DCPIP NADPH-dependent diaphorase assay revealed that the reaction catalysed by a recombinant FNRL protein followed a saturation Michaelis–Menten profile on the NADPH concentration with kcat = 3.2 ± 0.2 s-1, Km NADPH = 1.6 ± 0.3 µM and kcat/Km NADPH = 2.0 ± 0.4 µM-1 s-1. Biochemical assays suggested that FNRL is not likely to interact with Arabidopsis ferredoxin 1, which is supported by the sequence analysis implying that the known Fd-binding residues in plastidic FNRs differ from those of FNRL. In addition, based on structural modelling FNRL has an FAD-binding N-terminal domain built from a six-stranded ß-sheet and one a-helix, and a C-terminal NADP+-binding a/ß domain with a five-stranded ß-sheet with a pair of a-helices on each side. The FAD-binding site is highly hydrophobic and predicted to bind FAD in a bent conformation typically seen in bacterial FPRs.
000167981 536__ $$9info:eu-repo/grantAgreement/ES/DGA/B18$$9info:eu-repo/grantAgreement/ES/MINECO/BIO2016-75183-P
000167981 540__ $$9info:eu-repo/semantics/openAccess$$aAll rights reserved$$uhttp://www.europeana.eu/rights/rr-f/
000167981 590__ $$a3.0$$b2018
000167981 591__ $$aPLANT SCIENCES$$b48 / 226 = 0.212$$c2018$$dQ1$$eT1
000167981 592__ $$a1.23$$b2018
000167981 593__ $$aCell Biology$$c2018$$dQ1
000167981 593__ $$aGenetics$$c2018$$dQ1
000167981 593__ $$aPlant Science$$c2018$$dQ1
000167981 593__ $$aPhysiology$$c2018$$dQ1
000167981 593__ $$aMedicine (miscellaneous)$$c2018$$dQ1
000167981 655_4 $$ainfo:eu-repo/semantics/article$$vinfo:eu-repo/semantics/acceptedVersion
000167981 700__ $$aDahlström, K.M.
000167981 700__ $$0(orcid)0000-0003-4010-849X$$aGoñi, G.
000167981 700__ $$aLehtimäki, N.
000167981 700__ $$aNurmi, M.
000167981 700__ $$0(orcid)0000-0001-5702-4538$$aVelazquez-Campoy, A.$$uUniversidad de Zaragoza
000167981 700__ $$aHanke, G.
000167981 700__ $$aBölter, B.
000167981 700__ $$aSalminen, T.A.
000167981 700__ $$0(orcid)0000-0001-8743-0182$$aMedina, M.$$uUniversidad de Zaragoza
000167981 700__ $$aMulo, P.
000167981 7102_ $$11002$$2060$$aUniversidad de Zaragoza$$bDpto. Bioq.Biolog.Mol. Celular$$cÁrea Bioquímica y Biolog.Mole.
000167981 773__ $$g162, 2 (2018), 177-190$$pPhysiol. Plant.$$tPHYSIOLOGIA PLANTARUM$$x0031-9317
000167981 8564_ $$s386764$$uhttps://zaguan.unizar.es/record/167981/files/texto_completo.pdf$$yPostprint
000167981 8564_ $$s1075562$$uhttps://zaguan.unizar.es/record/167981/files/texto_completo.jpg?subformat=icon$$xicon$$yPostprint
000167981 909CO $$ooai:zaguan.unizar.es:167981$$particulos$$pdriver
000167981 951__ $$a2026-01-27-15:07:19
000167981 980__ $$aARTICLE