000168506 001__ 168506 000168506 005__ 20260219141450.0 000168506 0248_ $$2sideral$$a61944 000168506 037__ $$aART-2008-61944 000168506 041__ $$aeng 000168506 100__ $$0(orcid)0000-0003-4010-849X$$aGoñi, G$$uUniversidad de Zaragoza 000168506 245__ $$aFlavodoxin-Mediated Electron Transfer from Photosystem I to Ferredoxin-NADP+ Reductase in Anabaena: Role of Flavodoxin Hydrophobic Residues in Protein-Protein Interactions 000168506 260__ $$c2008 000168506 5203_ $$aThree surface hydrophobic residues located at the Anabaena flavodoxin (Fld) putative complex interface with its redox partners were replaced by site-directed mutagenesis. The effects of these replacements on Fld interaction with both its physiological electron donor, photosystem I (PSI), and its electron acceptor, ferredoxin-NADP+ reductase (FNR), were analyzed. Trp57, Ile59, and Ile92 contributed to the optimal orientation and tightening of the FNR:Fld and PSI:Fld complexes. However, these side chains did not appear to be involved in crucial specific interactions, but rather contributed to the obtainment of the optimal orientation and distance of the redox centers required for efficient electron transfer. This supports the idea that the interaction of Fld with its partners is less specific than that of ferredoxin and that more than one orientation is efficient for electron transfer in these transient complexes. Additionally, for some of the analyzed processes, WT Fld seems not to be the most optimized molecular species. Therefore, subtle changes at the isoalloxazine environment not only influence the Fld binding abilities, but also modulate the electron exchange processes by producing different orientations and distances between the redox centers. Finally, the weaker apoflavodoxin interaction with FNR suggests that the solventaccessible region of FMN plays a role either in complex formation with FNR or in providing the adequate conformation of the FNR binding region in Fld. 000168506 540__ $$9info:eu-repo/semantics/closedAccess$$aAll rights reserved$$uhttp://www.europeana.eu/rights/rr-f/ 000168506 590__ $$a3.379$$b2008 000168506 591__ $$aBIOCHEMISTRY & MOLECULAR BIOLOGY$$b96 / 269 = 0.357$$c2008$$dQ2$$eT2 000168506 655_4 $$ainfo:eu-repo/semantics/article$$vinfo:eu-repo/semantics/publishedVersion 000168506 700__ $$aSerrano, A 000168506 700__ $$aFrago, S$$uUniversidad de Zaragoza 000168506 700__ $$aHervas, M 000168506 700__ $$aPeregrina, J.R 000168506 700__ $$aRosa, D.L 000168506 700__ $$aGomez-Moreno, C 000168506 700__ $$aNavarro, J.A 000168506 700__ $$0(orcid)0000-0001-8743-0182$$aMedina, M.$$uUniversidad de Zaragoza 000168506 7102_ $$11002$$2060$$aUniversidad de Zaragoza$$bDpto. Bioq.Biolog.Mol. Celular$$cÁrea Bioquímica y Biolog.Mole. 000168506 773__ $$g47, 4 (2008), 1207-1217$$pBiochemistry$$tBiochemistry$$x0006-2960 000168506 8564_ $$s937623$$uhttps://zaguan.unizar.es/record/168506/files/texto_completo.pdf$$yVersión publicada 000168506 8564_ $$s3475142$$uhttps://zaguan.unizar.es/record/168506/files/texto_completo.jpg?subformat=icon$$xicon$$yVersión publicada 000168506 909CO $$ooai:zaguan.unizar.es:168506$$particulos$$pdriver 000168506 951__ $$a2026-02-19-14:14:15 000168506 980__ $$aARTICLE