000167979 001__ 167979
000167979 005__ 20260128112902.0
000167979 0247_ $$2doi$$a10.1016/j.bbabio.2008.12.006
000167979 0248_ $$2sideral$$a61050
000167979 037__ $$aART-2009-61050
000167979 041__ $$aeng
000167979 100__ $$0(orcid)0000-0003-4010-849X$$aGoñí, Guillermina
000167979 245__ $$aFlavodoxin: A compromise between efficiency and versatility in the electron transfer from Photosystem I to Ferredoxin-NADP(+) reductase.
000167979 260__ $$c2009
000167979 5060_ $$aAccess copy available to the general public$$fUnrestricted
000167979 5203_ $$aUnder iron-deficient conditions Flavodoxin (Fld) replaces Ferredoxin in Anabaena as electron carrier from Photosystem I (PSI) to Ferredoxin-NADP+ reductase (FNR). Several residues modulate the Fld interaction with
FNR and PSI, but no one appears as specifically critical for efficient electron transfer (ET). Fld shows a strong dipole moment, with its negative end directed towards the flavin ring. The role of this dipole moment in the processes of interaction and ET with positively charged surfaces exhibited by PSI and FNR has been analysed by introducing single and multiple charge reversal mutations on the Fld surface. Our data confirm that in this system interactions do not rely on a precise complementary surface of the reacting molecules. In fact, they indicate that the initial orientation driven by the alignment of dipole moment of the Fld molecule with that of the partner contributes to the formation of a bunch of alternative binding modes competent for the efficient ET reaction. Additionally, the fact that Fld uses different interaction surfaces to dock to PSI and to FNR is confirmed.
000167979 540__ $$9info:eu-repo/semantics/openAccess$$aby-nc-nd$$uhttps://creativecommons.org/licenses/by-nc-nd/4.0/deed.es
000167979 590__ $$a3.688$$b2009
000167979 591__ $$aBIOPHYSICS$$b18 / 74 = 0.243$$c2009$$dQ1$$eT1
000167979 591__ $$aBIOCHEMISTRY & MOLECULAR BIOLOGY$$b87 / 281 = 0.31$$c2009$$dQ2$$eT1
000167979 655_4 $$ainfo:eu-repo/semantics/article$$vinfo:eu-repo/semantics/acceptedVersion
000167979 700__ $$0(orcid)0000-0003-2044-4795$$aHerguedas, Beatriz$$uUniversidad de Zaragoza
000167979 700__ $$aHervás, Manuel
000167979 700__ $$aPeregrina, José R.
000167979 700__ $$ade la Rosa, Miguel A.
000167979 700__ $$0(orcid)0000-0003-4087-4733$$aGómez-Moreno, Carlos$$uUniversidad de Zaragoza
000167979 700__ $$aNavarro, José A.
000167979 700__ $$aHermoso, Juan A.
000167979 700__ $$0(orcid)0000-0001-9047-0046$$aMartínez-Júlvez, Marta$$uUniversidad de Zaragoza
000167979 700__ $$0(orcid)0000-0001-8743-0182$$aMedina, Milagros$$uUniversidad de Zaragoza
000167979 7102_ $$11002$$2060$$aUniversidad de Zaragoza$$bDpto. Bioq.Biolog.Mol. Celular$$cÁrea Bioquímica y Biolog.Mole.
000167979 773__ $$g1787, 3 (2009), 144-154$$pBiochim. biophys. acta, Bioenerg.$$tBIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS$$x0005-2728
000167979 8564_ $$s6042632$$uhttps://zaguan.unizar.es/record/167979/files/texto_completo.pdf$$yPostprint
000167979 8564_ $$s1252549$$uhttps://zaguan.unizar.es/record/167979/files/texto_completo.jpg?subformat=icon$$xicon$$yPostprint
000167979 909CO $$ooai:zaguan.unizar.es:167979$$particulos$$pdriver
000167979 951__ $$a2026-01-28-11:24:54
000167979 980__ $$aARTICLE