000167980 001__ 167980
000167980 005__ 20260128112902.0
000167980 0247_ $$2doi$$a10.1016/j.abb.2007.08.024
000167980 0248_ $$2sideral$$a64703
000167980 037__ $$aART-2007-64703
000167980 041__ $$aeng
000167980 100__ $$aFrago, Susana$$uUniversidad de Zaragoza
000167980 245__ $$aTuning of the FMN Binding and Oxido-Reduction Properties by Neighboring Side Chains in Anabaena Flavodoxin
000167980 260__ $$c2007
000167980 5060_ $$aAccess copy available to the general public$$fUnrestricted
000167980 5203_ $$aContribution of three regions (phosphate-binding, 50’s and 90’s loops) of Anabaena apoflavodoxin to FMN binding and reduction potential was studied. Thr12 and Glu16 did not influence FMN redox properties, but Thr12 played a role in FMN binding. Replacement of Trp57 with Glu, Lys or Arg moderately shifted Eox/sq and Esq/hq and altered the energetic of the FMN redox states binding profile. Our data indicate that the side chain of position 57 does not modulate Eox/sq by aromatic stacking or solvent exclusion, but rather by influencing the relative strength of the H-bond between the N(5) of the flavin and the Asn58-Ile59 bond. A correlation was observed between the isoalloxazine increase in solvent accessibility and less negative Esq/hq. Moreover, Esq/hq became less negative as positively
charged residues were added near to the isoalloxazine. Ile59 and Ile92 were simultaneously mutated to Ala or Glu. These mutations impaired FMN binding, while shifting Esq/hq to less negative values and Eox/sq to more negative. These effects are discussed on the bases of the X-ray structures of some of the Fld mutants, suggesting that in Anabaena Fld the structural control of both electron transfer steps is much more subtle than in other Flds.
000167980 540__ $$9info:eu-repo/semantics/openAccess$$aby-nc-nd$$uhttps://creativecommons.org/licenses/by-nc-nd/4.0/deed.es
000167980 590__ $$a2.578$$b2007
000167980 591__ $$aBIOPHYSICS$$b32 / 67 = 0.478$$c2007$$dQ2$$eT2
000167980 591__ $$aBIOCHEMISTRY & MOLECULAR BIOLOGY$$b131 / 262 = 0.5$$c2007$$dQ2$$eT2
000167980 655_4 $$ainfo:eu-repo/semantics/article$$vinfo:eu-repo/semantics/acceptedVersion
000167980 700__ $$0(orcid)0000-0003-4010-849X$$aGoñi, Guillermina$$uUniversidad de Zaragoza
000167980 700__ $$0(orcid)0000-0003-2044-4795$$aHerguedas, Beatriz
000167980 700__ $$aPeregrina, Jose Ramon
000167980 700__ $$aSerrano , Ana$$uUniversidad de Zaragoza
000167980 700__ $$aPerez-Dorado, Inmaculada
000167980 700__ $$aMolina, Rafael
000167980 700__ $$aGomez-Moreno, Carlos
000167980 700__ $$aHermoso, Juan A.
000167980 700__ $$0(orcid)0000-0001-9047-0046$$aMartinez-Julvez, Marta$$uUniversidad de Zaragoza
000167980 700__ $$aMayhew, Stephen G.
000167980 700__ $$0(orcid)0000-0001-8743-0182$$aMedina, Milagros$$uUniversidad de Zaragoza
000167980 7102_ $$11002$$2060$$aUniversidad de Zaragoza$$bDpto. Bioq.Biolog.Mol. Celular$$cÁrea Bioquímica y Biolog.Mole.
000167980 773__ $$g467, 2 (2007), 206-217$$pArch. biochem. biophys.$$tARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS$$x0003-9861
000167980 8564_ $$s520769$$uhttps://zaguan.unizar.es/record/167980/files/texto_completo.pdf$$yPostprint
000167980 8564_ $$s1021417$$uhttps://zaguan.unizar.es/record/167980/files/texto_completo.jpg?subformat=icon$$xicon$$yPostprint
000167980 909CO $$ooai:zaguan.unizar.es:167980$$particulos$$pdriver
000167980 951__ $$a2026-01-28-11:24:55
000167980 980__ $$aARTICLE