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dc.creatorArregui Casaus, José Luises
dc.creatorNavarro Carruesco, José Antonioes
dc.creatorHervás Morón, Manueles
dc.creatorLostao, Anabeles
dc.creatorRosa Acosta, Miguel Ángel de laes
dc.creatorGómez Moreno, Carloses
dc.creatorSancho, Javieres
dc.creatorMedina, Milagroses
dc.date.accessioned2022-05-31T09:47:20Z
dc.date.available2022-05-31T09:47:20Z
dc.date.issued2002
dc.identifier.citationArregui Casaus, J.L., Navarro Carruesco, J.A., Hervás Morón, M., Lostao, A., Rosa Acosta, M.Á.d.l., Gómez Moreno, C.,...,Medina, M. (2002). Anabaena sp. PCC 7119 Flavodoxin as Electron Carrier from Photosystem I to Ferredoxin-NADP+Reductase: ROLE OF TRP57 AND TYR94. Journal of Biological Chemistry, 277 (25), 22338-22344.
dc.identifier.issn0021-9258es
dc.identifier.urihttps://hdl.handle.net/11441/133881
dc.description.abstractThe influence of the amino acid residues sandwiching the flavin ring in flavodoxin (Fld) from the cyanobacteriumAnabaena sp. PCC 7119 in complex formation and electron transfer (ET) with its natural partners, photosystem I (PSI) and ferredoxin-NADP+ reductase (FNR), was examined in mutants of the key residues Trp57 and Tyr94. The mutants' ability to form complexes with either FNR or PSI is similar to that of wild-type Fld. However, some of the mutants exhibit altered kinetic properties in their ET processes that can be explained in terms of altered flavin accessibility and/or thermodynamic parameters. The most noticeable alteration is produced upon replacement of Tyr94 by alanine. In this mutant, the processes that involve the transfer of one electron from either PSI or FNR are clearly accelerated, which might be attributable to a larger accessibility of the flavin to the reductant. However, when the opposite ET flow is analyzed with FNR, the reduced Y94A mutant transfers electrons to FNR slightly more slowly than wild type. This can be explained thermodynamically from a decrease in driving force due to the significant shift of 137 mV in the reduction potential value for the semiquinone/hydroquinone couple (E 1) of Y94A, relative to wild type (Lostao, A., Gómez-Moreno, C., Mayhew, S. G., and Sancho, J. (1997) Biochemistry 36, 14334–14344). The behavior of the rest of the mutants can be explained in the same way. Overall, our data indicate that Trp57 and Tyr94 do not play any active role in flavodoxin redox reactions providing a path for the electrons but are rather involved in setting an appropriate structural and electronic environment that modulates in vivo ET from PSI to FNR while providing a tight FMN binding.es
dc.description.sponsorshipComisión Interministerial de Ciencia y Tecnología BIO2000-1259, BQU2001-2520es
dc.description.sponsorshipDiputación General de Aragón P006/2000es
dc.description.sponsorshipDirección General de Estudios Superiores PB97-1027 and BMC 2001-2522es
dc.description.sponsorshipDirección General de Investigación BMC2000-0444es
dc.description.sponsorshipEuropean Union Networks ERB-FMRXCT98-0218 and HPRN-CT1999-00095es
dc.description.sponsorshipJunta de Andalucía CVI-0198es
dc.formatapplication/pdfes
dc.format.extent7 p.es
dc.language.isoenges
dc.publisherElsevieres
dc.relation.ispartofJournal of Biological Chemistry, 277 (25), 22338-22344.
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 Internacional*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/*
dc.titleAnabaena sp. PCC 7119 Flavodoxin as Electron Carrier from Photosystem I to Ferredoxin-NADP+Reductase: ROLE OF TRP57 AND TYR94es
dc.typeinfo:eu-repo/semantics/articlees
dcterms.identifierhttps://ror.org/03yxnpp24
dc.type.versioninfo:eu-repo/semantics/publishedVersiones
dc.rights.accessRightsinfo:eu-repo/semantics/openAccesses
dc.contributor.affiliationUniversidad de Sevilla. Departamento de Bioquímica Vegetal y Biología Moleculares
dc.relation.projectIDBIO2000-1259es
dc.relation.projectIDBQU2001-2520es
dc.relation.projectIDP006/2000es
dc.relation.projectIDPB97-1027es
dc.relation.projectIDBMC 2001-2522es
dc.relation.projectIDBMC2000-0444es
dc.relation.projectIDERB-FMRXCT98-0218es
dc.relation.projectIDHPRN-CT1999-00095es
dc.relation.projectIDCVI-0198es
dc.relation.publisherversionhttps://dx.doi.org/10.1074/jbc.M112258200es
dc.identifier.doi10.1074/jbc.M112258200es
dc.journaltitleJournal of Biological Chemistryes
dc.publication.volumen277es
dc.publication.issue25es
dc.publication.initialPage22338es
dc.publication.endPage22344es
dc.contributor.funderComisión Interministerial de Ciencia y Tecnología (CICYT). Españaes
dc.contributor.funderDiputación General de Aragónes
dc.contributor.funderMinisterio de Ciencia Y Tecnología (MCYT). Españaes
dc.contributor.funderEuropean Union (UE)es
dc.contributor.funderJunta de Andalucíaes

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