Por favor, use este identificador para citar o enlazar a este item:
http://hdl.handle.net/10261/11129
COMPARTIR / EXPORTAR:
SHARE CORE BASE | |
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE | |
Título: | Anabaena flavodoxin as an electron carrier from photosystem I to ferredoxin-NADP+ reductase. Role of flavodoxin residues in protein-protein interaction and electron transfer |
Autor: | Nogués, Isabel; Hervás, Manuel CSIC ORCID; Peregrina, José R.; Navarro, José A. CSIC ORCID ; Rosa, Miguel A. de la CSIC ORCID; Gómez-Moreno, Carlos; Medina, Milagros CSIC ORCID | Fecha de publicación: | 11-ene-2005 | Editor: | American Chemical Society | Citación: | Biochemistry 44(1): 97-104 (2005) | Resumen: | Biochemical and structural studies indicate that electrostatic and hydrophobic interactions are critical in the formation of optimal complexes for efficient electron transfer (ET) between ferredoxin-NADP+ reductase (FNR) and ferredoxin (Fd). Moreover, it has been shown that several charged and hydrophobic residues on the FNR surface are also critical for the interaction with flavodoxin (Fld), although, so far, no key residue on the Fld surface has been found to be the counterpart of such FNR side chains. In this study, negatively charged side chains on the Fld surface have been individually modified, either by the introduction of positive charges or by their neutralization. Our results indicate that although Glu16, Glu20, Glu61, Asp65, and Asp96 contribute to the orientation and optimization of the Fld interaction, either with FNR or with photosystem I (PSI) (presumably through the formation of salt bridges), for efficient ET, none of these side chains is involved in the formation of crucial salt bridges for optimal interaction with FNR. These data support the idea that the FNR−Fld interaction is less specific than the FNR−Fd interaction. However, analysis of the reactivity of these mutated Flds toward the membrane-anchored PSI complex indicated that all mutants, except Glu16Gln, lack the ability to form a stable complex with PSI. Thr12, Thr56, Asn58, and Asn97 are present in the close environment of the isoalloxazine ring of FMN in Anabaena Fld. Their roles in the interaction with and ET to FNR and PSI have also been studied. Mutants at these Fld positions indicate that residues in the close environment of the isoalloxazine ring modulate the ability of Fld to bind to and to exchange electrons with its physiological counterparts. | Descripción: | 10 pages, 4 figures, 6 tables.-- PMID: 15628849 [PubMed].-- Available online on Dec 4, 2004. | Versión del editor: | http://dx.doi.org/10.1021/bi048324d | URI: | http://hdl.handle.net/10261/11129 | DOI: | 10.1021/bi048324d | ISSN: | 0006-2960 |
Aparece en las colecciones: | (IBVF) Artículos |
Mostrar el registro completo
CORE Recommender
SCOPUSTM
Citations
21
checked on 17-abr-2024
WEB OF SCIENCETM
Citations
23
checked on 26-feb-2024
Page view(s)
464
checked on 23-abr-2024
Google ScholarTM
Check
Altmetric
Altmetric
NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.