Flavodoxin: A compromise between efficiency and versatility in the electron transfer from Photosystem I to Ferredoxin-NADP(+) reductase.
Goñí, Guillermina ; Herguedas, Beatriz (Universidad de Zaragoza) ; Hervás, Manuel ; Peregrina, José R. ; de la Rosa, Miguel A. ; Gómez-Moreno, Carlos (Universidad de Zaragoza) ; Navarro, José A. ; Hermoso, Juan A. ; Martínez-Júlvez, Marta (Universidad de Zaragoza) ; Medina, Milagros (Universidad de Zaragoza)
Resumen: Under 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.
Idioma: Inglés
DOI: 10.1016/j.bbabio.2008.12.006
Año: 2009
Publicado en: BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS 1787, 3 (2009), 144-154
ISSN: 0005-2728
Factor impacto JCR: 3.688 (2009)
Categ. JCR: BIOPHYSICS rank: 18 / 74 = 0.243 (2009) - Q1 - T1
Categ. JCR: BIOCHEMISTRY & MOLECULAR BIOLOGY rank: 87 / 281 = 0.31 (2009) - Q2 - T1
Tipo y forma: Article (PostPrint)
Área (Departamento): Área Bioquímica y Biolog.Mole. (Dpto. Bioq.Biolog.Mol. Celular)
You must give appropriate credit, provide a link to the license, and indicate if changes were made. You may do so in any reasonable manner, but not in any way that suggests the licensor endorses you or your use. You may not use the material for commercial purposes. If you remix, transform, or build upon the material, you may not distribute the modified material.
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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.
Idioma: Inglés
DOI: 10.1016/j.bbabio.2008.12.006
Año: 2009
Publicado en: BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS 1787, 3 (2009), 144-154
ISSN: 0005-2728
Factor impacto JCR: 3.688 (2009)
Categ. JCR: BIOPHYSICS rank: 18 / 74 = 0.243 (2009) - Q1 - T1
Categ. JCR: BIOCHEMISTRY & MOLECULAR BIOLOGY rank: 87 / 281 = 0.31 (2009) - Q2 - T1
Tipo y forma: Article (PostPrint)
Área (Departamento): Área Bioquímica y Biolog.Mole. (Dpto. Bioq.Biolog.Mol. Celular)
You must give appropriate credit, provide a link to the license, and indicate if changes were made. You may do so in any reasonable manner, but not in any way that suggests the licensor endorses you or your use. You may not use the material for commercial purposes. If you remix, transform, or build upon the material, you may not distribute the modified material. Exportado de SIDERAL (2026-01-28-11:24:54)
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Record created 2026-01-23, last modified 2026-01-28