English   español  
Por favor, use este identificador para citar o enlazar a este item: http://hdl.handle.net/10261/96769
COMPARTIR / IMPACTO:
Estadísticas
logo share SHARE logo core CORE   Add this article to your Mendeley library MendeleyBASE

Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar a otros formatos:
Título

Communication between L-galactono-1,4-lactone dehydrogenase and cytochrome c

AutorHervás, Manuel ; Bashir, Qamar; Leferink, Nicole G.H.; Ferreira, Patricia ; Moreno-Beltrán, Blas ; Westphal, Adrie H.; Díaz-Moreno, Irene ; Medina, Milagros; Rosa, Miguel A. de la ; Ubbink, Marcellus; Navarro, José A. ; van Berkel, Willem, J.H.
Palabras claveCytochrome c
Electron transfer
Flavoprotein
Protein-protein interaction
Vitamin c
Fecha de publicación2013
EditorJohn Wiley & Sons
CitaciónFEBS Journal, 280(8): 1830-1840 (2013)
Resumenl-galactono-1,4-lactone dehydrogenase (GALDH) catalyzes the terminal step of vitamin C biosynthesis in plant mitochondria. Here we investigated the communication between Arabidopsis thaliana GALDH and its natural electron acceptor cytochrome c (Cc). Using laser-generated radicals we observed the formation and stabilization of the GALDH semiquinone anionic species (GALDHSQ). GALDHSQ oxidation by Cc exhibited a nonlinear dependence on Cc concentration consistent with a kinetic mechanism involving protein–partner association to form a transient bimolecular complex prior to the electron transfer step. Oxidation of GALDHSQ by Cc was significantly impaired at high ionic strength, revealing the existence of attractive charge–charge interactions between the two reactants. Isothermal titration calorimetry showed that GALDH weakly interacts with both oxidized and reduced Cc. Chemical shift perturbations for 1H and 15N nuclei of Cc, arising from the interactions with unlabeled GALDH, were used to map the interacting surface of Cc. For Arabidopsis Cc and yeast Cc, similar residues are involved in the interaction with GALDH. These residues are confined to a single surface surrounding the heme edge. The range of chemical shift perturbations for the physiological Arabidopsis Cc–GALDH complex is larger than that of the non-physiological yeast Cc–GALDH complex, indicating that the former complex is more specific. In summary, the results point to a relatively low affinity GALDH–Cc interaction, similar for all partner redox states, involving protein–protein dynamic motions. Evidence is also provided that Cc utilizes a conserved surface surrounding the heme edge for the interaction with GALDH and other redox partners.
URIhttp://hdl.handle.net/10261/96769
DOI10.1111/febs.12207
Aparece en las colecciones: (IBVF) Artículos
Ficheros en este ítem:
Fichero Descripción Tamaño Formato  
Hervas_FEBSJ_2013.pdf2,21 MBAdobe PDFVista previa
Visualizar/Abrir
Mostrar el registro completo
 

Artículos relacionados:


NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.