Logo du site
  • English
  • Français
  • Se connecter
Logo du site
  • English
  • Français
  • Se connecter
  1. Accueil
  2. Université de Neuchâtel
  3. Publications
  4. Ferredoxin/ferredoxin–thioredoxin reductase complex : Complete NMR mapping of the interaction site on ferredoxin by gallium substitution
 
  • Details
Options
Vignette d'image

Ferredoxin/ferredoxin–thioredoxin reductase complex : Complete NMR mapping of the interaction site on ferredoxin by gallium substitution

Auteur(s)
Xu, Xingfu
Editeur(s)
Kim, Sung-Kun
Schürmann, Peter
Hirasawa, Masakazu
Tripathy, Jatindra N.
Smith, Jody
Knaff, David B.
Ubbink, Marcellus
Date de parution
2006-12-11
In
FEBS Letters, Elsevier, 2006/580/28-29/6714-6720
Mots-clés
  • [2Fe–2S] Ferredoxin

  • Ferredoxin–thioredoxi...

  • Chemical shift pertur...

Résumé
The reduction of ferredoxin–thioredoxin reductase (FTR) by plant-type ferredoxin plays an important role in redox regulation in plants and cyanobacteria. Nuclear magnetic resonance (NMR) was used to map the binding sites on <i>Synechocystis</i> ferredoxin for FTR. A gallium-substituted structural analog of this [2Fe–2S] ferredoxin was obtained by reconstituting the apoprotein in a refolding buffer containing gallium. For the first time, the complete interaction interface of a [2Fe–2S] ferredoxin with a target enzyme has been mapped by NMR chemical shift perturbation with this diamagnetic structural analog.
URI
https://libra.unine.ch/handle/123456789/18251
DOI
10.1016/j.febslet.2006.11.027
Autre version
http://dx.doi.org/10.1016/j.febslet.2006.11.027
Type de publication
Resource Types::text::journal::journal article
Dossier(s) à télécharger
 main article: Xu_Xingfu_-_Ferredoxin_ferredoxin-thioredoxin_reductase_20070105.pdf (972.47 KB)
google-scholar
Présentation du portailGuide d'utilisationStratégie Open AccessDirective Open Access La recherche à l'UniNE Open Access ORCID

Adresse:
UniNE, Service information scientifique & bibliothèques
Rue Emile-Argand 11
2000 Neuchâtel

Construit avec Logiciel DSpace-CRIS Maintenu et optimiser par 4Sciences

  • Paramètres des témoins de connexion
  • Politique de protection de la vie privée
  • Licence de l'utilisateur final