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Ferredoxin/ferredoxin–thioredoxin reductase complex : Complete NMR mapping of the interaction site on ferredoxin by gallium substitution
Auteur(s)
Xu, Xingfu
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
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.
Identifiants
Type de publication
journal article
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