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Ferredoxin/ferredoxin–thioredoxin reductase complex: Complete NMR mapping of the interaction site on ferredoxin by gallium substitution
Author(s) -
Xu Xingfu,
Kim Sung-Kun,
Schürmann Peter,
Hirasawa Masakazu,
Tripathy Jatindra N.,
Smith Jody,
Knaff David B.,
Ubbink Marcellus
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.11.027
Subject(s) - ferredoxin , ferredoxin thioredoxin reductase , chemistry , reductase , biochemistry , stereochemistry , thioredoxin reductase , enzyme , thioredoxin
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 Synechocystis 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.