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

Authors
Journal
FEBS Letters
0014-5793
Publisher
Wiley Blackwell (John Wiley & Sons)
Publication Date
Volume
580
Identifiers
DOI: 10.1016/j.febslet.2006.11.027
Keywords
  • [2Fe–2S] Ferredoxin
  • Ferredoxin–Thioredoxin Reductase
  • Chemical Shift Perturbation
Disciplines
  • Biology
  • Chemistry

Abstract

Abstract 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.

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