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

Xingfu Xu, Sung Kun Kim, Peter Schürmann, Masakazu Hirasawa, Jatindra N. Tripathy, Jody Smith, David B. Knaff, Marcellus Ubbink

Research output: Contribution to journalArticle

22 Scopus citations

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.

Original languageEnglish
Pages (from-to)6714-6720
Number of pages7
JournalFEBS Letters
Volume580
Issue number28-29
DOIs
StatePublished - Dec 11 2006

Keywords

  • Chemical shift perturbation
  • Ferredoxin-thioredoxin reductase
  • [2Fe-2S] Ferredoxin

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