Ferredoxin/ferredoxin–thioredoxin reductase complex: Complete NMR mapping of the interaction site on ferredoxin by gallium substitution
Copyright policy )Ferredoxin/ferredoxin–thioredoxin reductase complex: Complete NMR mapping of the interaction site on ferredoxin by gallium substitution
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.
- Leiden University Netherlands
- UNIVERSITEIT LEIDEN Netherlands
- Leiden University - Leiden Institute of Chemistry Netherlands
- Texas A&M University United States
- The University of Texas System United States
Iron-Sulfur Proteins, Models, Molecular, Binding Sites, Molecular Sequence Data, Synechocystis, Titrimetry, Gallium, Chemical shift perturbation, Ferredoxins, Amino Acid Sequence, Ferredoxin–thioredoxin reductase, Oxidoreductases, Nuclear Magnetic Resonance, Biomolecular, [2Fe–2S] Ferredoxin
Iron-Sulfur Proteins, Models, Molecular, Binding Sites, Molecular Sequence Data, Synechocystis, Titrimetry, Gallium, Chemical shift perturbation, Ferredoxins, Amino Acid Sequence, Ferredoxin–thioredoxin reductase, Oxidoreductases, Nuclear Magnetic Resonance, Biomolecular, [2Fe–2S] Ferredoxin
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