Faculté des sciences

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

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

In: FEBS Letters, 2006, vol. 580, no. 28-29, p. 6714-6720

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... More

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    Summary
    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.