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

doi:10.1016/j.febslet.2006.11.027

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

Laboratoire de biologie moléculaire et cellulaire

Hirasawa, Masakazu

Tripathy, Jatindra N.

Smith, Jody

Knaff, David B.

Ubbink, Marcellus

Date issued

December 11, 2006

In

FEBS Letters, Elsevier, 2006/580/28-29/6714-6720

Subjects

[2Fe–2S] Ferredoxin Ferredoxin–thioredoxin reductase Chemical shift perturbation

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 <i>Synechocystis</i> 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.