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

被引：20

作者：

Xu, Xingfu

Kim, Sung-Kun

Schurmann, Peter

Hirasawa, Masakazu

Tripathy, Jatindra N.

Smith, Jody

Knaff, David B.

Ubbink, Marcellus

机构：

[1] Leiden Univ, Gorlaeus Labs, Leiden Inst Chem, NL-2300 RA Leiden, Netherlands

[2] Texas Tech Univ, Dept Chem & Biochem, Lubbock, TX 79409 USA

[3] Univ Neuchatel, Biol Cellulaire & Mol Lab, CH-2009 Neuchatel, Switzerland

[4] Texas Tech Univ, Ctr Biotechnol & Genom, Lubbock, TX 79409 USA

来源：

FEBS LETTERS | 2006年 / 580卷 / 28-29期

关键词：

2Fe-2S] ferredoxin; ferredoxin-thioredoxin reductase; chemical shift perturbation;

D O I：

10.1016/j.febslet.2006.11.027

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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. (c) 2006 Federation of European Biochemical Societies.

引用

页码：6714 / 6720

页数：7

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