| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 2052185 | FEBS Letters | 2006 | 7 Pages |
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.
Keywords
Related Topics
Life Sciences
Agricultural and Biological Sciences
Plant Science
Authors
Xingfu Xu, Sung-Kun Kim, Peter Schürmann, Masakazu Hirasawa, Jatindra N. Tripathy, Jody Smith, David B. Knaff, Marcellus Ubbink,