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.
Xu
Xingfu
X
Leiden Institute of Chemistry, Leiden University, Gorlaeus Laboratories, P.O. Box 9502, 2300 RA Leiden, The Netherlands.
Kim
Sung-Kun
SK
Schürmann
Peter
P
Hirasawa
Masakazu
M
Tripathy
Jatindra N
JN
Smith
Jody
J
Knaff
David B
DB
Ubbink
Marcellus
M
D000595:Amino Acid Sequence; D001665:Binding Sites; D005288:Ferredoxins / Q000737:chemistry / Q000378:metabolism*; D005708:Gallium / Q000378:metabolism*; D007506:Iron-Sulfur Proteins / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D010088:Oxidoreductases / Q000737:chemistry / Q000378:metabolism*; D046939:Synechocystis / Q000201:enzymology*; D017186:Titrimetry
D005288:Ferredoxins; D007506:Iron-Sulfur Proteins; D005708:Gallium; D010088:Oxidoreductases; C021588:ferredoxin-thioredoxin reductase