Abstract
Ferredoxin-thioredoxin reductase formed an electrostatically stabilized 1:1 complex with ferredoxin. Complex formation could be detected, following mixing of the two proteins, either by changes in optical absorbance and circular dichroism spectra or by co-chromatography during gel filtration. Chemical modification of three or four carboxyl groups on ferredoxin, which had previously been shown to inhibit the binding of ferredoxin to several ferredoxin-dependent chloroplast enzymes, had little effect on its interaction with ferredoxin-thioredoxin reductase. The results suggest that the ferredoxin domain that binds ferredoxin-thioredoxin reductase is not completely identical to that involved in binding other ferredoxin-dependent enzymes.
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