Abstract
As has previously been demonstrated for ferredoxin/NADP+ oxidoreductase (NADP+ reductase) and ferredoxin/nitrite oxidoreductase (nitrite reductase), ferrodoxin-dependent glutamate synthase has been shown to form a complex with ferredoxin. The complex (Kd = 14.5 μM) is stabilized by electrostatic forces and produces changes in the chromophore(s) of at least one of the proteins. Chemical modification of carboxyl groups on ferredoxin with glycine ethyl ester in the presence of a water-soluble carbodiimide affected the binding of ferredoxin to both glutamate synthase and nitrite reductase and also inhibited the ability of reduced ferredoxin to serve as an electron donor to both enzymes.
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