A Thioredoxin-Mediated Activation of Glutamine Synthetase and Glutamate Synthase in Synchronous Chlorella sorokiniana.

The effects of thioredoxin, dithioerythrol, and mixtures of both on enzymes involved in N metabolism of Chlorella sorokiniana have been studied. Glutamine synthetase, inactivated in vivo, was activated 8-fold by thioredoxin and dithioerythrol. By the same treatment, the activity of glutamate synthase was stimulated nearly 4-fold. Thus, two key enzymes of N metabolism were shown to be regulated via thioredoxin. The enzymes of the nitrate reducing system, i.e. nitrate reductase and nitrite reductase, were not affected by thiols. From these results, a model of NO(3) (-) metabolism is put forward which considers the regulating effect of light.