Characterization of spinach ferredoxin-thioredoxin reductase.
Ferredoxin-thioredoxin reductase (FTR) is an iron-sulfur protein which, in the presence of ferredoxin and thioredoxin, catalyses the activation of photosynthetic enzymes such as fructose-1,6-bisphosphatase, NADP-malate dehydrogenase and several others. The results from amino acid composition and N- and C-terminal sequences show that spinach FTR is composed of two nonidentical subunits (mol.wt. = 17,200: A; 15,500:B) present in equal amounts. Other components (mol. wt. = 16,300 and 14,200) observed in preparations are most likely derived from subunit A losing its amino terminal part. We report the amino acid compositions of the two subunits A and B of FTR including their partial terminal sequences. Subunit A has an additional amino-terminal serine-rich sequence which is phosphorylated.