Abstract
Part of the Ferredoxin-Thioredoxin system, ferredoxin:thioredoxin reductase (FTR) plays a major role in the regulation of key enzymes in oxygenic photosynthesis (1). In the presence of light, a chain of reduction-oxidation reactions occurs among ferredoxin, FTR and thioredoxin respectively, which converts an electron signal into a thiol signal (2). The latter is essential in the reduction of target enzymes, which in turn become activated in the case of biosynthetic enzymes, or inactivated in the case of degradatory enzymes. FTRs from different organisms have been studied and show two dissimilar subunits: the variable subunit (or subunit A) differs in size within species whereas the catalytic subunit (or subunit B) is constant at 13 kDa and carries a [4Fe-4S] cluster and the catalytically active disulfide bridge (3).
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