Abstract
It has been known for many years that reducing equivalents produced by photosynthetic electron transport reaction are not only used to promote carbon fixation reactions, but they also act as important factors which modulate the four important enzyme's activities in the Calvin-cycle. Redox regulated enzymes were first discovered by chance, when reducing agents were found to be required to maintain their activity in vitro. Following the completion of the genome sequence of A.thaliana in 2000, investigation into the interaction between such proteins has been studied in practice, with the thioredoxin family, now known to mediate the transfer of reducing equivalents, becoming a prime object of the research. In 2001, we reported an efficient method to comprehensively identify partner proteins which interact with thioredoxin. Many proteins which participate in redox reaction were discovered using this approach. The complex system which encompasses the redox regulation of metabolism, or 'redox network', is presented.
