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- W1434807704 abstract "This chapter focuses on the thioredoxin system. Thioredoxin is a small, ubiquitous redox protein with an active center cystine disulfide/dithiol. It may function in several oxidation-reduction reactions and have a regulatory role. For example, it can act as a protein-disulfide reductase and as a hydrogen donor to ribonucleotide reductase, it is required for the activity of DNA polymerase of bacteriophage T7 and for filamentous phage assembly, and it may regulate the activities of certain enzymes. Photosynthetically reduced ferredoxin, ferredoxin-thioredoxin reductase, and thioredoxin (the ferredoxin/thioredoxin system) provide a means whereby light can be linked to enzyme modulation, probably through the reduction of disulfides of the modulated enzymes. Such a mechanism of regulation is necessary because, in the cytoplasm of the cyanobacterial cell, enzymes of CO2 fixation and carbohydrate degradation coexist and their activities must be adjusted to meet the varying metabolic needs of the cell. Thioredoxins have been shown to occur in a wide range of cyanobacteria. Cyanobacteria, like plant chloroplasts, have two thioredoxins, designated f and m, which selectively modulate certain enzymes, and a ferredoxin-thioredoxin reductase. Thioredoxin m is considered in this chapter. Several potential functions of cyanobacterial thioredoxin m have been established, although the true physiological function(s) remains to be firmly established." @default.
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- W1434807704 date "1988-01-01" @default.
- W1434807704 modified "2023-09-26" @default.
- W1434807704 title "[42] Thioredoxin system" @default.
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- W1434807704 doi "https://doi.org/10.1016/0076-6879(88)67045-5" @default.
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