Thioredoxins (Trxs) are low-molecular-weight proteins that participate in the reduction of
target enzymes. Trxs contain a redox-active disulfide bond, in the form of a WCGPC amino …

Structural studies show that enzymes have a limited number of unique folds, although
structurally related enzymes have evolved to perform a large variety of functions. In this …

Flavin and redox-active disulfide domains of ferredoxin-dependent flavin thioredoxin
reductase (FFTR) homodimers should pivot between flavin-oxidizing (FO) and flavin …

Cyanobacteria evolved the ability to perform oxygenic photosynthesis using light energy to
reduce CO2 from electrons extracted from water and form nutrients. These organisms also …

Thioredoxins (Trxs) are disulfide oxidoreductases that regulate many biological processes.
The m-type thioredoxin (TrxA) is the only Trx present in all oxygenic photosynthetic …

Thioredoxin reductase (TR) regulates the intracellular redox environment by reducing
thioredoxin (Trx). In anaerobes, recent findings indicate that the Trx redox network is …

A recent report suggested that the thioredoxin-dependent metabolic regulation, which is
widespread in all domains of life, existed in methanogenic archaea about 3.5 billion years …

In the nitrogen-fixing cyanobacterium Anabaena sp. PCC 7120, glucose 6-phosphate
dehydrogenase (G6PDH) plays an important role in producing the power for reducing …

Flavoproteins participate in a wide variety of physiologically relevant processes that typically
involve redox reactions. Within this protein superfamily, there exists a group that is able to …

Thioredoxin reductases control the redox state of thioredoxins (Trxs)—ubiquitous proteins
that regulate a spectrum of enzymes by dithiol–disulfide exchange reactions. In most …