Human thioredoxin electron-transfer protein

We examined another system, an electron-transfer protein human thioredoxin (hTrx). Figure 31 shows the X-ray structure of oxidized hTrx at 2.1 A resolution [192, 193]. hTrx is a compact globular protein with a central core of five strands... 

On the other hand ferredoxin and thioredoxin are ubiquitous proteins present in bacteria, algae, plants and animals. This paper shows and discusses the effect of animal ferredoxin (ad enodoxin, ADX) and human lymphocyte thioredoxin (HTR) in several electron transfer reactions. 

Six human GSH peroxidases have been identified. Most of the enzymes contain selenocysteine in the active site, with the exceptions of GPX 5 and 6 (Burk, 1997). Some GSH transferase enzymes also display low GSH peroxidase activity (Ketterer and Meyer, 1989). Thioredoxin, a low iron-sulfur protein, can also transfer electrons (instead of GSH in some cases). Some GSH peroxidases are extracellular and function in plasma. 

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