The name thioredoxin (Trx) was first introduced by Peter Reichard for the enzyme providing electrons needed for the enzymatic reaction of ribonucleotide reductase, in 1964 (Buchanan et al. 2012). However, Trxs have been described in yeast before, using different names: fraction C of the sulfate-reducing system and enzyme II of the enzymatic system reducing L-methionine sulfoxide. E. coli Trx1 was sequenced in 1968, revealing the characteristic Cys-Gly-Pro-Cys active site motif. In 1975, the crystal structure of oxidized E. coli Trx1 was solved, describing the characteristic Trx fold for the first time. The role of essential plant proteins for the process of photosynthesis, identified as Trxs in 1976–1978, is one of the first descriptions of biological redox regulation (Buchanan et al. 2012). All these mentioned early advances...
KeywordsRedox Regulation Methionine Sulfoxide Active Site Cysteine Active Site Motif Trx1 Level
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