Structure-function studies of glutaredoxins and related oxidoreductases

@inproceedings{Elgn2008StructurefunctionSO,
  title={Structure-function studies of glutaredoxins and related oxidoreductases},
  author={Tobias H Elg{\'a}n},
  year={2008}
}
ABSTRACT The members of the ubiquitous group of thiol-disulfide oxidoreductases are characterized by a conserved tertiary structure, the thioredoxin (Trx) fold, and by having a consensus -C-X-X-C- active site sequence motif. By utilizing the active site cysteines, these proteins participate in redox reactions by catalyzing reversible disulfide oxidation and reduction. The glutaredoxin (Grx) subgroup and the group of protein disulfide oxidoreductases (PDOs) found in hyperthermophilic prokaryotes… CONTINUE READING

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