University thesis:
Dissertation, Georg-August-Universität Göttingen, 2022
Footnote:
Description:
Glutaredoxins are small proteins with a conserved thioredoxin fold. This fold allows for two functions, depending on the sequence of the active site. Class I glutaredoxins, which are characterized by a CPYC motif, show oxidoreductase activity and serve to control the redox status of reactive thiols in proteins under conditions of oxidative stress. The tripeptide glutathione serves as a cofactor for the underlying redox reactions. Class II glutaredoxins, which encode a highly conserved CGFS motif, are instrumental for the assembly and transfer of Fe-S-clusters. Here, the co-factor glutathion...