Ontology highlight
ABSTRACT:
SUBMITTER: Ukuwela AA
PROVIDER: S-EPMC5885593 | biostudies-literature | 2018 Feb
REPOSITORIES: biostudies-literature
Ukuwela Ashwinie A AA Bush Ashley I AI Wedd Anthony G AG Xiao Zhiguang Z
Chemical science 20171206 5
Glutaredoxins (Grxs) are a family of glutathione (GSH)-dependent thiol-disulfide oxidoreductases. They feature GSH-binding sites that directly connect the reversible redox chemistry of protein thiols to the abundant cellular nonprotein thiol pool GSSG/GSH. This work studied the pathways for oxidation of protein dithiols P(SH)<sub>2</sub> and reduction of protein disulfides P(SS) catalyzed by <i>Homo sapiens</i> HsGrx1 and <i>Escherichia coli</i> EcGrx1. The metal-binding domain HMA4n(SH)<sub>2</ ...[more]