PMID:10593884
| Citation |
Shi, J, Vlamis-Gardikas, A, Aslund, F, Holmgren, A and Rosen, BP (1999) Reactivity of glutaredoxins 1, 2, and 3 from Escherichia coli shows that glutaredoxin 2 is the primary hydrogen donor to ArsC-catalyzed arsenate reduction. J. Biol. Chem. 274:36039-42 |
|---|---|
| Abstract |
In Escherichia coli ArsC catalyzes the reduction of arsenate to arsenite using GSH with glutaredoxin as electron donors. E. coli has three glutaredoxins: 1, 2, and 3, each with a classical -Cys-Pro-Tyr-Cys- active site. Glutaredoxin 2 is the major glutathione disulfide oxidoreductase in E. coli, but its function remains unknown. In this report glutaredoxin 2 is shown to be the most effective hydrogen donor for the reduction of arsenate by ArsC. Analysis of single or double cysteine-to-serine substitutions in the active site of the three glutaredoxins indicated that only the N-terminal cysteine residue is essential for activity. This suggests that, during the catalytic cycle, ArsC forms a mixed disulfide with GSH before being reduced by glutaredoxin to regenerate the active ArsC reductase. |
| Links | |
| Keywords |
Arsenates/metabolism; Arsenites/metabolism; Bacterial Proteins/metabolism; Electron Transport; Escherichia coli/metabolism; Glutaredoxins; Hydrogen/metabolism; Oxidoreductases; Proteins/metabolism |
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