Journal
BIOCHEMISTRY
Volume 47, Issue 27, Pages 6985-6987Publisher
AMER CHEMICAL SOC
DOI: 10.1021/bi8008906
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Funding
- NIGMS NIH HHS [1 F32 GM071126-01A1] Funding Source: Medline
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The production of recombinant, disulfide-containing proteins often requires oxidative folding in vitro. Here, we show that diselenides, such as selenoglutathione, catalyze oxidative protein folding by O(2). Substantially lower concentrations of a redox buffer composed of selenoglutathione and the thiol form of glutathione can consequently be used to achieve the same rate and yield of folding as a standard glutathione redox buffer. Further, the low pK(a) of selenols extends the pH range for folding by selenoglutathione to acidic conditions, where glutathione is inactive. Harnessing the catalytic power of diselenides may thus pave the way for more efficient oxidative protein folding.
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