Catalysis of oxidative protein folding by small-molecule diselenides

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 thi...

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Bibliographic Details
Published in:Biochemistry (Easton) Vol. 47; no. 27; p. 6985
Main Authors: Beld, Joris, Woycechowsky, Kenneth J, Hilvert, Donald
Format: Journal Article
Language:English
Published: United States 08.07.2008
Subjects:
Catalysis
Glutathione - metabolism
Kinetics
Oxidation-Reduction
Protein Folding
Ribonuclease, Pancreatic - chemistry
Ribonuclease, Pancreatic - metabolism
Selenium Compounds - metabolism
ISSN:1520-4995, 1520-4995
Online Access:Get more information
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Summary: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 p K 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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ISSN:1520-4995
1520-4995
DOI:10.1021/bi8008906