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Author Spotlight: Advancing Structural and Biochemical Studies of Proteins Through Thermal Shift Assays
Published on: August 9, 2024
Selenoprotein K form an intermolecular diselenide bond with unusually high redox potential
Jun Liu1, Zhengqi Zhang1, Sharon Rozovsky1
1Department of Chemistry and Biochemistry, University of Delaware, Newark, DE 19716, United States.
Abstract:
Selenoprotein K (SelK) is a membrane protein involved in antioxidant defense, calcium regulation and the ER-associated protein degradation pathway. We found that SelK exhibits a peroxidase activity with a rate that is low but within the range of other peroxidases. Notably, SelK reduced hydrophobic substrates, such as phospholipid hydroperoxides, which damage membranes. Thus, SelK might be involved in membrane repair or related pathways. SelK was also found to contain a diselenide bond-the first intramolecular bond of that kind reported for a selenoprotein. The redox potential of SelK was -257 mV, significantly higher than that of diselenide bonds in small molecules or proteins. Consequently, SelK can be reduced by thioredoxin reductase. These finding are essential for understanding SelK activity and function.
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