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• W2000805812 abstract "Dehydroascorbate (DHA) is a higher oxidation state of ascorbate formed through its action as an intracellular antioxidant. The recycling of DHA back to ascorbate is thought to be catalyzed by a variety of enzymes, including protein disulfide isomerase (PDI), linking ascorbate metabolism to oxidative protein folding in the endoplasmic reticulum (ER). Here we examine the possible role of PDI as a dehydroascorbate reductase. We find the reaction too slow to be the major route for reduction of DHA in the ER, with a second-order rate constant for the reaction of reduced PDI with DHA of only 12.5 M−1s−1. Rates of a similar order of magnitude were obtained for other thioredoxin-superfamily members. However, glutaredoxin was able to catalyze DHA reduction more rapidly through a monothiol mechanism. In addition, DHA can rapidly react with many other dithiol systems, including dithiols in unfolded or partially folded proteins in a PDI-independent manner, with second-order rate constants of up to 186 M−1s−1. Furthermore, we identify borate as a potent inhibitor of catalyzed and noncatalyzed DHA reduction in vitro. This study both provides insights into the link between ascorbate metabolism and oxidative protein folding and suggests a novel link between ascorbate metabolism and borate toxicity. Antioxid. Redox Signal. 12, 15–25." @default.
• W2000805812 created "2016-06-24" @default.
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• W2000805812 date "2010-01-01" @default.
• W2000805812 modified "2023-09-27" @default.
• W2000805812 title "The Role of Dehydroascorbate in Disulfide Bond Formation" @default.
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• W2000805812 doi "https://doi.org/10.1089/ars.2009.2674" @default.
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