ArticleAntioxidants (Basel, Switzerland)2022
Oxidized Forms of Ergothioneine Are Substrates for Mammalian Thioredoxin Reductase.
Article in Antioxidants (Basel, Switzerland), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 20 citations in OpenAlex.
- Effect of Ergothioneine on the Stability of Hyaluronic Acid-Based Wound-Healing Materials.Polymers · 2026Article
- CH•••S hydrogen bonds drive molecular recognition of ergothioneine by the microbial transporter.Science advances · 2026Article
- Expression and purification of the intact bacterial ergothioneine transporter EgtU.Protein expression and purification · 2025Article
- The Effects of Antioxidant Approved Drugs and Under Investigation Compounds with Potential of Improving Sleep Disorders and their Associated Comorbidities Associated with Oxidative Stress and Inflammation.Mini reviews in medicinal chemistry · 2025Review
- Exogenous Ergothioneine and Glutathione Limit Postharvest Senescence of Arugula.Antioxidants (Basel, Switzerland) · 2024Article
- The Role of Ergothioneine in Red Blood Cell Biology: A Review and Perspective.Antioxidants (Basel, Switzerland) · 2024Review
- Impact of aging and ergothioneine pre-treatment on naphthalene toxicity in lung.Toxicology letters · 2024Article
- Selenium vitaminology: The connection between selenium, vitamin C, vitamin E, and ergothioneine.Current opinion in chemical biology · 2023Review
- Ergothioneine: an underrecognised dietary micronutrient required for healthy ageing?The British journal of nutrition · 2023Review
- Discovery and structure of a widespread bacterial ABC transporter specific for ergothioneine.Nature communications · 2022Article
- Computational Insights into the Regeneration of Ovothiol and Ergothioneine and Their Selenium Analogues by Glutathione.ACS omega · 2022Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Ergothioneine (EGT) is a sulfur-containing amino acid analog that is biosynthesized in fungi and bacteria, accumulated in plants, and ingested by humans where it is concentrated in tissues under oxidative stress. While the physiological function of EGT is not yet fully understood, EGT is a potent antioxidant in vitro. Here we report that oxidized forms of EGT, EGT-disulfide (ESSE) and 5-oxo-EGT, can be reduced by the selenoenzyme mammalian thioredoxin reductase (Sec-TrxR). ESSE and 5-oxo-EGT are formed upon reaction with biologically relevant reactive oxygen species. We found that glutathione reductase (GR) can reduce ESSE, but only with the aid of glutathione (GSH). The reduction of ESSE by TrxR was found to be selenium dependent, with non-selenium-containing TrxR enzymes having little or no ability to reduce ESSE. In comparing the reduction of ESSE by Sec-TrxR in the presence of thioredoxin to that of GR/GSH, we find that the glutathione system is 10-fold more efficient, but Sec-TrxR has the advantage of being able to reduce both ESSE and 5-oxo-EGT directly. This represents the first discovered direct enzymatic recycling system for oxidized forms of EGT. Based on our in vitro results, the thioredoxin system may be important for EGT redox biology and requires further in vivo investigation.
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Registered trials
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