ArticleNature communications2017
Glutaredoxin catalysis requires two distinct glutathione interaction sites.
Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed, 109 citations in OpenAlex.
- Emerging roles of glutaredoxins in plant metabolism.Journal of experimental botany · 2026Review
- Molecular Analysis of Two CC-Type Glutaredoxins from the Model LegumeInternational journal of molecular sciences · 2026Article
- Making HEDS or tails of glutaredoxin catalysis: Direct reduction of bis(2-hydroxyethyl) disulfide as a non-glutathione disulfide substrate.Redox biology · 2026Article
- Genome-wide identification and expression analysis under selenium stress of glutaredoxin system genes in Cardamine hupingshanensis.BMC plant biology · 2026Article
- Bicyclic Selenenyl Sulfides with Tuned Bioreductive Step Rates Reveal Constraints for Probes Targeting Thioredoxin Reductase.Angewandte Chemie (International ed. in English) · 2025Article
- Structural Adaptations of Bacterial Grx3 to Temperature: Pro29 Is Essential for Cold Adaptation inACS omega · 2025Article
- Molecular basis for the enzymatic inactivity of class III glutaredoxin ROXY9 on standard glutathionylated substrates.Nature communications · 2025Article
- The ascorbate-glutathione cycle coming of age.Journal of experimental botany · 2024Review
- Ageing-dependent thiol oxidation reveals early oxidation of proteins with core proteostasis functions.Life science alliance · 2024Article
- Deciphering the mechanism of glutaredoxin-catalyzed roGFP2 redox sensing reveals a ternary complex with glutathione for protein disulfide reduction.Nature communications · 2024Article
- Chloroplasts lacking class I glutaredoxins are functional but show a delayed recovery of protein cysteinyl redox state after oxidative challenge.Redox biology · 2024Article
- Redox regulation, thioredoxins, and glutaredoxins in retrograde signalling and gene transcription.Journal of experimental botany · 2023Review
- Glutathione and Glutaredoxin-Key Players in Cellular Redox Homeostasis and Signaling.Antioxidants (Basel, Switzerland) · 2023Review
- Chemistry and biology of enzymes in protein glutathionylation.Current opinion in chemical biology · 2023Review
- Structural and functional fine mapping of cysteines in mammalian glutaredoxin reveal their differential oxidation susceptibility.Nature communications · 2023Article
- Response and Tolerance ofPlants (Basel, Switzerland) · 2023Article
- Tyr76 is essential for the cold adaptation of a class II glutaredoxin 4 with a heat-labile structure from the Arctic bacterium Sphingomonas sp.FEBS open bio · 2023Article
- Glutathione-Related Enzymes and Proteins: A Review.Molecules (Basel, Switzerland) · 2023Review
- Article
- Quantification of Redox-Sensitive GFP Cysteine Redox State via Gel-Based Read-Out.Methods in molecular biology (Clifton, N.J.) · 2023Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Glutaredoxins are key players in cellular redox homoeostasis and exert a variety of essential functions ranging from glutathione-dependent catalysis to iron metabolism. The exact structure-function relationships and mechanistic differences among glutaredoxins that are active or inactive in standard enzyme assays have so far remained elusive despite numerous kinetic and structural studies. Here, we elucidate the enzymatic mechanism showing that glutaredoxins require two distinct glutathione interaction sites for efficient redox catalysis. The first site interacts with the glutathione moiety of glutathionylated disulfide substrates. The second site activates glutathione as the reducing agent. We propose that the requirement of two distinct glutathione interaction sites for the efficient reduction of glutathionylated disulfide substrates explains the deviating structure-function relationships, activities and substrate preferences of different glutaredoxin subfamilies as well as thioredoxins. Our model also provides crucial insights for the design or optimization of artificial glutaredoxins, transition-state inhibitors and glutaredoxin-coupled redox sensors.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.