ArticleBioscience reports2015
The glutaredoxin mono- and di-thiol mechanisms for deglutathionylation are functionally equivalent: implications for redox systems biology.
Article in Bioscience reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Disulfide stress and its role in cardiovascular diseases.Redox biology · 2024Review
- More than Just Antioxidants: Redox-Active Components and Mechanisms Shaping Redox Signalling Network.Antioxidants (Basel, Switzerland) · 2022Review
- Structure of BrxA from Staphylococcus aureus, a bacilliredoxin involved in redox homeostasis in Firmicutes.Acta crystallographica. Section F, Structural biology communications · 2022Article
- Can thiol-based redox systems be utilized as parts for synthetic biology applications?Redox report : communications in free radical research · 2021Article
- Ectopic Expression of a Heterologous Glutaredoxin Enhances Drought Tolerance and Grain Yield in Field Grown Maize.International journal of molecular sciences · 2021Article
- Stoichiometric Thiol Redox Proteomics for Quantifying Cellular Responses to Perturbations.Antioxidants (Basel, Switzerland) · 2021Review
- Article
- Role of Glutaredoxin-1 and Glutathionylation in Cardiovascular Diseases.International journal of molecular sciences · 2020Review
- The role of thiols in antioxidant systems.Free radical biology & medicine · 2019Review
- A glutaredoxin domain fused to the radical-generating subunit of ribonucleotide reductase (RNR) functions as an efficient RNR reductant.The Journal of biological chemistry · 2018Article
- The thioredoxin system and not the Michaelis-Menten equation should be fitted to substrate saturation datasets from the thioredoxin insulin assay.Redox report : communications in free radical research · 2016Article
- Systematic re-evaluation of the bis(2-hydroxyethyl)disulfide (HEDS) assay reveals an alternative mechanism and activity of glutaredoxins.Chemical science · 2015Article
Corrections and comments
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Authors and funding
3 authors.
Funding
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Abstract
Glutathionylation plays a central role in cellular redox regulation and anti-oxidative defence. Grx (Glutaredoxins) are primarily responsible for reversing glutathionylation and their activity therefore affects a range of cellular processes, making them prime candidates for computational systems biology studies. However, two distinct kinetic mechanisms involving either one (monothiol) or both (dithiol) active-site cysteines have been proposed for their deglutathionylation activity and initial studies predicted that computational models based on either of these mechanisms will have different structural and kinetic properties. Further, a number of other discrepancies including the relative activity of active-site mutants and contrasting reciprocal plot kinetics have also been reported for these redoxins. Using kinetic modelling, we show that the dithiol and monothiol mechanisms are identical and, we were also able to explain much of the discrepant data found within the literature on Grx activity and kinetics. Moreover, our results have revealed how an apparently futile side-reaction in the monothiol mechanism may play a significant role in regulating Grx activity in vivo.
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