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Human Mitochondrial Glutaredoxin Reduces S-Glutathionylated Proteins with High Affinity Accepting Electrons from Either Glutathione or Thioredoxin Reductase
Open accessAbstract
Glutaredoxins catalyze glutathione-dependent thiol disulfide oxidoreductions via a GSH-binding site and active cysteines. Recently a second human glutaredoxin (Grx2), which is targeted to either mitochondria or the nucleus, was cloned. Grx2 contains the active site sequence CSYC, which is different from the conserved CPYC motif present in the cytosolic Grx1. Here we have compared the activity of Grx2 and Grx1 using glutathionylated substrates and active site mutants. The kinetic studies showed that Grx2 catalyzes the reduction of glutathionylated substrates with a lower rate but higher affinity compared with Grx1, resulting in almost identical catalytic efficiencies (k(cat)/K(m)). Permutation of the active site motifs of Grx1 and Grx2 revealed that the CSYC sequence of Grx2 is a prerequisite for its high affinity toward glutathionylated proteins, which comes at the price of lower k(cat). Furthermore Grx2 was a substrate for NADPH and thioredoxin reductase, which efficiently reduced both the active site disulfide and the GSH-glutaredoxin intermediate formed in the reduction of glutathionylated substrates. Using this novel electron donor pathway, Grx2 reduced low molecular weight disulfides such as CoA but with particular high efficiency glutathionylated substrates including GSSG. These results suggest an important role for Grx2 in protection and recovery from oxidative stress.
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“reduction of the oxidized form of Grx2 can be mediated by GSH or NADH and thioredoxin reductase (TrxR) (195)”
From Redox regulation of mitochondrial function (2012) · cites this paper as [195]
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“As an example, glutaredoxin-2 (GLRX2) is reduced non-enzymatically by GSH but can be reduced by thioredoxin reductases when GSH is depleted (62).”
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Exploring thioredoxin reductase as an anticancer drug target
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Isoforms of mammalian Glutaredoxin 2
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Metadata
- Authors
- Johansson, C., Lillig, C. H., & Holmgren, A.
- Affiliations
- Karolinska Institutet (SE)
- Corresponding author
- Holmgren, Arne
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2004-02
- Volume
- 279
- Issue
- 9
- Pages
- 7537-7543
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2103665725
- Cited by
- 320
- References
- 81
- Citations by year
- 2026: 6 · 2025: 8 · 2024: 7 · 2023: 12 · 2022: 10 · 2021: 10 · 2020: 8 · 2019: 11 · 2018: 16 · 2017: 14 · 2016: 8 · 2015: 14 · 2014: 16 · 2013: 14 · 2012: 18
- FWCI
- 6.87
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- Wenner-Gren Foundation
- Cancerfonden
- Knut och Alice Wallenbergs Stiftelse
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glutathione Transferases and Polymorphisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Sulfur Compounds in Biology
- Keywords
- glutaredoxin 2, glutaredoxin 1, glutathione, thioredoxin reductase, NADPH, catalytic efficiency, glutathione disulfide, antioxidant defense
- MeSH terms
- Amino Acid Sequence, Animals, Binding Sites, Catalysis, Cattle, Cytosol, Disulfides, Glutathione, Humans, Mitochondria, Molecular Sequence Data, NADP, Oxidation-Reduction, Oxidoreductases, Proteins, Recombinant Proteins, Structure-Activity Relationship, Substrate Specificity, Thioredoxin-Disulfide Reductase, Mutagenesis, Site-Directed, Sequence Alignment, Conserved Sequence, Oxidative Stress, Glutaredoxins
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