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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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“Second, based on the observation that some Grxs can be reduced by thioredoxin reductases (Johansson et al., 2004; Zaffagnini et al., 2008; Couturier et al., 2013), another possibility could be that in specific physiological situations or sub-cellular compartments where glutathione is depleted,…”
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“Interestingly, Grx2 is not only dependent on GSH for reduction, but it is also a direct substrate for Txnrd2 (Johansson et al., 2004).”
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“Due to this feature, Grx2 is also a substrate of thioredoxin reductase [12] and can coordinate a [2Fe–2S] iron-sulfur center forming a dimer [13].”
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“Several disulfide exchange reactions among the Trx and GSH systems exist (27, 28, 34, 38, 60), although they are not at equilibrium (22).”
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“Human Trx1, Grx1, Grx2, and Grx2C40S were prepared as described previously (25, 38, 40).”
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“GR catalyzes the conversion of GSSG to GSH, using the cofactor nicotinamide adenine dinucleotide phosphate (NADPH) produced by the pentose phosphate pathway (PPP) with the enzymatic function of glucose 6-phosphate dehydrogenase (G6PD) and 6-phosphogluconate dehydrogenase (6PGD) (Johansson et al., 2004; Rhee et al., 20…”
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Effects of Mammalian Thioredoxin Reductase Inhibitors
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Oxidative Disassembly of the [2Fe-2S] Cluster of Human Grx2 and Redox Regulation in the Mitochondria
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Phylogenetic distribution and structural analyses of cyanobacterial glutaredoxins (Grxs)
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Safeguarding the brain from oxidative damage
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Identification of potential protein dithiol-disulfide substrates of mammalian Grx2
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“Human Trx1 and Grx1 were recombinant expressed and purified as described before [21,22].”
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HyPer as a tool to determine the reductive activity in cellular compartments
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“[26].”
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Proteomic Characterization of Reversible Thiol Oxidations in Proteomes and Proteins
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“For instance, it has been reported that human Grx2 can be directly reduced in vitro not only by GSH but also by Trx reductase (48), and the same applies to bacterial Grx4 (26).”
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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