Depletion of thiol reducing capacity impairs cytosolic but not mitochondrial iron-sulfur protein assembly machineries

Braymer, Joseph J.; Stümpfig, Martin; Thelen, Stefanie; Mühlenhoff, Ulrich; Lill, Roland

doi:10.1016/j.bbamcr.2018.11.003

Cited by 11 publications

(5 citation statements)

References 71 publications

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“…Interestingly, inactivation of mitochondrial thioredoxin did not impair the synthesis of Fe−S clusters by the Isc system, which is present in mitochondria and utilizes ferredoxin as a reductant for Fe−S cluster biogenesis. 84 The isolation of TrxA bound to Fe−S species was an unexpected finding in this study. The loss of TrxA oxidoreductase activity following in vitro cluster reconstitution, combined with the lack of cluster accumulation or activity of the TrxA Cys to Ala variants, suggests that Fe−S species are transiently ligated to the protein via the active site Cys residues.…”

Section: ■ Discussionmentioning

confidence: 88%

“…Inactivation of cytosolic thioredoxin led to impairment of Fe–S enzymes with defects attributed to Fe–S cluster biosynthetic components present in the cytosol. Interestingly, inactivation of mitochondrial thioredoxin did not impair the synthesis of Fe–S clusters by the Isc system, which is present in mitochondria and utilizes ferredoxin as a reductant for Fe–S cluster biogenesis …”

Section: Discussionmentioning

confidence: 99%

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The Thioredoxin System Reduces Protein Persulfide Intermediates Formed during the Synthesis of Thio-Cofactors in Bacillus subtilis

et al. 2019

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The biosynthesis of Fe−S clusters and other thio-cofactors requires the participation of redox agents. A shared feature in these pathways is the formation of transient protein persulfides, which are susceptible to reduction by artificial reducing agents commonly used in reactions in vitro. These agents modulate the reactivity and catalytic efficiency of biosynthetic reactions and, in some cases, skew the enzymes' kinetic behavior, bypassing sulfur acceptors known to be critical for the functionality of these pathways in vivo. Here, we provide kinetic evidence for the selective reactivity of the Bacillus subtilis Trx (thioredoxin) system toward proteinbound persulfide intermediates. Our results demonstrate that the redox flux of the Trx system modulates the rate of sulfide production in cysteine desulfurase assays. Likewise, the activity of the Trx system is dependent on the rate of persulfide formation, suggesting the occurrence of coupled reaction schemes between both enzymatic systems in vitro. Inactivation of TrxA (thioredoxin) or TrxR (thioredoxin reductase) impairs the activity of Fe−S enzymes in B. subtilis, indicating the involvement of the Trx system in Fe−S cluster metabolism. Surprisingly, biochemical characterization of TrxA reveals that this enzyme is able to coordinate Fe−S species, resulting in the loss of its reductase activity. The inactivation of TrxA through the coordination of a labile cluster, combined with its proposed role as a physiological reducing agent in sulfur transfer pathways, suggests a model for redox regulation. These findings provide a potential link between redox regulation and Fe−S metabolism.

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Section: ■ Discussionmentioning

confidence: 88%

Section: Discussionmentioning

confidence: 99%

The Thioredoxin System Reduces Protein Persulfide Intermediates Formed during the Synthesis of Thio-Cofactors in Bacillus subtilis

et al. 2019

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“…Dardalhon et al also showed that GSH depletion had profound effects on mitochondrial genome stability, while the nuclear genome remained stable (Figure 6) [46]. Braymer et al investigated the dependence between iron-sulfur protein assembly and the thiol-reducing glutaredoxin and thioredoxin systems [217]. The cytosolic Fe/S protein assembly machinery was observed to be significantly more sensitive to thiol redox enzyme depletion than that of mitochondria, which was found to be functionally robust.…”

Section: Glutathione and Thioredoxin Systemsmentioning

confidence: 99%

In Vivo Imaging with Genetically Encoded Redox Biosensors

Kostyuk

Panova

Kokova

et al. 2020

IJMS

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Redox reactions are of high fundamental and practical interest since they are involved in both normal physiology and the pathogenesis of various diseases. However, this area of research has always been a relatively problematic field in the context of analytical approaches, mostly because of the unstable nature of the compounds that are measured. Genetically encoded sensors allow for the registration of highly reactive molecules in real-time mode and, therefore, they began a new era in redox biology. Their strongest points manifest most brightly in in vivo experiments and pave the way for the non-invasive investigation of biochemical pathways that proceed in organisms from different systematic groups. In the first part of the review, we briefly describe the redox sensors that were used in vivo as well as summarize the model systems to which they were applied. Next, we thoroughly discuss the biological results obtained in these studies in regard to animals, plants, as well as unicellular eukaryotes and prokaryotes. We hope that this work reflects the amazing power of this technology and can serve as a useful guide for biologists and chemists who work in the field of redox processes.

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“…Fe enzyme Fe-S dehydratase such as Fe(II)-cysteine is oxidized through Fenton reactions to the sulphinic RSO(=H) or sulphonic RS=O 2 -OH species, displacing Fe(II) from the metalloenzyme. The latter reaction involves several steps: (a) oxidant depletion and (b) additional (excess) ROS and thiol depletion from the cell bilayer topmost functional groups [62]. Thiol depletion due to Fenton-like reactions is shown schematically in Figure 9.…”

Section: Ifct In Fe 2 O 3 /Tio 2 Giving Rise To Fenton-like Reactions Mediating Virus/bacterial Inactivationmentioning

confidence: 99%

Update on Interfacial Charge Transfer (IFTC) Processes on Films Inactivating Viruses/Bacteria under Visible Light: Mechanistic Considerations and Critical Issues

Rtimi

Kiwi

2021

Catalysts

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This review presents an update describing binary and ternary semiconductors involving interfacial charge transfer (IFCT) in composites made up by TiO2, CuO, Ag2O and Fe2O3 used in microbial disinfection (bacteria and viruses). The disinfection mechanism, kinetics and generation of reactive oxygen species (ROS) in solution under solar/visible light are discussed. The surface properties of the photocatalysts and their active catalytic sites are described in detail. Pathogenic biofilm inactivation by photocatalytic thin films is addressed since biofilms are the most dangerous agents of spreading pathogens into the environment.

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Depletion of thiol reducing capacity impairs cytosolic but not mitochondrial iron-sulfur protein assembly machineries

Cited by 11 publications

References 71 publications

The Thioredoxin System Reduces Protein Persulfide Intermediates Formed during the Synthesis of Thio-Cofactors in Bacillus subtilis

The Thioredoxin System Reduces Protein Persulfide Intermediates Formed during the Synthesis of Thio-Cofactors in Bacillus subtilis

In Vivo Imaging with Genetically Encoded Redox Biosensors

Update on Interfacial Charge Transfer (IFTC) Processes on Films Inactivating Viruses/Bacteria under Visible Light: Mechanistic Considerations and Critical Issues

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