ArticleMolecular microbiology2023
Excess copper catalyzes protein disulfide bond formation in the bacterial periplasm but not in the cytoplasm.
Article in Molecular microbiology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 20 citations in OpenAlex.
- Copper oxide nanoparticles: from EU-regulatory landscape and mechanistic toxicity towards a cuproptosis-linked adverse outcome pathway.Archives of toxicology · 2026Review
- CuiT is a Cu importer required for metal homeostasis inBiochemistry and biophysics reports · 2026Article
- Effects of Glutathione on Antibiotic Susceptibility and Resistance in Bacteria: A Comprehensive Review.Infection and drug resistance · 2026Review
- Green synthesis of Cu-doped ZnO nanocomposites using Phytolacca Dodecandra root extract to improve photocatalytic and antibacterial activity and extend avocado shelf-life.Scientific reports · 2025Article
- Copper(II) Complexes of Selected Acylhydrazones as Potential Biological Agents.International journal of molecular sciences · 2025Article
- Ecological Imprint of Rare Earth Mining on Microbial Communities and Water Quality Across Depth and Distance Gradients in Ganzhou, China.Microorganisms · 2025Article
- Cu2+ mediates the oxidation of the transcription factor MscA to regulate the antioxidant defense of mycobacteria.Nucleic acids research · 2025Article
- Iron, Copper, and Zinc Homeostasis in the Battle between Macrophage andCurrent medicinal chemistry · 2025Review
- Glycyl-l-histidyl-l-lysine prevents copper- and zinc-induced protein aggregation and central nervous system cell death in vitro.Metallomics : integrated biometal science · 2024Article
- An intramolecular macrocyclase in plant ribosomal peptide biosynthesis.Nature chemical biology · 2024Article
- Identification of a novel transcriptional regulator, CorR, for copper stress response inApplied and environmental microbiology · 2023Article
- Revisiting the pro-oxidant activity of copper: interplay of ascorbate, cysteine, and glutathione.Metallomics : integrated biometal science · 2023Article
- Evidence that protein thiols are not primary targets of intracellular reactive oxygen species in growingFrontiers in microbiology · 2023Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Copper avidly binds thiols and is redox active, and it follows that one element of copper toxicity may be the generation of undesirable disulfide bonds in proteins. In the present study, copper oxidized the model thiol N-acetylcysteine in vitro. Alkaline phosphatase (AP) requires disulfide bonds for activity, and copper activated reduced AP both in vitro and when it was expressed in the periplasm of mutants lacking their native disulfide-generating system. However, AP was not activated when it was expressed in the cytoplasm of copper-overloaded cells. Similarly, this copper stress failed to activate OxyR, a transcription factor that responds to the creation of a disulfide bond. The elimination of cellular disulfide-reducing systems did not change these results. Nevertheless, in these cells, the cytoplasmic copper concentration was high enough to impair growth and completely inactivate enzymes with solvent-exposed [4Fe-4S] clusters. Experiments with N-acetylcysteine determined that the efficiency of thiol oxidation is limited by the sluggish pace at which oxygen regenerates copper(II) through oxidation of the thiyl radical-Cu(I) complex. We conclude that this slow step makes copper too inefficient a catalyst to create disulfide stress in the thiol-rich cytoplasm, but it can still impact the few thiol-containing proteins in the periplasm. It also ensures that copper accumulates intracellularly in the Cu(I) valence.
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