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Updated: Dec 9, 2025
12:59
A Study of the Complexation of MercuryII with Dicysteinyl Tetrapeptides by Electrospray Ionization Mass Spectrometry
Published on: January 8, 2016
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Sulfhydryl groups as targets of mercury toxicity.
Olga P Ajsuvakova1,2,3, Alexey A Tinkov1,2,3, Michael Aschner3,4
1Yaroslavl State University, Yaroslavl, Russia.
Coordination Chemistry Reviews
|September 9, 2020
Summary
Mercury (Hg) binds to thiol groups in biological molecules like cysteine and glutathione, causing cellular damage and toxicity. Understanding Hg-thiol interactions is crucial for developing strategies against mercury overload.
Area of Science:
- Environmental Toxicology
- Biochemistry
- Molecular Biology
Background:
- Mercury (Hg) exhibits high affinity for sulfhydryl (thiol; -SH) groups present in biological ligands.
- Cysteine (Cys) residues are primary targets for Hg, leading to cellular damage.
- Hg-ligand conjugates play a significant role in Hg metabolism and transport.
Purpose of the Study:
- To review existing data on Hg affinity and conjugation with biological thiols.
- To highlight the toxicological consequences of Hg-thiol interactions.
- To emphasize the need for further research into Hg-thiol binding in toxicology.
Main Methods:
- Literature review of studies on mercury-thiol interactions.
- Analysis of data concerning Hg binding to proteins (e.g., albumin) and small molecules (e.g., glutathione).
- Examination of the molecular pathways implicated in Hg toxicity.
Main Results:
- Hg binding to Cys residues inhibits enzymes and proteins, mediating toxic effects.
- Albumin is a major Hg-binding protein in plasma, with Hg binding at Cys34.
- Hg-thiol interactions contribute to apoptosis, oxidative stress, and neurotoxicity.
Conclusions:
- Hg-thiol binding is a key mechanism underlying mercury toxicity.
- Further research is needed to fully elucidate the role of Hg-thiol interactions in Hg toxicology.
- Understanding these interactions is vital for developing countermeasures against mercury overload.
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