Demethylation of Methylmercury in Bird, Fish, and Earthworm

Toxicity of methylmercury (MeHg) to wildlife and humans results from its binding to cysteine residues of proteins, forming MeHg-cysteinate (MeHgCys) complexes that hinder biological functions. MeHgCys complexes can be detoxified in vivo, yet how this occurs is unknown. We report that MeHgCys complexes are transformed into selenocysteinate [Hg(Sec)(4)] complexes in multiple animals from two phyla (a waterbird, freshwater fish, and earthworms) sampled in different geographical areas and contaminated by different Hg sources. In addition, high energy-resolution X-ray absorption spectroscopy (HR-XANES) and chromatography-inductively coupled plasma mass spectrometry of the waterbird liver support the binding of Hg(Sec)(4) to selenoprotein P and biomineralization of Hg(Sec)(4) to chemically inert nanoparticulate mercury selenide (HgSe). The results provide a foundation for understanding mercury detoxification in higher organisms and suggest that the identified MeHgCys to Hg(Sec) 4 demethylation pathway is common in nature.

Automated summary

The research findings demonstrate that in various animals, methylmercury cysteinate complexes can be transformed into selenocysteinate complexes, potentially involving the binding to selenoprotein P and formation of mercury selenide, providing new insights into mercury detoxification mechanisms.