Demethylation of Methylmercury in Bird, Fish, and Earthworm
Alain Manceau, Jean‐Paul Bourdineaud, Ricardo Bezerra de Oliveira, Sandra Layse Ferreira Sarrazin, David P. Krabbenhoft, Collin A. Eagles‐Smith, Joshua T. Ackerman, A. Robin Stewart, Christian Ward-Deitrich, M. Estela del Castillo Busto, Heidi Goenaga‐Infante, Aude Wack, Marius Retegan, Blanka Detlefs, Pieter Glatzel, Paco Bustamante, Kathryn L. Nagy, Brett A. Poulin
Abstract
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.