ArticleProceedings of the National Academy of Sciences of the United States of America2024
S-adenosyl-L-methionine is the unexpected methyl donor for the methylation of mercury by the membrane-associated HgcAB complex.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Zebrafish parental co-exposure to environmentally relevant levels of inorganic arsenic + methylmercury impacts neurobehavior in parents and progeny.Environmental toxicology and pharmacology · 2026Article
- The cobalamin-binding domain of cobalamin-dependent radical S-adenosylmethionine enzymes: Familiarity in unfamiliar places.Journal of inorganic biochemistry · 2026Review
- An unusual Co-S bond links BProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Concentrations and Health Implications of As, Hg, and Cd and Micronutrients in Rice and Emissions of CHGeoHealth · 2025Article
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Authors and funding
9 authors.
Funding
Abstract
Mercury (Hg) is a heavy metal that exhibits high biological toxicity. Monomethylmercury and dimethylmercury are neurotoxins and a significant environmental concern as they bioaccumulate and biomagnify within the aquatic food web. Microbial Hg methylation involves two proteins, HgcA and HgcB. Here, we show that HgcA and HgcB can be heterologously coexpressed, and the HgcAB complex can be purified. We demonstrated that HgcA is a membrane-associated cobalamin-dependent methyltransferase and HgcB is a ferredoxin-like protein containing two [4Fe-4S] clusters. Further, spectroscopic and kinetic results demonstrate that S-adenosyl-L-methionine (SAM) donates the methyl group to Hg in a two-step reaction involving a methylcob(III)alamin intermediate including Co-thiolate ligation from a conserved Cys residue. Our findings uncover a biological role for SAM in microbial Hg methylation.
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Registered trials
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