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| Main Authors: | , , , , , , , |
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| Format: | Artículo científico |
| Language: | en |
| Published: |
Environmental science & technology
2025
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| Subjects: | |
| Online Access: | https://pubmed.ncbi.nlm.nih.gov/40773659/ |
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| _version_ | 1868266167314939906 |
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| author | Li, Xue-Ting Shen, Jie Bickel, David Mu, Da-Shuai Rosen, Barry P Messens, Joris Zhang, Jun Zhao, Fang-Jie |
| author_facet | Li, Xue-Ting Shen, Jie Bickel, David Mu, Da-Shuai Rosen, Barry P Messens, Joris Zhang, Jun Zhao, Fang-Jie Li, Xue-Ting Shen, Jie Bickel, David Mu, Da-Shuai Rosen, Barry P Messens, Joris Zhang, Jun Zhao, Fang-Jie |
| collection | PubMed - marine biology |
| contents | The Thioredoxin System Powers ArsM-Mediated Arsenite Methylation in . Li, Xue-Ting Shen, Jie Bickel, David Mu, Da-Shuai Rosen, Barry P Messens, Joris Zhang, Jun Zhao, Fang-Jie Methylation Arsenites Thioredoxins Bacteroidetes Methyltransferases Arsenic biomethylation plays a critical role in modulating environmental arsenic toxicity yet remains understudied in the phylum . Here, we characterize HeArsM, a methyltransferase from the soil bacterium , which effectively methylates arsenite [As(III)] into various species. We demonstrated that this activity is primarily supported by the thioredoxin (Trx)-thioredoxin reductase (TR)-NADPH system, which is significantly more effective than alternative reductants such as glutathione/glutaredoxin (GSH/Grx), cysteine, or tris(2-carboxyethyl)phosphine (TCEP). Site-directed mutagenesis identified Cys23, Cys48, and Cys143 as essential for catalysis, with Cys143 uniquely required for monomethylarsenite [MMAs(III)] methylation. Structural modeling using AlphaFold and energy minimization supports a thiol-disulfide exchange mechanism as the basis for arsenic methylation. These findings provide mechanistic insight into arsenic detoxification in and highlight as a model for understanding microbial arsenic cycling in terrestrial environments. |
| format | Artículo científico |
| id | pubmed_40773659 |
| institution | PubMed |
| language | en |
| publishDate | 2025 |
| publisher | Environmental science & technology |
| record_format | pubmed |
| spellingShingle | The Thioredoxin System Powers ArsM-Mediated Arsenite Methylation in . Li, Xue-Ting Shen, Jie Bickel, David Mu, Da-Shuai Rosen, Barry P Messens, Joris Zhang, Jun Zhao, Fang-Jie Methylation Arsenites Thioredoxins Bacteroidetes Methyltransferases The Thioredoxin System Powers ArsM-Mediated Arsenite Methylation in . Li, Xue-Ting Shen, Jie Bickel, David Mu, Da-Shuai Rosen, Barry P Messens, Joris Zhang, Jun Zhao, Fang-Jie Methylation Arsenites Thioredoxins Bacteroidetes Methyltransferases Arsenic biomethylation plays a critical role in modulating environmental arsenic toxicity yet remains understudied in the phylum . Here, we characterize HeArsM, a methyltransferase from the soil bacterium , which effectively methylates arsenite [As(III)] into various species. We demonstrated that this activity is primarily supported by the thioredoxin (Trx)-thioredoxin reductase (TR)-NADPH system, which is significantly more effective than alternative reductants such as glutathione/glutaredoxin (GSH/Grx), cysteine, or tris(2-carboxyethyl)phosphine (TCEP). Site-directed mutagenesis identified Cys23, Cys48, and Cys143 as essential for catalysis, with Cys143 uniquely required for monomethylarsenite [MMAs(III)] methylation. Structural modeling using AlphaFold and energy minimization supports a thiol-disulfide exchange mechanism as the basis for arsenic methylation. These findings provide mechanistic insight into arsenic detoxification in and highlight as a model for understanding microbial arsenic cycling in terrestrial environments. |
| title | The Thioredoxin System Powers ArsM-Mediated Arsenite Methylation in . |
| topic | Methylation Arsenites Thioredoxins Bacteroidetes Methyltransferases |
| url | https://pubmed.ncbi.nlm.nih.gov/40773659/ |