ArticleThe ISME journal2018
Bacterial SBP56 identified as a Cu-dependent methanethiol oxidase widely distributed in the biosphere.
Article in The ISME journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed, 81 citations in OpenAlex.
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- Regulation of DMSP organosulfur cycling in ubiquitous Roseobacter marine bacteria.The EMBO journal · 2026Article
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- In Hyphomicrobium denitrificans Two Related Sulfane-Sulfur Responsive Transcriptional Repressors Regulate Thiosulfate Oxidation and Have a Deep Impact on Nitrate Respiration and Anaerobic Biosyntheses.Molecular microbiology · 2025Article
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- Culture-supported ecophysiology of the SAR116 clade demonstrates metabolic and spatial niche partitioning.The ISME journal · 2025Article
- Active microorganisms and potential metabolic pathways mediating anaerobic degradation of DMSP in anoxic saltmarsh sediment.ISME communications · 2025Article
- Selenium-Binding Protein 1 (SBP1): A New Putative Player of Stress Sensing in Plants.International journal of molecular sciences · 2024Review
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- Diversity and potential host-interactions of viruses inhabiting deep-sea seamount sediments.Nature communications · 2024Article
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- The critical roles of propanethiol oxidoreductase and sulfide-quinone oxidoreductase in the propanethiol catabolism pathway inApplied and environmental microbiology · 2024Article
- Mitigation of biogenic methanethiol using bacteriophages in synthetic wastewater augmented with Pseudomonas putida.Scientific reports · 2023Article
- Methanethiol: A Scent Mark of Dysregulated Sulfur Metabolism in Cancer.Antioxidants (Basel, Switzerland) · 2023Review
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Authors and funding
15 authors at 8 institutions in 4 countries.
Funding
Abstract
Oxidation of methanethiol (MT) is a significant step in the sulfur cycle. MT is an intermediate of metabolism of globally significant organosulfur compounds including dimethylsulfoniopropionate (DMSP) and dimethylsulfide (DMS), which have key roles in marine carbon and sulfur cycling. In aerobic bacteria, MT is degraded by a MT oxidase (MTO). The enzymatic and genetic basis of MT oxidation have remained poorly characterized. Here, we identify for the first time the MTO enzyme and its encoding gene (mtoX) in the DMS-degrading bacterium Hyphomicrobium sp. VS. We show that MTO is a homotetrameric metalloenzyme that requires Cu for enzyme activity. MTO is predicted to be a soluble periplasmic enzyme and a member of a distinct clade of the Selenium-binding protein (SBP56) family for which no function has been reported. Genes orthologous to mtoX exist in many bacteria able to degrade DMS, other one-carbon compounds or DMSP, notably in the marine model organism Ruegeria pomeroyi DSS-3, a member of the Rhodobacteraceae family that is abundant in marine environments. Marker exchange mutagenesis of mtoX disrupted the ability of R. pomeroyi to metabolize MT confirming its function in this DMSP-degrading bacterium. In R. pomeroyi, transcription of mtoX was enhanced by DMSP, methylmercaptopropionate and MT. Rates of MT degradation increased after pre-incubation of the wild-type strain with MT. The detection of mtoX orthologs in diverse bacteria, environmental samples and its abundance in a range of metagenomic data sets point to this enzyme being widely distributed in the environment and having a key role in global sulfur cycling.
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