Radical-mediated C-S bond cleavage in C2 sulfonate degradation by anaerobic bacteria. View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2019-12

AUTHORS

Meining Xing, Yifeng Wei, Yan Zhou, Jun Zhang, Lianyun Lin, Yiling Hu, Gaoqun Hua, Ankanahalli N Nanjaraj Urs, Dazhi Liu, Feifei Wang, Cuixia Guo, Yang Tong, Mengya Li, Yanhong Liu, Ee Lui Ang, Huimin Zhao, Zhiguang Yuchi, Yan Zhang

ABSTRACT

Bacterial degradation of organosulfonates plays an important role in sulfur recycling, and has been extensively studied. However, this process in anaerobic bacteria especially gut bacteria is little known despite of its potential significant impact on human health with the production of toxic H2S. Here, we describe the structural and biochemical characterization of an oxygen-sensitive enzyme that catalyzes the radical-mediated C-S bond cleavage of isethionate to form sulfite and acetaldehyde. We demonstrate its involvement in pathways that enables C2 sulfonates to be used as terminal electron acceptors for anaerobic respiration in sulfate- and sulfite-reducing bacteria. Furthermore, it plays a key role in converting bile salt-derived taurine into H2S in the disease-associated gut bacterium Bilophila wadsworthia. The enzymes and transporters in these anaerobic pathways expand our understanding of microbial sulfur metabolism, and help deciphering the complex web of microbial pathways involved in the transformation of sulfur compounds in the gut. More... »

PAGES

1609

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/s41467-019-09618-8

DOI

http://dx.doi.org/10.1038/s41467-019-09618-8

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1113300655

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/30962433


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