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Structural and mechanistic insights into dimethylsulfoxide formation through dimethylsulfide oxidation
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Wang, Xiu-Juan, Zhang, Nan, Teng, Zhao-Jie, Wang, Peng, Zhang, Wei-Peng, Chen, Xiu-Lan, Zhang, Yu-Zhong, Chen, Yin, Fu, Hui-Hui and Li, Chun-Yang (2021) Structural and mechanistic insights into dimethylsulfoxide formation through dimethylsulfide oxidation. Frontiers in Microbiology, 12 . 735793. doi:10.3389/fmicb.2021.735793 ISSN 1664-302X.
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WRAP-Structural-mechanistic-insights-dimethylsulfoxide-formation-dimethylsulfide-oxidation-2021.pdf - Accepted Version - Requires a PDF viewer. Available under License Creative Commons Attribution 4.0. Download (3029Kb) | Preview |
Official URL: https://doi.org/10.3389/fmicb.2021.735793
Abstract
Dimethylsulfide (DMS) and dimethylsulfoxide (DMSO) are widespread in marine environment, and are important participants in the global sulfur cycle. Microbiol oxidation of DMS to DMSO represents a major sink of DMS in marine surface waters. The SAR11 clade and the marine Roseobacter clade (MRC) are the most abundant heterotrophic bacteria in the ocean surface seawater. It has been reported that trimethylamine monooxygenase (Tmm, EC 1.14.13.148) from both MRC and SAR11 bacteria likely oxidizes DMS to generate DMSO. However, the structural basis of DMS oxidation has not been explained. Here, we characterized a Tmm homolog from the SAR11 bacterium Pelagibacter sp. HTCC7211 (Tmm7211). Tmm7211 exhibits DMS oxidation activity in vitro. We further solved the crystal structures of Tmm7211 and Tmm7211 soaked with DMS, and proposed the catalytic mechanism of Tmm7211, which comprises a reductive half-reaction and an oxidative half-reaction. FAD and NADPH molecules are essential for the catalysis of Tmm7211. In the reductive half-reaction, FAD is reduced by NADPH. In the oxidative half-reaction, the reduced FAD reacts with O2 to form the C4a-(hydro)peroxyflavin. The binding of DMS may repel the nicotinamide ring of NADP+, and make NADP+ generate a conformational change, shutting off the substrate entrance and exposing the active C4a-(hydro)peroxyflavin to DMS to complete the oxidation of DMS. The proposed catalytic mechanism of Tmm7211 may be widely adopted by MRC and SAR11 bacteria. This study provides important insight into the conversion of DMS into DMSO in marine bacteria, leading to a better understanding of the global sulfur cycle.
| Item Type: | Journal Article | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Subjects: | Q Science > QE Geology Q Science > QH Natural history Q Science > QP Physiology |
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| Divisions: | Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- ) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| SWORD Depositor: | Library Publications Router | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Library of Congress Subject Headings (LCSH): | Dimethyl sulfide , Dimethyl sulfoxide , Dimethyl sulfide -- Oxidation , Marine biodiversity , Sulfur -- Metabolism , Monooxygenases , Marine bacteria | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Journal or Publication Title: | Frontiers in Microbiology | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Publisher: | Frontiers Media S.A. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| ISSN: | 1664-302X | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Official Date: | 24 September 2021 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Volume: | 12 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Article Number: | 735793 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| DOI: | 10.3389/fmicb.2021.735793 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Status: | Peer Reviewed | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Publication Status: | Published | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Access rights to Published version: | Open Access (Creative Commons) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Date of first compliant deposit: | 25 October 2021 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Date of first compliant Open Access: | 25 October 2021 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| RIOXX Funder/Project Grant: |
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