Dissimilatory Sulfite Reductase (Desulfoviridin) of the Taurine-Degrading, Non-Sulfate-Reducing Bacterium Bilophila wadsworthia RZATAU Contains a Fused DsrB-DsrD Subunit
Open accessAbstract
A dissimilatory sulfite reductase (DSR) was purified from the anaerobic, taurine-degrading bacterium Bilophila wadsworthia RZATAU to apparent homogeneity. The enzyme is involved in energy conservation by reducing sulfite, which is formed during the degradation of taurine as an electron acceptor, to sulfide. According to its UV-visible absorption spectrum with maxima at 392, 410, 583, and 630 nm, the enzyme belongs to the desulfoviridin type of DSRs. The sulfite reductase was isolated as an alpha2beta)gamma(n) (n > or = 2) multimer with a native size of 285 kDa as determined by gel filtration. We have sequenced the genes encoding the alpha and beta subunits (dsrA and dsrB, respectively), which probably constitute one operon. dsrA and dsrB encode polypeptides of 49 (alpha) and 54 kDa (beta) which show significant similarities to the homologous subunits of other DSRs. The dsrB gene product of B. wadsworthia is apparently a fusion protein of dsrB and dsrD. This indicates a possible functional role of DsrD in DSR function because of its presence as a fusion protein as an integral part of the DSR holoenzyme in B. wadsworthia. A phylogenetic analysis using the available Dsr sequences revealed that B. wadsworthia grouped with its closest 16S rDNA relative Desulfovibrio desulfuricans Essex 6.
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Desulfovibrio is one of the few gut bacteria able to consume taurine anaerobically, which could reduce taurine in the BA pool, thus preventing reconjugation of taurine forms, as reported in this study.
“one of the few gut bacteria able to consume taurine anaerobically,61 which could reduce taurine in the BA pool, thus preventing reconjugation of taurine forms, as reported in this study.”
From <i>Lactiplantibacillus plantarum</i> strains KABP011, KABP012, and KABP013 modulate bile acids and cholesterol metabolism in humans (2024) · cites this paper as [61]
The Abstract and Results report anaerobic taurine use by Bilophila wadsworthia, not Desulfovibrio. The Materials and Methods describe Desulfovibrio grown with cysteate rather than taurine; the paper does not establish that Desulfovibrio is one of a few gut bacteria able to consume taurine anaerobically. Page numbers were not provided in our copy. (LLM, conf=0.85)
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“…on general microbiota diversity but significantly increased abundance of members of the class Desulfovibrio , one of the few gut bacteria able to consume taurine anaerobically, 61 which could reduce taurine in the BA pool, thus preventing reconjugation of taurine forms, as reported in this study.”
Result
- Authors
- Laue, H., Friedrich, M., Ruff, J., & Cook, A. M.
- Affiliations
- University of Konstanz (DE)
- Max Planck Institute for Terrestrial Microbiology (DE)
- <!--label omitted: 1-->Fachbereich Biologie, Universität Konstanz, D-78457 Konstanz,1 and
- Venue
- Journal of Bacteriology
- Publisher
- American Society for Microbiology
- Published
- 2001-03
- Volume
- 183
- Issue
- 5
- Pages
- 1727-1733
- ISSN
- 0021-9193 (ISSN-L)
- 1098-5530
- PMC
- PMC95058
- OpenAlex
- W2123127064
- Cited by
- 87
- References
- 49
- Citations by year
- 2026: 3 · 2025: 1 · 2024: 6 · 2023: 5 · 2022: 5 · 2021: 4 · 2020: 7 · 2019: 5 · 2018: 2 · 2017: 5 · 2016: 2 · 2015: 6 · 2014: 1 · 2013: 2 · 2012: 3
- FWCI
- 2.96
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Journal of Bacteriology (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- KOPS (University of Konstanz) (submittedVersion, cc-by-nc-nd)
- Funders
- Deutsche Forschungsgemeinschaft
- Max-Planck-Gesellschaft
- Topics
- Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › Metalloenzymes and iron-sulfur proteins
- Physical Sciences › Environmental Science › Ecology › Microbial Community Ecology and Physiology
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Keywords
- dissimilatory sulfite reductase, desulfoviridin, Bilophila wadsworthia, DsrA, enzyme purification, multimeric enzyme, gene operon, phylogenetic analysis, Desulfovibrio desulfuricans, anaerobic bacteria, sulfite reduction
- MeSH terms
- Amino Acid Sequence, Anaerobiosis, Electrophoresis, Polyacrylamide Gel, Molecular Sequence Data, Oxidoreductases, Phylogeny, Sulfates, Sulfites, Taurine, Sequence Analysis, DNA, Deltaproteobacteria, Oxidoreductases Acting on Sulfur Group Donors
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