ArticleThe Journal of biological chemistry2008
The crystal structure of Desulfovibrio vulgaris dissimilatory sulfite reductase bound to DsrC provides novel insights into the mechanism of sulfate respiration.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.
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59 citing papers in PubMed, 184 citations in OpenAlex.
- Zero-valent sulfur is the product of assimilatory sulfite reductase and a substrate of cysteine synthase.Applied and environmental microbiology · 2026Article
- Distribution of a novel DsrEFH sulfur transferase suggests widespread sulfur oxidation capacity in sulfate reducers.The ISME journal · 2026Article
- Harnessing Pseudodesulfovibrio sp., a sulfate-reducing bacterium for the sustainable synthesis of cerium sulfide.World journal of microbiology & biotechnology · 2025Article
- Structure of dimerized assimilatory NADPH-dependent sulfite reductase reveals the minimal interface for diflavin reductase binding.Nature communications · 2025Article
- Structure of dimerized assimilatory NADPH-dependent sulfite reductase reveals the minimal interface for diflavin reductase binding.bioRxiv : the preprint server for biology · 2025Article
- Virtual screening and molecular dynamic simulations ofIn silico pharmacology · 2025Article
- Characterization of DsrD and its interaction with the DsrAB dissimilatory sulfite reductase.Protein science : a publication of the Protein Society · 2024Article
- Disentangling the microbial genomic traits associated with aromatic hydrocarbon degradation in a jet fuel-contaminated aquifer.Biodegradation · 2024Article
- Multi-omics analyses provide insights into the sulfur metabolism of a novel deep-sea sulfate-reducing bacterium.iScience · 2024Article
- DsrMKJOP is the terminal reductase complex in anaerobic sulfate respiration.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Evolutionary history and origins of Dsr-mediated sulfur oxidation.The ISME journal · 2024Article
- Assimilatory sulfate reduction in the marine methanogen Methanothermococcus thermolithotrophicus.Nature microbiology · 2023Article
- Structures of the sulfite detoxifying FNature chemical biology · 2023Article
- Generation and Physiology of Hydrogen Sulfide and Reactive Sulfur Species in Bacteria.Antioxidants (Basel, Switzerland) · 2022Review
- A Reduced FJournal of bacteriology · 2022Article
- Article
- The DsrD functional marker protein is an allosteric activator of the DsrAB dissimilatory sulfite reductase.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- DiSCo: a sequence-based type-specific predictor of Dsr-dependent dissimilatory sulphur metabolism in microbial data.Microbial genomics · 2021Article
- Screening and testing potential inhibitors of sulphide gas production by sulphate-reducing bacteria.Journal of molecular modeling · 2021Article
- Molecular understanding of heteronuclear active sites in heme-copper oxidases, nitric oxide reductases, and sulfite reductases through biomimetic modelling.Chemical Society reviews · 2021Review
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Sulfate reduction is one of the earliest types of energy metabolism used by ancestral organisms to sustain life. Despite extensive studies, many questions remain about the way respiratory sulfate reduction is associated with energy conservation. A crucial enzyme in this process is the dissimilatory sulfite reductase (dSiR), which contains a unique siroheme-[4Fe4S] coupled cofactor. Here, we report the structure of desulfoviridin from Desulfovibrio vulgaris, in which the dSiR DsrAB (sulfite reductase) subunits are bound to the DsrC protein. The alpha(2)beta(2)gamma(2) assembly contains two siroheme-[4Fe4S] cofactors bound by DsrB, two sirohydrochlorins and two [4Fe4S] centers bound by DsrA, and another four [4Fe4S] centers in the ferredoxin domains. A sulfite molecule, coordinating the siroheme, is found at the active site. The DsrC protein is bound in a cleft between DsrA and DsrB with its conserved C-terminal cysteine reaching the distal side of the siroheme. We propose a novel mechanism for the process of sulfite reduction involving DsrAB, DsrC, and the DsrMKJOP membrane complex (a membrane complex with putative disulfide/thiol reductase activity), in which two of the six electrons for reduction of sulfite derive from the membrane quinone pool. These results show that DsrC is involved in sulfite reduction, which changes the mechanism of sulfate respiration. This has important implications for models used to date ancient sulfur metabolism based on sulfur isotope fractionations.
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