ArticleThe Journal of biological chemistry2015
Thiosulfate dehydrogenase (TsdA) from Allochromatium vinosum: structural and functional insights into thiosulfate oxidation.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed.
- Isolation and Characterization of a Novel Sulfur-OxidizingMicroorganisms · 2026Article
- Photocatalytic Biohybrid Vesicles.Chemical reviews · 2026Review
- Sulfur oxidation and implications for oxygen consumption in Base Mine Lake, the first pilot oil sands pit lake in the Athabasca oil sands region.Frontiers in microbiology · 2025Article
- The two-component system TtrRS boosts Vibrio parahaemolyticus colonization by exploiting sulfur compounds in host gut.PLoS pathogens · 2024Article
- Structural and mechanistic basis for RiPP epimerization by a radical SAM enzyme.Nature chemical biology · 2024Article
- The Complete Genome of a Novel Typical SpeciesMicroorganisms · 2024Article
- pH and thiosulfate dependent microbial sulfur oxidation strategies across diverse environments.Frontiers in microbiology · 2024Article
- Tetrathionate hydrolase from the acidophilic microorganisms.Frontiers in microbiology · 2024Review
- Cold Sulfur Springs-Neglected Niche for Autotrophic Sulfur-Oxidizing Bacteria.Microorganisms · 2023Review
- ONature communications · 2023Article
- Generation and Physiology of Hydrogen Sulfide and Reactive Sulfur Species in Bacteria.Antioxidants (Basel, Switzerland) · 2022Review
- Reaction of Thiosulfate Dehydrogenase with a Substrate Mimic Induces Dissociation of the Cysteine Heme Ligand Giving Insights into the Mechanism of Oxidative Catalysis.Journal of the American Chemical Society · 2022Article
- Complete genome sequence of Pseudomonas stutzeri S116 owning bifunctional catalysis provides insights into affecting performance of microbial fuel cells.BMC microbiology · 2022Article
- Biodesulfurization of thiosulfate by a Pseudomonas strain PSP1 and the investigation of underlying metabolic mechanisms.Environmental science and pollution research international · 2022Article
- Heterotrophic Sulfur Oxidation ofFrontiers in microbiology · 2022Article
- A new regime of heme-dependent aromatic oxygenase superfamily.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- A novel catalytic heme cofactor in SfmD with a single thioether bond and aChemical science · 2021Article
- Aerobic Denitrification and Heterotrophic Sulfur Oxidation in the GenusFrontiers in microbiology · 2021Article
- X-ray-induced photoreduction of heme metal centers rapidly induces active-site perturbations in a protein-independent manner.The Journal of biological chemistry · 2020Article
- A novel bacterial thiosulfate oxidation pathway provides a new clue about the formation of zero-valent sulfur in deep sea.The ISME journal · 2020Article
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5 authors.
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Abstract
Although the oxidative condensation of two thiosulfate anions to tetrathionate constitutes a well documented and significant part of the natural sulfur cycle, little is known about the enzymes catalyzing this reaction. In the purple sulfur bacterium Allochromatium vinosum, the reaction is catalyzed by the periplasmic diheme c-type cytochrome thiosulfate dehydrogenase (TsdA). Here, we report the crystal structure of the "as isolated" form of A. vinosum TsdA to 1.98 Å resolution and those of several redox states of the enzyme to different resolutions. The protein contains two typical class I c-type cytochrome domains wrapped around two hemes axially coordinated by His(53)/Cys(96) and His(164)/Lys(208). These domains are very similar, suggesting a gene duplication event during evolution. A ligand switch from Lys(208) to Met(209) is observed upon reduction of the enzyme. Cys(96) is an essential residue for catalysis, with the specific activity of the enzyme being completely abolished in several TsdA-Cys(96) variants. TsdA-K208N, K208G, and M209G variants were catalytically active in thiosulfate oxidation as well as in tetrathionate reduction, pointing to heme 2 as the electron exit point. In this study, we provide spectroscopic and structural evidence that the TsdA reaction cycle involves the transient presence of heme 1 in the high-spin state caused by movement of the Sγ atom of Cys(96) out of the iron coordination sphere. Based on the presented data, we draw important conclusions about the enzyme and propose a possible reaction mechanism for TsdA.
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