ArticleThe Journal of biological chemistry2016
Electron Accepting Units of the Diheme Cytochrome c TsdA, a Bifunctional Thiosulfate Dehydrogenase/Tetrathionate Reductase.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 50 citations in OpenAlex.
- Multiheme selenoenzyme essential for elemental sulfur respiration.Science advances · 2026Article
- Demonstration of the Role of Both a Ttr and a Psr Homologue Enzymes in the Respiration of Tetrathionate by an Environmental Bacterium Shewanella sp. ANA-3.Environmental microbiology · 2026Article
- Article
- YeeD is an essential partner for YeeE-mediated thiosulfate uptake in bacteria and regulates thiosulfate ion decomposition.PLoS biology · 2024Article
- Chemoautotrophic production of gaseous hydrocarbons, bioplastics and osmolytes by a novel Halomonas species.Biotechnology for biofuels and bioproducts · 2023Article
- The Troyer syndrome protein spartin mediates selective autophagy of lipid droplets.Nature cell biology · 2023Article
- Microbe-driven elemental cycling enables microbial adaptation to deep-sea ferromanganese nodule sediment fields.Microbiome · 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
- Sulfur and methane oxidation by a single microorganism.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Unraveling Fe(II)-Oxidizing Mechanisms in a Facultative Fe(II) Oxidizer, Sideroxydans lithotrophicus Strain ES-1, via Culturing, Transcriptomics, and Reverse Transcription-Quantitative PCR.Applied and environmental microbiology · 2022Article
- Heterotrophic Sulfur Oxidation ofFrontiers in microbiology · 2022Article
- C-type cytochrome-initiated reduction of bacterial lytic polysaccharide monooxygenases.The Biochemical journal · 2021Article
- Insights into growth kinetics and roles of enzymes of Krebs' cycle and sulfur oxidation during exochemolithoheterotrophic growth of Achromobacter aegrifaciens NCCB 38021 on succinate with thiosulfate as the auxiliary electron donor.Archives of microbiology · 2021Article
- Promoting Extracellular Electron Transfer ofFrontiers 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
- Role of multiheme cytochromes involved in extracellular anaerobic respiration in bacteria.Protein science : a publication of the Protein Society · 2020Review
- Heme ligation and redox chemistry in two bacterial thiosulfate dehydrogenase (TsdA) enzymes.The Journal of biological chemistry · 2019Article
- Divergent Nrf Family Proteins and MtrCAB Homologs Facilitate Extracellular Electron Transfer in Aeromonas hydrophila.Applied and environmental microbiology · 2018Article
Corrections and comments
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Authors and funding
13 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The enzymes of the thiosulfate dehydrogenase (TsdA) family are wide-spread diheme c-type cytochromes. Here, redox carriers were studied mediating the flow of electrons arising from thiosulfate oxidation into respiratory or photosynthetic electron chains. In a number of organisms, including Thiomonas intermedia and Sideroxydans lithotrophicus, the tsdA gene is immediately preceded by tsdB encoding for another diheme cytochrome. Spectrophotometric experiments in combination with enzymatic assays in solution showed that TsdB acts as an effective electron acceptor of TsdA in vitro when TsdA and TsdB originate from the same source organism. Although TsdA covers a range from -300 to +150 mV, TsdB is redox active between -100 and +300 mV, thus enabling electron transfer between these hemoproteins. The three-dimensional structure of the TsdB-TsdA fusion protein from the purple sulfur bacterium Marichromatium purpuratum was solved by X-ray crystallography to 2.75 Å resolution providing insights into internal electron transfer. In the oxidized state, this tetraheme cytochrome c contains three hemes with axial His/Met ligation, whereas heme 3 exhibits the His/Cys coordination typical for TsdA active sites. Interestingly, thiosulfate is covalently bound to Cys
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