ArticleThe Journal of biological chemistry2019
Heme ligation and redox chemistry in two bacterial thiosulfate dehydrogenase (TsdA) enzymes.
Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 20 citations in OpenAlex.
- Electrochemical Investigation of Enzyme Kinetics with an Unmediated, Unmodified Platinum Microelectrode: The Case of Glucose Oxidase.ACS electrochemistry · 2025Article
- Article
- 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
- The Di-Iron Protein YtfE Is a Nitric Oxide-Generating Nitrite Reductase Involved in the Management of Nitrosative Stress.Journal of the American Chemical Society · 2022Article
- Heterotrophic Sulfur Oxidation ofFrontiers in microbiology · 2022Article
- X-ray-induced photoreduction of heme metal centers rapidly induces active-site perturbations in a protein-independent manner.The Journal of biological chemistry · 2020Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Thiosulfate dehydrogenases (TsdAs) are bidirectional bacterial di-heme enzymes that catalyze the interconversion of tetrathionate and thiosulfate at measurable rates in both directions. In contrast to our knowledge of TsdA activities, information on the redox properties in the absence of substrates is rather scant. To address this deficit, we combined magnetic CD (MCD) spectroscopy and protein film electrochemistry (PFE) in a study to resolve heme ligation and redox chemistry in two representative TsdAs. We examined the TsdAs from
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