ArticleThe Journal of biological chemistry2015
Polymorphic Variants of Human Rhodanese Exhibit Differences in Thermal Stability and Sulfur Transfer Kinetics.
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 44 papers.
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Who cites it
44 citing papers in PubMed, 69 citations in OpenAlex.
- Aglycemia triggers alternative electron transport to sustain mesenchymal stem cell survival under anoxia.Redox biology · 2026Article
- Biodegradation of Cyanide-Based Compounds by Rhodanese Produced fromMolecules (Basel, Switzerland) · 2026Article
- Hydrogen Sulfide Consumption and Cell Bioenergetics in Human (Patho)physiology.Handbook of experimental pharmacology · 2026Review
- Hydrogen Sulfide Signaling in Neurodegenerative Movement Disorders.Handbook of experimental pharmacology · 2026Review
- Enzymes that generate and regulate intracellular persulfides and polysulfides: mechanistic insights and inhibitors.Frontiers in physiology · 2026Review
- Gut sulfide metabolism modulates behavior and brain bioenergetics.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Thiosulphate sulfurtransferase: Biological roles and therapeutic potential.Redox biology · 2025Review
- Essential role of sulfide oxidation in brain health and neurological disorders.Pharmacology & therapeutics · 2025Review
- Integrated Metabolomics and Proteomics Analysis of the Myocardium in a Mouse Model of Acute Viral Myocarditis.Immunity, inflammation and disease · 2025Article
- Role of hydrogen sulfide in health and disease.MedComm · 2024Review
- Structural and biochemical characterization of an encapsulin-associated rhodanese from Acinetobacter baumannii.Protein science : a publication of the Protein Society · 2024Article
- Hydrogen sulfide maintains mitochondrial homeostasis and regulates ganoderic acids biosynthesis by SQR under heat stress in Ganoderma lucidum.Redox biology · 2024Article
- Structural and biochemical characterization of an encapsulin-associated rhodanese frombioRxiv : the preprint server for biology · 2024Article
- Thiosulfate sulfurtransferase deficiency promotes oxidative distress and aberrant NRF2 function in the brain.Redox biology · 2023Article
- Role of Hydrogen Sulfide in Inflammatory Bowel Disease.Antioxidants (Basel, Switzerland) · 2023Review
- Emerging Chemical Biology of Protein Persulfidation.Antioxidants & redox signaling · 2023Review
- Hydrogen sulfide as an anti-calcification stratagem in human aortic valve: Altered biogenesis and mitochondrial metabolism of HRedox biology · 2023Article
- Rhodanese-Fold Containing Proteins in Humans: Not Just Key Players in Sulfur Trafficking.Antioxidants (Basel, Switzerland) · 2023Review
- Implications of hydrogen sulfide in colorectal cancer: Mechanistic insights and diagnostic and therapeutic strategies.Redox biology · 2023Review
- A Metabolic Paradigm for Hydrogen Sulfide SignalingAntioxidants & redox signaling · 2023Review
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3 authors at 1 institution in 1 country.
Funding
Abstract
Rhodanese is a component of the mitochondrial H2S oxidation pathway. Rhodanese catalyzes the transfer of sulfane sulfur from glutathione persulfide (GSSH) to sulfite generating thiosulfate and from thiosulfate to cyanide generating thiocyanate. Two polymorphic variations have been identified in the rhodanese coding sequence in the French Caucasian population. The first, 306A→C, has an allelic frequency of 1% and results in an E102D substitution in the encoded protein. The second polymorphism, 853C→G, has an allelic frequency of 5% and leads to a P285A substitution. In this study, we have examined differences in the stability between wild-type rhodanese and the E102D and P285A variants and in the kinetics of the sulfur transfer reactions. The Asp-102 and Ala-285 variants are more stable than wild-type rhodanese and exhibit kcat/Km,CN values that are 17- and 1.6-fold higher, respectively. All three rhodanese forms preferentially catalyze sulfur transfer from GSSH to sulfite, generating thiosulfate and glutathione. The kcat/Km,sulfite values for the variants in the sulfur transfer reaction from GSSH to sulfite were 1.6- (Asp-102) and 4-fold (Ala-285) lower than for wild-type rhodanese, whereas the kcat/Km,GSSH values were similar for all three enzymes. Thiosulfate-dependent H2S production in murine liver lysate is low, consistent with a role for rhodanese in sulfide oxidation. Our studies show that polymorphic variations that are distant from the active site differentially modulate the sulfurtransferase activity of human rhodanese to cyanide versus sulfite and might be important in differences in susceptibility to diseases where rhodanese dysfunction has been implicated, e.g. inflammatory bowel diseases.
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