ArticleJournal of the American Chemical Society2024
Cobalt(II)-Substituted Cysteamine Dioxygenase Oxygenation Proceeds through a Cobalt(III)-Superoxo Complex.
Article in Journal of the American Chemical Society, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Dynamic coordination and reconstruction-induced chemiluminescence in chiral covalent organic frameworks for enantioselective sensing.Chemical science · 2026Article
- A Structurally Analogous Series of Mn(II), Fe(II), and Co(II) Complexes Which Exhibit Three Distinct Reactivities with Dioxygen.Inorganic chemistry · 2026Article
- Recent discoveries in mono- and dinuclear nonheme iron enzymes: Emerging mechanisms and catalytic strategies.Archives of biochemistry and biophysics · 2026Review
- Inhibition of Ring-Cleaving Dioxygenases by Natural Amino Acids.ACS omega · 2026Article
- Elucidating the Oxygen-Activation Mechanism in Nonheme MnInorganic chemistry · 2026Article
- EPR spectroscopy reveals glycerol-dependent activation of cysteamine dioxygenase (ADO) enables bidentate substrate coordination.The Journal of biological chemistry · 2026Article
- Hydralazine inhibits cysteamine dioxygenase to treat preeclampsia and senesce glioblastoma.Science advances · 2025Article
- Promiscuity in Molecular Mimics of the Cysteine Dioxygenase: Effects of Selenium in the Substrate and Cobalt as the Central Metal Ion.Angewandte Chemie (International ed. in English) · 2025Article
- An mRNA-display derived cyclic peptide scaffold reveals the substrate binding interactions of an N-terminal cysteine oxidase.Nature communications · 2025Article
- Influence of the second coordination sphere on OJournal of inorganic biochemistry · 2025Article
- Hydralazine inhibits cysteamine dioxygenase to treat preeclampsia and senesce glioblastoma.bioRxiv : the preprint server for biology · 2024Article
- Unveiling the mechanism of cysteamine dioxygenase: A combined HPLC-MS assay and metal-substitution approach.Methods in enzymology · 2024Article
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3 authors.
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Abstract
We investigated the metal-substituted catalytic activity of human cysteamine dioxygenase (ADO), an enzyme pivotal in regulating thiol metabolism and contributing to oxygen homeostasis. Our findings demonstrate the catalytic competence of cobalt(II)- and nickel(II)-substituted ADO in cysteamine oxygenation. Notably, Co(II)-ADO exhibited superiority over Ni(II)-ADO despite remaining significantly less active than the natural enzyme. Structural analyses through X-ray crystallography and cobalt K-edge excitation confirmed successful metal substitution with minimal structural perturbations. This provided a robust structural basis, supporting a conserved catalytic mechanism tailored to distinct metal centers. This finding challenges the proposed high-valent ferryl-based mechanism for thiol dioxygenases, suggesting a non-high-valent catalytic pathway in the native enzyme. Further investigation of the cysteamine-bound or a peptide mimic of
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