ArticleThe Journal of biological chemistry2014
Mercaptosuccinate dioxygenase, a cysteine dioxygenase homologue, from Variovorax paradoxus strain B4 is the key enzyme of mercaptosuccinate degradation.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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18 citing papers in PubMed, 28 citations in OpenAlex.
- Recent discoveries in mono- and dinuclear nonheme iron enzymes: Emerging mechanisms and catalytic strategies.Archives of biochemistry and biophysics · 2026Review
- EPR spectroscopy reveals glycerol-dependent activation of cysteamine dioxygenase (ADO) enables bidentate substrate coordination.The Journal of biological chemistry · 2026Article
- Influence of the second coordination sphere on OJournal of inorganic biochemistry · 2025Article
- Kinetic and Spectroscopic Investigation of the Y157F and C93G/Y157F Variants of Cysteine Dioxygenase: Dissecting the Roles of the Second-Sphere Residues C93 and Y157.Biochemistry · 2024Article
- A Nonheme Iron(III) Superoxide Complex Leads to Sulfur Oxygenation.Journal of the American Chemical Society · 2024Article
- Spectroscopic analysis of the mammalian enzyme cysteine dioxygenase.Methods in enzymology · 2023Article
- Differences in the Second Coordination Sphere Tailor the Substrate Specificity and Reactivity of Thiol Dioxygenases.Accounts of chemical research · 2022Article
- Charge Maintenance during Catalysis in Nonheme Iron Oxygenases.ACS catalysis · 2022Article
- Low-Spin Cyanide Complexes of 3-Mercaptopropionic Acid Dioxygenase (MDO) Reveal the Impact of Outer-Sphere SHY-Motif Residues.Inorganic chemistry · 2021Article
- Characterization of the nonheme iron center of cysteamine dioxygenase and its interaction with substrates.The Journal of biological chemistry · 2020Article
- Carbon-fluorine bond cleavage mediated by metalloenzymes.Chemical Society reviews · 2020Review
- Spectroscopic Investigation of Cysteamine Dioxygenase.Biochemistry · 2020Article
- Biochemical characterization and essentiality ofThe Journal of biological chemistry · 2018Article
- Proteomic analysis of organic sulfur compound utilisation in Advenella mimigardefordensis strain DPN7T.PloS one · 2017Article
- Influence of cysteine 164 on active site structure in rat cysteine dioxygenase.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2016Article
- Substrate and Cofactor Range Differences of Two Cysteine Dioxygenases from Ralstonia eutropha H16.Applied and environmental microbiology · 2016Article
- The cysteine dioxygenase homologue from Pseudomonas aeruginosa is a 3-mercaptopropionate dioxygenase.The Journal of biological chemistry · 2015Article
- Structure of 3-mercaptopropionic acid dioxygenase with a substrate analog reveals bidentate substrate binding at the iron center.The Journal of biological chemistryArticle
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3 authors at 2 institutions in 2 countries.
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Abstract
The versatile thiol mercaptosuccinate has a wide range of applications, e.g. in quantum dot research or in bioimaging. Its metabolism is investigated in Variovorax paradoxus strain B4, which can utilize this compound as the sole source of carbon and sulfur. Proteomic studies of strain B4 resulted in the identification of a putative mercaptosuccinate dioxygenase, a cysteine dioxygenase homologue, possibly representing the key enzyme in the degradation of mercaptosuccinate. Therefore, the putative mercaptosuccinate dioxygenase was heterologously expressed, purified, and characterized in this study. The results clearly demonstrated that the enzyme utilizes mercaptosuccinate with concomitant consumption of oxygen. Thus, the enzyme is designated as mercaptosuccinate dioxygenase. Succinate and sulfite were verified as the final reaction products. The enzyme showed an apparent Km of 0.4 mM, and a specific activity (Vmax) of 20.0 μmol min(-1) mg(-1) corresponding to a kcat of 7.7 s(-1). Furthermore, the enzyme was highly specific for mercaptosuccinate, no activity was observed with cysteine, dithiothreitol, 2-mercaptoethanol, and 3-mercaptopropionate. These structurally related thiols did not have an inhibitory effect either. Fe(II) could clearly be identified as metal cofactor of the mercaptosuccinate dioxygenase with a content of 0.6 mol of Fe(II)/mol of enzyme. The recently proposed hypothesis for the degradation pathway of mercaptosuccinate based on proteome analyses could be strengthened in the present study. (i) Mercaptosuccinate is first converted to sulfinosuccinate by this mercaptosuccinate dioxygenase; (ii) sulfinosuccinate is spontaneously desulfinated to succinate and sulfite; and (iii) whereas succinate enters the central metabolism, sulfite is detoxified by the previously identified putative molybdopterin oxidoreductase.
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