ArticleThe Journal of biological chemistry2015
Characterizations of Two Bacterial Persulfide Dioxygenases of the Metallo-β-lactamase Superfamily.
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 32 papers.
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Who cites it
32 citing papers in PubMed, 41 citations in OpenAlex.
- Medicinal Plants: A Promising Therapeutic Approach for Addressing Antimicrobial Resistance.International journal of molecular sciences · 2026Review
- A Dinuclear Iron(II) Persulfide Complex Reacts with OJournal of the American Chemical Society · 2026Article
- The genetic repertoire underlying electrogenic sulphur oxidation in cable bacteria.BMC genomics · 2026Article
- Self-bioRxiv : the preprint server for biology · 2026Article
- Structure and function of persulfide dioxygenase fromiScience · 2026Article
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- Pulling back the mitochondria's iron curtain.npj metabolic health and disease · 2025Review
- Mechanism of Intracellular Elemental Sulfur Oxidation inInternational journal of molecular sciences · 2024Article
- Antibiotic Potentiation Through Phytochemical-Based Efflux Pump Inhibitors to Combat Multidrug Resistance Bacteria.Medicinal chemistry (Shariqah (United Arab Emirates)) · 2024Review
- Evolutionary adaptation from hydrolytic to oxygenolytic catalysis at the α/β-hydrolase fold.Chemical science · 2023Article
- Review
- Production of selenium nanoparticles occurs through an interconnected pathway of sulphur metabolism and oxidative stress response in Pseudomonas putida KT2440.Microbial biotechnology · 2023Article
- Generation and Physiology of Hydrogen Sulfide and Reactive Sulfur Species in Bacteria.Antioxidants (Basel, Switzerland) · 2022Review
- Rhodaneses minimize the accumulation of cellular sulfane sulfur to avoid disulfide stress during sulfide oxidation in bacteria.Redox biology · 2022Article
- Innovation and tinkering in the evolution of oxidases.Protein science : a publication of the Protein Society · 2022Review
- Thioesterase enzyme families: Functions, structures, and mechanisms.Protein science : a publication of the Protein Society · 2022Article
- Metallo-β-lactamases in the Age of Multidrug Resistance: From Structure and Mechanism to Evolution, Dissemination, and Inhibitor Design.Chemical reviews · 2021Review
- HThe Journal of biological chemistry · 2020Review
- The Response ofmBio · 2020Article
- Spectroscopic and Electronic Structure Study of ETHE1: Elucidating the Factors Influencing Sulfur Oxidation and Oxygenation in Mononuclear Nonheme Iron Enzymes.Journal of the American Chemical Society · 2018Article
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Authors and funding
10 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Persulfide dioxygenases (PDOs), also known as sulfur dioxygenases (SDOs), oxidize glutathione persulfide (GSSH) to sulfite and GSH. PDOs belong to the metallo-β-lactamase superfamily and play critical roles in animals, plants, and microorganisms, including sulfide detoxification. The structures of two PDOs from human and Arabidopsis thaliana have been reported; however, little is known about the substrate binding and catalytic mechanism. The crystal structures of two bacterial PDOs from Pseudomonas putida and Myxococcus xanthus were determined at 1.5- and 2.5-Å resolution, respectively. The structures of both PDOs were homodimers, and their metal centers and β-lactamase folds were superimposable with those of related enzymes, especially the glyoxalases II. The PDOs share similar Fe(II) coordination and a secondary coordination sphere-based hydrogen bond network that is absent in glyoxalases II, in which the corresponding residues are involved instead in coordinating a second metal ion. The crystal structure of the complex between the Pseudomonas PDO and GSH also reveals the similarity of substrate binding between it and glyoxalases II. Further analysis implicates an identical mode of substrate binding by known PDOs. Thus, the data not only reveal the differences in metal binding and coordination between the dioxygenases and the hydrolytic enzymes in the metallo-β-lactamase superfamily, but also provide detailed information on substrate binding by PDOs.
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