title: Characterizations of Two Bacterial Persulfide Dioxygenases of the Metallo-β-lactamase Superfamily.
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.
authors.affiliation: From the School of Molecular Biosciences, Washington State University, Pullman, Washington 99164-4660.
authors.forename: Steven A
authors.initials: SA
authors.lastname: Sattler
authors.affiliation: From the School of Molecular Biosciences, Washington State University, Pullman, Washington 99164-4660, the State Key Laboratory of Microbial Technology, Shandong University, Jinan, Shandong, China, and.
authors.forename: Xia
authors.initials: X
authors.lastname: Wang
authors.affiliation: the Department of Chemistry, Washington State University, Pullman, Washington 99164-4630.
authors.forename: Kevin M
authors.initials: KM
authors.lastname: Lewis
authors.affiliation: From the School of Molecular Biosciences, Washington State University, Pullman, Washington 99164-4660.
authors.forename: Preston J
authors.initials: PJ
authors.lastname: DeHan
authors.affiliation: the Department of Chemistry, Washington State University, Pullman, Washington 99164-4630.
authors.forename: Chung-Min
authors.initials: CM
authors.lastname: Park
authors.affiliation: the State Key Laboratory of Microbial Technology, Shandong University, Jinan, Shandong, China, and.
authors.forename: Yufeng
authors.initials: Y
authors.lastname: Xin
authors.affiliation: the State Key Laboratory of Microbial Technology, Shandong University, Jinan, Shandong, China, and.
authors.forename: Honglei
authors.initials: H
authors.lastname: Liu
authors.affiliation: the Department of Chemistry, Washington State University, Pullman, Washington 99164-4630.
authors.forename: Ming
authors.initials: M
authors.lastname: Xian
authors.affiliation: From the School of Molecular Biosciences, Washington State University, Pullman, Washington 99164-4660, the State Key Laboratory of Microbial Technology, Shandong University, Jinan, Shandong, China, and luying_xun@vetmed.wsu.edu.
authors.forename: Luying
authors.initials: L
authors.lastname: Xun
authors.affiliation: From the School of Molecular Biosciences, Washington State University, Pullman, Washington 99164-4660, the Department of Chemistry, Washington State University, Pullman, Washington 99164-4630 chkang@wsu.edu.
authors.forename: ChulHee
authors.initials: C
authors.lastname: Kang
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry*; D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D049308:Dioxygenases / Q000737:chemistry*; D005978:Glutathione; D006860:Hydrogen Bonding; D007700:Kinetics; D008958:Models, Molecular; D008969:Molecular Sequence Data; D016941:Myxococcus xanthus / Q000201:enzymology*; D011485:Protein Binding; D020836:Protein Structure, Quaternary; D016958:Pseudomonas putida / Q000201:enzymology*; D012996:Solutions; D013379:Substrate Specificity; D001618:beta-Lactamases / Q000737:chemistry*
chemical_list: D001426:Bacterial Proteins; D012996:Solutions; D049308:Dioxygenases; C477654:sulfur dioxygenase; D001618:beta-Lactamases; D005978:Glutathione
keywords: ETHE1; bacterial metabolism; bioenergetics; dioxygenase; enzyme structure; glutathione; glyoxalase II; sulfur