Results 1 to 10 of about 657 (82)

Persulfide Dioxygenase From Acidithiobacillus caldus: Variable Roles of Cysteine Residues and Hydrogen Bond Networks of the Active Site [PDF]

Frontiers in Microbiology, 2018
Persulfide dioxygenases (PDOs) are abundant in Bacteria and also crucial for H2S detoxification in mitochondria. One of the two pdo-genes of the acidophilic bacterium Acidithiobacillus caldus was expressed in Escherichia coli.
Arnulf Kletzin, Patrick Ruhl
exaly   +8 more sources

Cupriavidus pinatubonensis JMP134 Alleviates Sulfane Sulfur Toxicity after the Loss of Sulfane Dehydrogenase through Oxidation by Persulfide Dioxygenase and Hydrogen Sulfide Release [PDF]

Metabolites, 2023
An incomplete Sox system lacking sulfane dehydrogenase SoxCD may produce and accumulate sulfane sulfur when oxidizing thiosulfate. However, how bacteria alleviate the pressure of sulfane sulfur accumulation remains largely unclear.
Yufeng Xin, Yaxin Wang, Honglin Zhang, Yu Wu, Yongzhen Xia, Huanjie Li, Xiaohua Qu   +6 more
doaj   +4 more sources

Characterization of Patient Mutations in Human Persulfide Dioxygenase (ETHE1) Involved in H2S Catabolism [PDF]

Journal of Biological Chemistry, 2012
Hydrogen sulfide (H(2)S) is a recently described endogenously produced gaseous signaling molecule that influences various cellular processes in the central nervous system, cardiovascular system, and gastrointestinal tract. The biogenesis of H(2)S involves the cytoplasmic transsulfuration enzymes, cystathionine β-synthase and γ-cystathionase, whereas ...
, Ömer Kabil
exaly   +6 more sources

Mechanism-based inhibition of human persulfide dioxygenase by γ-glutamyl-homocysteinyl-glycine [PDF]

Journal of Biological Chemistry, 2018
Hydrogen sulfide (H2S) is a signaling molecule with many beneficial effects. However, its cellular concentration is strictly regulated to avoid toxicity. Persulfide dioxygenase (PDO or ETHE1) is a mononuclear non-heme iron-containing protein in the sulfide oxidation pathway catalyzing the conversion of GSH persulfide (GSSH) to sulfite and GSH.
Nils Metzler-Nolte, , Ömer Kabil
exaly   +5 more sources

Cytoplasmic Localization of Sulfide:Quinone Oxidoreductase and Persulfide Dioxygenase of Cupriavidus pinatubonensis JMP134 [PDF]

Applied and Environmental Microbiology, 2017
ABSTRACT Heterotrophic bacteria have recently been reported to oxidize sulfide to sulfite and thiosulfate by using sulfide:quinone oxidoreductase (SQR) and persulfide dioxygenase (PDO). In chemolithotrophic bacteria, both SQR and PDO have been reported to function in the periplasmic space, with SQR as a peripheral membrane ...
Luying Xun
exaly   +5 more sources

Crystal structure of human persulfide dioxygenase: structural basis of ethylmalonic encephalopathy [PDF]

Human Molecular Genetics, 2015
The ethylmalonic encephalopathy protein 1 (ETHE1) catalyses the oxygen-dependent oxidation of glutathione persulfide (GSSH) to give persulfite and glutathione. Mutations to the hETHE1 gene compromise sulfide metabolism leading to the genetic disease ethylmalonic encephalopathy.
Jürgen Brem, Christopher Schofield, Ilaria Pettinati   +2 more
exaly   +5 more sources

Staphylococcus aureus CstB Is a Novel Multidomain Persulfide Dioxygenase-Sulfurtransferase Involved in Hydrogen Sulfide Detoxification [PDF]

Biochemistry, 2015
Hydrogen sulfide (H2S) is both a lethal gas and an emerging gasotransmitter in humans, suggesting that the cellular H2S level must be tightly regulated. CstB is encoded by the cst operon of the major human pathogen Staphylococcus aureus and is under the transcriptional control of the persulfide sensor CstR and H2S.
Katherine Edmonds, David Giedroc, Jiangchuan Shen   +2 more
exaly   +5 more sources

Structural and biochemical analyses indicate that a bacterial persulfide dioxygenase–rhodanese fusion protein functions in sulfur assimilation [PDF]

Journal of Biological Chemistry, 2017
Hydrogen sulfide (H2S) is a signaling molecule that is toxic at elevated concentrations. In eukaryotes, it is cleared via a mitochondrial sulfide oxidation pathway, which comprises sulfide quinone oxidoreductase, persulfide dioxygenase (PDO), rhodanese, and sulfite oxidase and converts H2S to thiosulfate and sulfate.
, Janet L Smith, Meredith Skiba
exaly   +5 more sources

Enzymes that generate and regulate intracellular persulfides and polysulfides: mechanistic insights and inhibitors [PDF]

Frontiers in Physiology
Reactive sulfur species (RSS), which include various persulfides and polysulfides, are generated by multiple enzymes in vivo and play critical roles in mammalian physiological processes such as redox signaling, metabolic regulation, radical scavenging ...
Ko Hirabayashi, Eita Sasaki, Hisashi Ohno, Orie Takayama, Sota Yamada, Kenjiro Hanaoka, Kenjiro Hanaoka   +6 more
doaj   +2 more sources

Structure and function of persulfide dioxygenase from <i>Pseudomonas aeruginosa</i>: Implications on H₂S homeostasis and interplay with nitric oxide. [PDF]

iScience
Hydrogen sulfide is an important signaling molecule, beneficial at physiological concentrations but harmful at higher levels, due to which a tight control of its bioavailability is essential. Here, we investigated persulfide dioxygenase, an enzyme involved in H2S catabolism, from the pathogen Pseudomonas aeruginosa (PaPDO). Deletion of the gene pdo led
Giordano F, Troilo F, Nastasi MR, Caruso L, Mellini M, Travaglini-Allocatelli C, Giardina G, Vicente JB, Rampioni G, Di Matteo A, Forte E, Giuffrè A.   +11 more
europepmc   +4 more sources