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 +6 more
doaj +4 more sources
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.
Patrick Rühl +4 more
doaj +6 more sources
Human ultrarare genetic disorders of sulfur metabolism demonstrate redundancies in H2S homeostasis [PDF]
Redox Biology, 2022 Regulation of H2S homeostasis in humans is poorly understood. Therefore, we assessed the importance of individual enzymes in synthesis and catabolism of H2S by studying patients with respective genetic defects.
Viktor Kožich +27 more
doaj +3 more sources
Mechanism-based inhibition of human persulfide dioxygenase by γ-glutamyl-homocysteinyl-glycine. [PDF]
J Biol Chem, 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.
Kabil O +5 more
europepmc +4 more sources
Characterization of patient mutations in human persulfide dioxygenase (ETHE1) involved in H2S catabolism. [PDF]
J Biol Chem, 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 ...
Kabil O, Banerjee R.
europepmc +5 more sources
Cytoplasmic Localization of Sulfide:Quinone Oxidoreductase and Persulfide Dioxygenase of Cupriavidus pinatubonensis JMP134. [PDF]
Appl Environ Microbiol, 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 ...
Gao R, Liu H, Xun L.
europepmc +4 more sources
Crystal structure of human persulfide dioxygenase: structural basis of ethylmalonic encephalopathy. [PDF]
Hum Mol Genet, 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.
Pettinati I +3 more
europepmc +4 more sources
Structural and biochemical analyses indicate that a bacterial persulfide dioxygenase-rhodanese fusion protein functions in sulfur assimilation. [PDF]
J Biol Chem, 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.
Motl N +4 more
europepmc +4 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.
Shen J +5 more
europepmc +4 more sources
HIF-1 Has a Central Role in Caenorhabditis elegans Organismal Response to Selenium [PDF]
Frontiers in Genetics, 2020 Selenium is a trace element for most organisms; its deficiency and excess are detrimental. Selenium beneficial effects are mainly due to the role of the 21st genetically encoded amino acid selenocysteine (Sec).
Laura Romanelli-Credrez +3 more
doaj +4 more sources