ArticleHuman molecular genetics2015
Crystal structure of human persulfide dioxygenase: structural basis of ethylmalonic encephalopathy.
Article in Human molecular genetics, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed, 63 citations in OpenAlex.
- A Dinuclear Iron(II) Persulfide Complex Reacts with OJournal of the American Chemical Society · 2026Article
- Self-bioRxiv : the preprint server for biology · 2026Article
- Structure and function of persulfide dioxygenase fromiScience · 2026Article
- Hydrogen Sulfide Consumption and Cell Bioenergetics in Human (Patho)physiology.Handbook of experimental pharmacology · 2026Review
- Enzymes that generate and regulate intracellular persulfides and polysulfides: mechanistic insights and inhibitors.Frontiers in physiology · 2026Review
- Article
- Review
- Pulling back the mitochondria's iron curtain.npj metabolic health and disease · 2025Review
- Emerging roles of hydrogen sulfide-metabolizing enzymes in cancer.Redox report : communications in free radical research · 2024Review
- Mechanism of Intracellular Elemental Sulfur Oxidation inInternational journal of molecular sciences · 2024Article
- GlialProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Disruption of Bioenergetics in the Intestine of Wistar Rats Caused by Hydrogen Sulfide and Thiosulfate: A Potential Mechanism of Chronic Hemorrhagic Diarrhea in Ethylmalonic Encephalopathy.Cell biochemistry and biophysics · 2023Article
- Persulfide Biosynthesis Conserved Evolutionarily in All Organisms.Antioxidants & redox signaling · 2023Review
- Sensing and regulation of reactive sulfur species (RSS) in bacteria.Current opinion in chemical biology · 2023Review
- Supersulfide catalysis for nitric oxide and aldehyde metabolism.Science advances · 2023Article
- Role of Hydrogen Sulfide in Inflammatory Bowel Disease.Antioxidants (Basel, Switzerland) · 2023Review
- Generation and Physiology of Hydrogen Sulfide and Reactive Sulfur Species in Bacteria.Antioxidants (Basel, Switzerland) · 2022Review
- Hydrogen Sulfide Metabolizing Enzymes in the Intestinal Mucosa in Pediatric and Adult Inflammatory Bowel Disease.Antioxidants (Basel, Switzerland) · 2022Article
- Electronic structures and spectroscopic signatures of diiron intermediates generated by ODalton transactions (Cambridge, England : 2003) · 2021Article
- Ethylmalonic Encephalopathy 1 Protein Is Increased in Colorectal Adenocarcinoma.Anticancer research · 2021Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
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. hETHE1 is a mono-iron binding member of the metallo-β-lactamase (MBL) fold superfamily. We report crystallographic analysis of hETHE1 in complex with iron to 2.6 Å resolution. hETHE1 contains an αββα MBL-fold, which supports metal-binding by the side chains of an aspartate and two histidine residues; three water molecules complete octahedral coordination of the iron. The iron binding hETHE1 enzyme is related to the 'classical' di-zinc binding MBL hydrolases involved in antibiotic resistance, but has distinctive features. The histidine and aspartate residues involved in iron-binding in ETHE1, occupy similar positions to those observed across both the zinc 1 and zinc 2 binding sites in classical MBLs. The active site of hETHE1 is very similar to an ETHE1-like enzyme from Arabidopsis thaliana (60% sequence identity). A channel leading to the active site is sufficiently large to accommodate a GSSH substrate. Some of the observed hETHE1 clinical mutations cluster in the active site region. The structure will serve as a basis for detailed functional and mechanistic studies on ETHE1 and will be useful in the development of selective MBL inhibitors.
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