ArticleScientific reports2018
Structural insights into the electron/proton transfer pathways in the quinol:fumarate reductase from Desulfovibrio gigas.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 16 citations in OpenAlex.
- Shifts in ruminant fermentation during inhibition of methanogenesis are reflected in the isotope compositions of volatile fatty acids.Applied and environmental microbiology · 2026Article
- Structural basis of menaquinone reduction by succinate dehydrogenase from Chloroflexus aurantiacus.Nature communications · 2025Article
- Red seaweed supplementation suppresses methanogenesis in the rumen, revealing potentially advantageous traits among hydrogenotrophic bacteria.Microbiome · 2025Article
- Functionality of the NaArchives of microbiology · 2023Article
- Genomic insight into iron acquisition by sulfate-reducing bacteria in microaerophilic environments.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2023Review
- Membrane Potential-requiring Succinate Dehydrogenase Constitutes the Key to Propionate Oxidation and Is Unique to Syntrophic Propionate-oxidizing Bacteria.Microbes and environments · 2023Article
- Architecture of the mycobacterial succinate dehydrogenase with a membrane-embedded Rieske FeS cluster.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Cryo-EM structure of trimeric Mycobacterium smegmatis succinate dehydrogenase with a membrane-anchor SdhF.Nature communications · 2020Article
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Authors and funding
13 authors at 4 institutions in 3 countries.
Funding
Abstract
The membrane-embedded quinol:fumarate reductase (QFR) in anaerobic bacteria catalyzes the reduction of fumarate to succinate by quinol in the anaerobic respiratory chain. The electron/proton-transfer pathways in QFRs remain controversial. Here we report the crystal structure of QFR from the anaerobic sulphate-reducing bacterium Desulfovibrio gigas (D. gigas) at 3.6 Å resolution. The structure of the D. gigas QFR is a homo-dimer, each protomer comprising two hydrophilic subunits, A and B, and one transmembrane subunit C, together with six redox cofactors including two b-hemes. One menaquinone molecule is bound near heme b
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