ArticleNature structural & molecular biology2025
A scaffold for quinone channeling between membrane and soluble bacterial oxidoreductases.
Article in Nature structural & molecular biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Quinone-transporting filaments expand bioenergetic capacity in Gram-positive Bacillota.Nature microbiology · 2026Article
- Semiartificial COChemical reviews · 2026Review
- A Bacillales-specific tubular scaffold essential for NADH dehydrogenase activity.Nature communications · 2026Article
- Shedding light on YfhS and YjlC: novel effectors of the NADH dehydrogenase activity of the electron transport chain inbioRxiv : the preprint server for biology · 2026Article
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Authors and funding
17 authors.
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Abstract
Redox processes are at the heart of energetic metabolism that drives life on earth. By extension, complex and efficient electron transfer wires are necessary to connect the various metabolic pathways that are often located in distinct cellular compartments. Here, we uncovered a structural module that enables channeling of quinones from the membrane to various water-soluble redox catalytic units in prokaryotes. Using X-ray crystallography and cryo-electron microscopy, we determined the structure of the unusual bacterial formate dehydrogenase ForCE that contains four ForC catalytic subunits docked around a membrane-associated tetrameric ForE central scaffold. In the latter, a conserved domain that we propose to name helical membrane plugin (HMP) was identified as essential to link formate oxidation, in Bacillus subtilis, to the aerobic respiratory chain. Our bioinformatic analysis indicates that this HMP is associated with different quinone-reducing oxidoreductases, highlighting its broad importance as a functional unit to wire electrons between a given catalytic redox center and the quinone pool.
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