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TitleAn electron-bifurcating "plug" to a protein nanowire in tungsten-dependent aldehyde detoxification.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 122, Issue 30, Page e2501900122, Year 2025
Publish dateJul 29, 2025
AuthorsXiang Feng / Gerrit J Schut / Saisuki Putumbaka / Huilin Li / Michael W W Adams /
PubMed AbstractMembers of the tungsten-containing oxidoreductase (WOR) family, which contain a tungstopyranopterin (Tuco) cofactor, are typically either monomeric (WorL) or heterodimeric (WorLS). These enzymes ...Members of the tungsten-containing oxidoreductase (WOR) family, which contain a tungstopyranopterin (Tuco) cofactor, are typically either monomeric (WorL) or heterodimeric (WorLS). These enzymes oxidize aldehydes to the corresponding acids while reducing the redox protein ferredoxin. They have been structurally characterized mainly using WORs from hyperthermophilic archaea. The WORs of some bacteria contain three additional subunits of the BfuABC family and these chimeric WorABCSL enzymes catalyze an electron-bifurcating reaction in which aldehyde oxidation is coupled to the simultaneous reduction of ferredoxin and nicotinamide adenine dinucleotide. In human gut microbes, electron bifurcation by WorABSL is proposed to enable the detoxification of aldehydes generated from cooked foods and in the tungstocentric production of beneficial short chain fatty acids from lactate, potentially impacting health. Herein we present the high-resolution cryogenic electron microscopy (cryo-EM) structure of the WorABCSL purified from the bacterium The structure reveals a surprising 1:3 stoichiometry between WorABC and WorSL, with the WorSL units forming a nanowire-like architecture leading from three Tuco-containing catalytic sites in WorL via strings of multiple iron-sulfur clusters in WorS to a single bifurcating WorABC core. Our structure uncovers a distinct domain arrangement that links three Tuco-dependent aldehyde oxidation sites with the bifurcation process and potentially facilitates environmental aldehyde oxidation.
External linksProc Natl Acad Sci U S A / PubMed:40694326 / PubMed Central
MethodsEM (single particle)
Resolution2.7 - 3.2 Å
Structure data

EMDB-48541: WorABC region of the electron bifurcating Tungstopyranopterin-containing oxidoreductase WorABCSL with NADH
Method: EM (single particle) / Resolution: 3.0 Å

EMDB-48542: Electron bifurcating tungstopyranopterin-containing aldehyde oxidoreductase WorABCSL with NADH
Method: EM (single particle) / Resolution: 2.7 Å

48543

9mqx

EMDB-48543, PDB-9mqx:
Electron-bifurcating Tungstopyranopterin-containing aldehyde oxidoreductase with NADH
Method: EM (single particle) / Resolution: 3.0 Å

EMDB-48545: electron-bifurcating tungstopyranopterin-containing aldehyde oxidoreductase WorABCSL
Method: EM (single particle) / Resolution: 3.2 Å

Chemicals

ChemComp-SF4:
IRON/SULFUR CLUSTER

ChemComp-FES:
FE2/S2 (INORGANIC) CLUSTER

ChemComp-ZN:
Unknown entry

ChemComp-FMN:
FLAVIN MONONUCLEOTIDE

ChemComp-NAI:
1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE

ChemComp-PTE:
TUNGSTOPTERIN COFACTOR

ChemComp-MG:
Unknown entry

Source
  • acetomicrobium mobile (bacteria)
KeywordsOXIDOREDUCTASE / electron bifurcation

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