9G7J
Crystal structure of the tungsten-dependent aldehyde:ferredoxin oxidoreductase from Clostridium autoethanogenum.
This is a non-PDB format compatible entry.
Summary for 9G7J
| Entry DOI | 10.2210/pdb9g7j/pdb |
| Descriptor | Aldehyde ferredoxin oxidoreductase, IRON/SULFUR CLUSTER, Tungstopterin cofactor, ... (7 entities in total) |
| Functional Keywords | anaerobic metabolism, metalloenzyme, tungstopterin, ethanol production, acetogenic bacteria, iron-sulfur cluster, oxidoreductase |
| Biological source | Clostridium autoethanogenum DSM 10061 |
| Total number of polymer chains | 2 |
| Total formula weight | 135767.14 |
| Authors | Lemaire, O.N.,Wagner, T. (deposition date: 2024-07-21, release date: 2025-05-28, Last modification date: 2026-01-07) |
| Primary citation | Lemaire, O.N.,Belhamri, M.,Shevchenko, A.,Wagner, T. Carbon-monoxide-driven bioethanol production operates through a tungsten-dependent catalyst. Nat.Chem.Biol., 22:28-36, 2026 Cited by PubMed Abstract: Microbial alcohol production from waste gases is a game changer for sustainable carbon cycling and remediation. While the biotechnological process using Clostridium autoethanogenum to transform syngas (H, CO and CO) is blooming, scientific debates remain on the ethanol biosynthesis pathway. Here, we experimentally validated that ethanol production is initiated through a tungsten-dependent aldehyde:ferredoxin oxidoreductase (AFOR), which reduces acetate to acetaldehyde. The reaction, thermodynamically unfavorable under standard conditions, has been considered by many as unsuitable in vivo but is rather approved by metabolic modeling. To answer this riddle, we demonstrated that the thermodynamic coupling of CO oxidation and ethanol synthesis allows acetate reduction. The experiments, performed with native CO dehydrogenase and AFOR, highlighted the key role of ferredoxin in stimulating the activity of both metalloenzymes and electron shuttling. The crystal structure of holo AFOR, refined to 1.59-Å resolution, and its biochemical characterization provide new insights into the cofactor chemistry and the specificities of this enzyme, fundamental to sustainable biofuel production. PubMed: 41162695DOI: 10.1038/s41589-025-02055-3 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.59 Å) |
Structure validation
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