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Publication Abstract from PubMed

In the ancient microbial Wood-Ljungdahl pathway, carbon dioxide (CO(2)) is fixed in a multistep process that ends with acetyl-coenzyme A (acetyl-CoA) synthesis at the bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase complex (CODH/ACS). In this work, we present structural snapshots of the CODH/ACS from the gas-converting acetogen Clostridium autoethanogenum, characterizing the molecular choreography of the overall reaction, including electron transfer to the CODH for CO(2) reduction, methyl transfer from the corrinoid iron-sulfur protein (CoFeSP) partner to the ACS active site, and acetyl-CoA production. Unlike CODH, the multidomain ACS undergoes large conformational changes to form an internal connection to the CODH active site, accommodate the CoFeSP for methyl transfer, and protect the reaction intermediates. Altogether, the structures allow us to draw a detailed reaction mechanism of this enzyme, which is crucial for CO(2) fixation in anaerobic organisms.

Conformational dynamics of a multienzyme complex in anaerobic carbon fixation.,Yin MD, Lemaire ON, Rosas Jimenez JG, Belhamri M, Shevchenko A, Hummer G, Wagner T, Murphy BJ Science. 2025 Jan 31;387(6733):498-504. doi: 10.1126/science.adr9672. Epub 2025 , Jan 30. PMID:39883773^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.