Conformational dynamics of a multienzyme complex in anaerobic carbon fixation.
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PubMed
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| Auteurs principaux: | , , , , , , , |
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| Format: | Artículo científico |
| Langue: | en |
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Science (New York, N.Y.)
2025
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| _version_ | 1868266249882959873 |
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| author | Yin, Max Dongsheng Lemaire, Olivier N Rosas Jiménez, José Guadalupe Belhamri, Mélissa Shevchenko, Anna Hummer, Gerhard Wagner, Tristan Murphy, Bonnie J |
| author_facet | Yin, Max Dongsheng Lemaire, Olivier N Rosas Jiménez, José Guadalupe Belhamri, Mélissa Shevchenko, Anna Hummer, Gerhard Wagner, Tristan Murphy, Bonnie J Yin, Max Dongsheng Lemaire, Olivier N Rosas Jiménez, José Guadalupe Belhamri, Mélissa Shevchenko, Anna Hummer, Gerhard Wagner, Tristan Murphy, Bonnie J |
| collection | PubMed - marine biology |
| contents | Conformational dynamics of a multienzyme complex in anaerobic carbon fixation. Yin, Max Dongsheng Lemaire, Olivier N Rosas Jiménez, José Guadalupe Belhamri, Mélissa Shevchenko, Anna Hummer, Gerhard Wagner, Tristan Murphy, Bonnie J Acetate-CoA Ligase Acetyl Coenzyme A Aldehyde Oxidoreductases Anaerobiosis Bacterial Proteins Carbon Cycle Carbon Dioxide Catalytic Domain Clostridium Crystallography, X-Ray Electron Transport Iron-Sulfur Proteins Multienzyme Complexes Oxidation-Reduction Protein Conformation In the ancient microbial Wood-Ljungdahl pathway, carbon dioxide (CO) 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 , characterizing the molecular choreography of the overall reaction, including electron transfer to the CODH for CO 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 fixation in anaerobic organisms. |
| format | Artículo científico |
| id | pubmed_39883773 |
| institution | PubMed |
| language | en |
| publishDate | 2025 |
| publisher | Science (New York, N.Y.) |
| record_format | pubmed |
| spellingShingle | Conformational dynamics of a multienzyme complex in anaerobic carbon fixation. Yin, Max Dongsheng Lemaire, Olivier N Rosas Jiménez, José Guadalupe Belhamri, Mélissa Shevchenko, Anna Hummer, Gerhard Wagner, Tristan Murphy, Bonnie J Acetate-CoA Ligase Acetyl Coenzyme A Aldehyde Oxidoreductases Anaerobiosis Bacterial Proteins Carbon Cycle Carbon Dioxide Catalytic Domain Clostridium Crystallography, X-Ray Electron Transport Iron-Sulfur Proteins Multienzyme Complexes Oxidation-Reduction Protein Conformation Conformational dynamics of a multienzyme complex in anaerobic carbon fixation. Yin, Max Dongsheng Lemaire, Olivier N Rosas Jiménez, José Guadalupe Belhamri, Mélissa Shevchenko, Anna Hummer, Gerhard Wagner, Tristan Murphy, Bonnie J Acetate-CoA Ligase Acetyl Coenzyme A Aldehyde Oxidoreductases Anaerobiosis Bacterial Proteins Carbon Cycle Carbon Dioxide Catalytic Domain Clostridium Crystallography, X-Ray Electron Transport Iron-Sulfur Proteins Multienzyme Complexes Oxidation-Reduction Protein Conformation In the ancient microbial Wood-Ljungdahl pathway, carbon dioxide (CO) 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 , characterizing the molecular choreography of the overall reaction, including electron transfer to the CODH for CO 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 fixation in anaerobic organisms. |
| title | Conformational dynamics of a multienzyme complex in anaerobic carbon fixation. |
| topic | Acetate-CoA Ligase Acetyl Coenzyme A Aldehyde Oxidoreductases Anaerobiosis Bacterial Proteins Carbon Cycle Carbon Dioxide Catalytic Domain Clostridium Crystallography, X-Ray Electron Transport Iron-Sulfur Proteins Multienzyme Complexes Oxidation-Reduction Protein Conformation |
| url | https://pubmed.ncbi.nlm.nih.gov/39883773/ |