Bibliographic Details
| Title: |
Coupling CO2 Reduction and Acetyl‐CoA Formation: The Role of a CO Capturing Tunnel in Enzymatic Catalysis. |
| Authors: |
Ruickoldt, Jakob, Jeoung, Jae‐Hun, Rudolph, Maik Alexander, Lennartz, Frank, Kreibich, Julian, Schomäcker, Reinhard, Dobbek, Holger |
| Source: |
Angewandte Chemie International Edition; 7/29/2024, Vol. 63 Issue 31, p1-8, 8p |
| Subject Terms: |
ACETYLCOENZYME A, CATALYSIS, BIOCHEMICAL substrates, BINDING sites |
| Abstract: |
The bifunctional CO‐dehydrogenase/acetyl‐CoA synthase (CODH/ACS) complex couples the reduction of CO2 to the condensation of CO with a methyl moiety and CoA to acetyl‐CoA. Catalysis occurs at two sites connected by a tunnel transporting the CO. In this study, we investigated how the bifunctional complex and its tunnel support catalysis using the CODH/ACS from Carboxydothermus hydrogenoformans as a model. Although CODH/ACS adapted to form a stable bifunctional complex with a secluded substrate tunnel, catalysis and CO transport is even more efficient when two monofunctional enzymes are coupled. Efficient CO channeling appears to be ensured by hydrophobic binding sites for CO, which act in a bucket‐brigade fashion rather than as a simple tube. Tunnel remodeling showed that opening the tunnel increased activity but impaired directed transport of CO. Constricting the tunnel impaired activity and CO transport, suggesting that the tunnel evolved to sequester CO rather than to maximize turnover. [ABSTRACT FROM AUTHOR] |
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| Database: |
Complementary Index |
