An international study coordinated by Cristiano Mota and Maria João Romão, from the XTAL - Macromolecular Crystallography Lab at UCIBIO-NOVA FCT, in collaboration with ITQB-NOVA, reveals how a highly efficient natural enzyme captures and converts carbon dioxide (CO₂). This breakthrough provides the structural knowledge needed to inspire new green technologies.
Reducing CO₂ levels in the atmosphere is undoubtedly one of today's greatest scientific and environmental challenges. While industrial technologies are being developed to capture and convert CO₂, nature has already been performing this chemical transformation for billions of years using enzymes. Now, a team of researchers has uncovered the inner workings of this biological system with an unprecedented level of detail.
The study, recently published in the prestigious journal Angewandte Chemie International Edition, was coordinated by Maria João Romão, leader of the XTAL - Macromolecular Crystallography Lab, and Cristiano Mota, senior researcher in the same Lab at UCIBIO - NOVA FCT. The research has as first authors Guilherme Vilela-Alves (UCIBIO - NOVA FCT), PhD student under the supervision of the coordinators of the study and Rita Rebelo Manuel, under the supervision of Inês Cardoso Pereira (ITQB-NOVA).
By combining Structural Biology, Enzymology, Protein Engineering, Physics, and Computational Modeling, the team was able to map the exact path CO₂ takes within the protein. Using advanced X-ray Crystallography techniques at the European Synchrotron Radiation Facility (ESRF) in France, the researchers visualized how gas molecules move inside the enzyme.
The discovery was surprising: CO₂ is guided through internal tunnels into a small cavity adjacent to the active site, described by the researchers as a "molecular waiting room." By strategically retaining the CO₂ in this location, the enzyme concentrates the molecule close to the reaction zone, ensuring a much faster and more efficient process before it is converted into a molecule capable of storing energy.
"Understanding at an atomic detail how these enzymes work and guide CO₂ inside gives us the fundamental knowledge needed to design more efficient technologies," explain Cristiano Mota and Maria João Romão. "This discovery directly inspires the development of new artificial catalysts for industrial carbon capture and clean energy production."
In essence, the researchers realized that the enzyme evolved a smart structural strategy: concentrating the substrate (CO₂) as close as possible to the reaction site, significantly increasing the efficiency of the entire process. This intelligent mechanism opens up new technological possibilities for developing improved enzymes for industrial carbon capture and creating nature-inspired catalysts for the production of green fuels.
This multidisciplinary research also included the collaboration of researchers from the European Synchrotron Radiation Facility (ESRF) and the Université Grenoble Alpes/CNRS/CEA (France), as well as the Jerzy Haber Institute of Catalysis and Surface Chemistry, Polish Academy of Sciences, Krakow (Poland).
Read the full paper:
Angewandte Chemie International Edition
Structural Insights Into CO2 Transport Pathways in a W-Formate Dehydrogenase: Structural Basis for CO2 Reduction. Guilherme Vilela-Alves, Rita Rebelo Manuel, Guilherme Martins, Philippe Carpentier, Agata Raczyńska, Maciej Szaleniec, Inês A. Cardoso Pereira, Maria João Romão and Cristiano Mota.
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