Scientists replicate enzyme that captures carbon

Scientists at King’s College London have recreated the active site of acetyl-CoA synthase, an enzyme that captures carbon from the atmosphere. The work, carried out in collaboration with Imperial College London, improves our understanding of this key enzyme and points to potential new solutions for capturing CO2.₂ from the atmosphere in the fight against climate change.

The team, led by Dr Rebecca Musgrave from the Department of Chemistry and Dr Daniel Wilson from UCL, Active Site—where chemical reactions occur— enzyme Acetyl-CoA synthase (ACS).

ACS converts CO₂ It is converted into acetyl coenzyme A, a molecule essential for living organisms. Published In Journal of the American Chemical Society.

ACS is best known for its role in the acetate or Krebs cycle, a series of chemical reactions in living organisms in which acetate is oxidized to produce energy, and is therefore essential for the storage and release of energy, as well as the capture of CO.₂ It is absorbed from the atmosphere and stored as carbon.

The team’s new model was able to recreate this chemical reaction in the lab, capturing carbon from the atmosphere and storing it as acetyl coenzyme A.

Enzymes act as biocatalysts, Chemical reactionAs such, they serve important functions in nature, including human biology.

The chemical pathways produced by enzymes have developed over billions of years into large, complex living systems, making them extremely difficult to study and replicate in the laboratory. To study enzymes, scientists often recreate smaller molecular versions of the enzymes, or models of their “active sites,” in the lab.

ACS enzymes are present in bacteria and in some Single-celled organisms They function without oxygen, building complex organic molecules from carbon dioxide and hydrogen. Attempts have been made to model the active site of enzymes in the laboratory, but no one has been able to accurately recreate the shape and electronic environment of the carbon-capturing active site.

Lead researcher Dr Daniel Wilson, from UCL, said: “Scientists have studied the ACS enzyme for decades but have had difficulty elucidating the mechanism by which acetyl-coenzyme A is produced in the enzyme’s active site. In our study, we report an active site model, a molecular cluster featuring two nickel atoms, that mimics a remarkably similar shape and size to the active site of the ACS enzyme.”

“We are pleased to announce that our model Carbon monoxide As a result, we have succeeded in synthesizing ACS enzymes in a way that mimics the way they produce acetyl-CoA in nature.”

Working with Dr Maxie Roesler from Imperial College, the team used a technique called electron paramagnetic spectroscopy to study the steps involved, and believe their results will provide valuable insights for scientists studying ACS enzymes, and other enzymes involved in atmospheric carbon fixation. Carbon capture.

Dr Rebecca Musgrave said: “Our new model paves the way to a better understanding of how this reaction works. By studying the individual reaction steps using electron paramagnetic resonance spectroscopy and other techniques, what we learn can be used to help design artificial catalysts. Industrial Applications.

“This could have applications in a variety of areas, including new ways to capture CO2.₂ It takes carbon from the atmosphere and uses it as a feedstock to produce carbon-based chemicals, such as biofuels for cars and medicines.”

The researchers also hope that those working in the field of enzyme spectroscopy will be able to apply the new model to their own research.

Dr Musgrave said: “Natural enzymes carry out these amazing transformations incredibly quickly and efficiently, in ways that are extremely difficult to replicate in the laboratory. Our new model brings us a step closer to understanding how these biological systems do it so well, which may enable us to design catalysts on an industrial scale to replicate nature’s transformative capabilities and tackle important societal problems such as climate change.”