Max-Planck Laboratory for Computational Biophysical Chemistry.

Carbon dioxide is one of the most abundant greenhouse gases associated with global warming. One of the main goals to reduce global warming’s adversary effects is to reduce its emission and develop alternative methods to transform this gas into valuable compounds.

In our lab we try to understand how enzymes fix CO2 and transform it to organic compounds with high efficiency. We have studied the reaction mechanism of RuBisCO, one of the most abundant proteins that fixes most of atmospheric CO2 in the Calvin cycle. Although abundant, RuBisCO is not the most efficient one. To learn from the best in Nature, we focused on the family of Enoyl-crotonyl-CoA carboxylase/reductase, which possess the fastest fixation rate observed in enzymes and no side reaction with oxygen. At the end, we would like to disclose the whole catalytic cycle: possible conformational changes of the protein in the catalytic cycle, CO2 binding in the active site and the reaction mechanism to form the products.

To address the CO2 distribution in enzymes and the associated conformational changes, we work in close collaboration with Prof. Grubmüller at the Max-Planck Institute Göttingen in Germany in the established Computational Reaction Dynamics Max-Planck Partner group.

The reaction mechanism is elucidated from a computational point of view by us. Our results, together with the biochemical characterization of the protein structure with Prof. Soichi at Stanford and the kinetics in the group of Prof. Erb at the Max-Planck Institute Marburg, provide a detailed picture of how these molecular machines are able to transform CO2 efficiently.

Our final goal is to understand how these enzymes work and then design new variants with enhanced efficiency to be applied in biocatalysis.