Carbon Dioxide Migration Pathways in Proteins.
Some of the most important biological processes, such as carbon fixation, are dependent on protein-gas interactions. The motion of CO2 through the enzyme phosphoenolpyruvate carboxykinase was investigated using extensive all-atom molecular dynamics simulations. Three discrete migration pathways were located, suggesting the protein directs the movement of CO2. The chemical nature of these pathways is discussed, as are their biotechnological ramifications.
Center for Advanced Scientific Computing and Modeling (CASCaM), Department of Chemistry, University of North Texas, Denton, Texas 76203-5070, United States.
Michael L
ML
Drummond
Center for Advanced Scientific Computing and Modeling (CASCaM), Department of Chemistry, University of North Texas, Denton, Texas 76203-5070, United States.
Angela K
AK
Wilson
Center for Advanced Scientific Computing and Modeling (CASCaM), Department of Chemistry, University of North Texas, Denton, Texas 76203-5070, United States.
Thomas R
TR
Cundari
carbon capture and sequestration; ligand migration; molecular dynamics; phosphoenolpyruvate carboxykinase; protein−ligand interactions