The kinetics of ligand migration in crystallized myoglobin as revealed by molecular dynamics simulations.
By using multiple molecular dynamics trajectories of photolyzed carbon monoxide (CO) within crystallized myoglobin, a quantitative description of CO diffusion and corresponding kinetics was obtained. Molecular dynamics results allowed us to construct a detailed kinetic model of the migration process, shedding light on the kinetic mechanism and relevant steps of CO migration and remarkably-well reproducing the available experimental data as provided by time-resolved Laue x-ray diffraction.
Anselmi
Massimiliano
M
Department of Chemistry, University of Rome "La Sapienza", Rome, Italy.
Di Nola
Alfredo
A
Amadei
Andrea
A
D001665:Binding Sites; D002245:Carbon Dioxide / Q000737:chemistry*; D003198:Computer Simulation; D003460:Crystallization; D006454:Hemoglobins / Q000737:chemistry*; D007700:Kinetics; D008024:Ligands; D008956:Models, Chemical; D008958:Models, Molecular; D009038:Motion; D009211:Myoglobin / Q000737:chemistry*; D011485:Protein Binding; D011487:Protein Conformation
D006454:Hemoglobins; D008024:Ligands; D009211:Myoglobin; C018013:carboxymyoglobin; D002245:Carbon Dioxide