title: CO migration in native and mutant myoglobin: atomistic simulations for the understanding of protein function.
abstract: Molecular dynamics simulations of the events after the photodissociation of CO in the myoglobin mutant L29F in which leucine is replaced by phenylalanine are reported. Using both classical and mixed quantum-classical molecular dynamics calculations, we observed the rapid motion of CO away from the distal heme pocket to other regions of the protein, in agreement with recent experimental results. The experimentally observed and calculated infrared spectra of CO after dissociation are also in good agreement. We compared the results with data from simulations of WT myoglobin. As the time resolution of experimental techniques is increased, theoretical methods and models can be validated at the atomic scale by direct comparison with experiment.
authors.affiliation: Department of Chemistry, University of Basel, Klingelbergstrasse 80, 4056 Basel, Switzerland.
authors.forename: David R
authors.initials: DR
authors.lastname: Nutt
authors.forename: Markus
authors.initials: M
authors.lastname: Meuwly
mesh_terms: D002248:Carbon Monoxide / Q000737:chemistry*; D008958:Models, Molecular; D009154:Mutation; D009211:Myoglobin / Q000737:chemistry* / Q000235:genetics; D011487:Protein Conformation; D013055:Spectrophotometry, Infrared
chemical_list: D009211:Myoglobin; D002248:Carbon Monoxide