CO migration in native and mutant myoglobin: Atomistic simulations for the understanding of protein function
AUTOR(ES)
Nutt, David R.
FONTE
National Academy of Sciences
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=395912Documentos Relacionados
- Ligand migration pathway and protein dynamics in myoglobin: A time-resolved crystallographic study on L29W MbCO
- Myoglobin: A scavenger of bioactive NO
- Myoglobin: The hydrogen atom of biology and a paradigm of complexity
- Vibrational population relaxation of carbon monoxide in the heme pocket of photolyzed carbonmonoxy myoglobin: Comparison of time-resolved mid-IR absorbance experiments and molecular dynamics simulations
- Atomistic understanding of kinetic pathways for single base-pair binding and unbinding in DNA