NO rebinding to myoglobin: a reactive molecular dynamics study.
The rebinding of NO to myoglobin after photolysis is studied using the 'reactive molecular dynamics' method. In this approach the energy of the system is evaluated on two potential energy surfaces that include the heme-ligand interactions which change between liganded and unliganded myoglobin. This makes it possible to take into account in a simple way, the high dimensionality of the transition seam connecting the reactant and product states. The dynamics of the dissociated NO molecules are examined, and the geometrical and energetic properties of the transition seam are studied. Analysis of the frequency of recrossing shows that the height of the effective rebinding barrier is dependent on the time after photodissociation. This effect is due mainly to protein relaxation and may contribute to the experimentally observed non-exponential rebinding rate of NO, as has been suggested previously.
Laboratoire de Chimie Biophysique, ISIS UMR 7006, Universite Louis Pasteur, 67000, Strasbourg, France.
Markus
M
Meuwly
Oren M
OM
Becker
Roland
R
Stote
Martin
M
Karplus
D003198:Computer Simulation; D006418:Heme / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D007501:Iron / Q000737:chemistry / Q000378:metabolism; D007700:Kinetics; D008024:Ligands; D008956:Models, Chemical; D008958:Models, Molecular; D009211:Myoglobin / Q000737:chemistry / Q000378:metabolism*; D009569:Nitric Oxide / Q000737:chemistry / Q000378:metabolism*; D010782:Photolysis; D011485:Protein Binding; D011487:Protein Conformation; D013816:Thermodynamics; D013997:Time Factors
D008024:Ligands; D009211:Myoglobin; D009569:Nitric Oxide; D006418:Heme; D007501:Iron