NO rebinding to myoglobin: a reactive molecular dynamics study.

Détails

ID Serval
serval:BIB_41EF0CF331E4
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
NO rebinding to myoglobin: a reactive molecular dynamics study.
Périodique
Biophysical Chemistry
Auteur(s)
Meuwly M., Becker O.M., Stote R., Karplus M.
ISSN
0301-4622
Statut éditorial
Publié
Date de publication
2002
Peer-reviewed
Oui
Volume
98
Numéro
1-2
Pages
183-207
Langue
anglais
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S. - Publication Status: ppublish
Résumé
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.
Mots-clé
Computer Simulation, Heme, Humans, Iron, Kinetics, Ligands, Models, Chemical, Models, Molecular, Myoglobin, Nitric Oxide, Photolysis, Protein Binding, Protein Conformation, Thermodynamics, Time Factors
Pubmed
Web of science
Création de la notice
11/04/2008 13:19
Dernière modification de la notice
03/03/2018 16:34
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