NO rebinding to myoglobin: a reactive molecular dynamics study.

Details

Serval ID
serval:BIB_41EF0CF331E4
Type
Article: article from journal or magazin.
Collection
Publications
Title
NO rebinding to myoglobin: a reactive molecular dynamics study.
Journal
Biophysical Chemistry
Author(s)
Meuwly M., Becker O.M., Stote R., Karplus M.
ISSN
0301-4622
Publication state
Published
Issued date
2002
Peer-reviewed
Oui
Volume
98
Number
1-2
Pages
183-207
Language
english
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S. - Publication Status: ppublish
Abstract
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.
Keywords
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
Create date
11/04/2008 13:19
Last modification date
20/08/2019 14:43
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