Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

NO rebinding to myoglobin: a reactive molecular dynamics study.

Markus Meuwly1, Oren M Becker, Roland Stote

  • 1Laboratoire de Chimie Biophysique, ISIS UMR 7006, Universite Louis Pasteur, 67000, Strasbourg, France.

Biophysical Chemistry
|July 20, 2002
PubMed
Summary

This study used reactive molecular dynamics to investigate nitric oxide (NO) rebinding to myoglobin. Protein relaxation influences the rebinding barrier, potentially explaining experimentally observed non-exponential NO rebinding rates.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Anisotropic unbinding and location-dependent hovering of a kinesin motor head over microtubule.

Biophysical journal·2026
Same author

Toward Quantitative Reaction Dynamics of O<sub>3</sub>.

The journal of physical chemistry letters·2026
Same author

Reaction Pathway Dynamics for Atmospheric Decomposition Reactions: Unimolecular Dissociation of H<sub>2</sub>COO.

The journal of physical chemistry letters·2026
Same author

Compact Kernel/Neural Network Representation for Accurate, Fast, and Global Reactive Molecular Potential Energy Surfaces.

Precision chemistry·2026
Same author

High-Accuracy Molecular Simulations with Machine-Learning Potentials and Semiclassical Approximations to Quantum Dynamics.

Chimia·2026
Same author

Tripeptide dynamics from empirical and machine-learned energy functions.

Biophysical journal·2026

Area of Science:

  • Biophysics
  • Computational Chemistry
  • Molecular Dynamics

Background:

  • Myoglobin's interaction with nitric oxide (NO) is crucial for its biological function.
  • Understanding the dynamics of NO rebinding after photodissociation is key to elucidating myoglobin's reaction mechanisms.
  • Experimental observations suggest non-exponential rebinding rates, requiring theoretical explanation.

Purpose of the Study:

  • To investigate the rebinding of nitric oxide (NO) to myoglobin post-photolysis.
  • To explore the role of protein relaxation in modulating the NO rebinding kinetics.
  • To provide a theoretical basis for experimentally observed non-exponential rebinding rates.

Main Methods:

  • Employed the 'reactive molecular dynamics' method.

Related Experiment Videos

  • Evaluated system energy on two potential energy surfaces capturing heme-ligand interactions.
  • Analyzed the dynamics of dissociated NO molecules and the properties of the transition seam.

    • Main Results:

    • The effective rebinding barrier height is time-dependent after photodissociation.
    • Protein relaxation was identified as the primary cause of this time-dependency.
    • The findings support the hypothesis that protein relaxation contributes to non-exponential NO rebinding.

    Conclusions:

    • Reactive molecular dynamics provides insights into NO-myoglobin rebinding.
    • Protein relaxation significantly impacts the NO rebinding barrier dynamics.
    • The study offers a mechanistic explanation for experimentally observed non-exponential rebinding kinetics.