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Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase
Published on: December 4, 2017
Redox-promoting protein motions in rubredoxin
Jose M Borreguero1, Junhong He, F Meilleur
1Neutron Scattering Science Division, Oak Ridge National Laboratory, Oak Ridge, Tennessee 37831, United States. borreguerojm@ornl.gov
The Journal of Physical Chemistry. B
|May 26, 2011
Summary
Protein dynamics influence function. This study reveals how temperature-activated atomic motions in rubredoxin affect electrostatic forces on its iron ion, potentially impacting its biological activity.
Area of Science:
- Biophysics
- Protein dynamics
- Computational biology
Background:
- Protein function is linked to internal motions, but this relationship is debated.
- Rubredoxin (RdPf) from Pyrococcus furiosus is a small protein with a coordinated Fe(3+) ion.
Purpose of the Study:
- To characterize temperature-activated atomic motions in oxidized rubredoxin.
- To investigate the relationship between protein dynamics and electrostatic interactions with the Fe(3+) ion.
Main Methods:
- Computational modeling of protein dynamics at various temperatures.
- Neutron scattering experiments for validation of computational results.
Main Results:
- Above the dynamical transition temperature, anharmonic motions reorient and strengthen electrostatic forces on the Fe(3+) ion.
- At higher temperatures, activated anharmonic modes dominate electrostatic fluctuations.
- At 360 K, motions of conserved residues Ile7 and Ile40 contribute significantly to electrostatic fluctuations, potentially aiding solvent access.
Conclusions:
- Temperature-activated protein motions critically influence electrostatic interactions at the active site.
- Specific residue dynamics in rubredoxin may play a role in substrate or solvent accessibility.
- Computational and experimental approaches provide insights into protein dynamics and function.
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