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Reactivity Tracking of an Enzyme Progress Coordinate.
Wei Li1, Meghan Kohne1, Kurt Warncke1
1Department of Physics, Emory University, Atlanta, Georgia 30322, United States.
The Journal of Physical Chemistry Letters
|August 4, 2023
Summary
Ethanolamine ammonia-lyase (EAL) enzyme catalysis involves tracking protein configurations. Optimized reactivity arises from configuration space collapse, refining enzyme catalysis models.
Area of Science:
- Biochemistry
- Enzyme kinetics
- Protein dynamics
Background:
- Ethanolamine ammonia-lyase (EAL) from Salmonella enterica catalyzes crucial reactions.
- Understanding enzyme catalysis requires resolving reaction intermediates and progress coordinates.
Purpose of the Study:
- To track and resolve the progress coordinate for substrate radical rearrangement and hydrogen atom transfer in EAL.
- To investigate the role of solvent-coupled protein configurations in enzyme reactivity.
Main Methods:
- Monitoring the first-order decay of the substrate radical intermediate.
- Analyzing heterogeneous confinement effects from sucrose hydrates on cryotrapped EAL.
- Investigating distributed kinetics arising from configurational microstates.
Main Results:
- Distributed kinetics observed in non-native decay of substrate radical pair capture substate.
- Reaction rates increased >10^3-fold across the distribution, approaching native rates.
- Native progress coordinate involves configuration space collapse for optimized reactivity.
Conclusions:
- Solvent-protein-reaction configurational coupling is fundamental to EAL function.
- A refined ensemble model of enzyme catalysis is proposed for adiabatic chemical steps.
- Protein configuration dynamics are key to achieving high catalytic efficiency.
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