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Fast product release requires active-site water dynamics in carbonic anhydrase
Jin Kyun Kim1,2, Seon Woo Lim1, Hannah Jeong1
1Department of Physics, Ulsan National Institute of Science and Technology (UNIST), Ulsan, 44919, Republic of Korea.
Nature Communications
|May 12, 2025
Summary
Researchers visualized enzyme catalysis using UV photolysis and X-ray crystallography. They revealed how active-site water dynamics in carbonic anhydrase II (CAII) drive its high catalytic efficiency.
Area of Science:
- Biochemistry
- Structural Biology
- Enzymology
Background:
- Water is crucial for enzyme function, impacting structure, stability, and catalysis.
- Observing active-site water dynamics during enzyme catalysis is experimentally challenging.
Purpose of the Study:
- To visualize the catalytic pathway of carbonic anhydrase II (CAII) at high resolution.
- To understand the role of active-site water dynamics in CAII's catalytic efficiency.
Main Methods:
- Integration of ultraviolet (UV) photolysis with temperature-controlled X-ray crystallography.
- Achieved 1.2 Å resolution to create molecular movies of CAII catalysis.
Main Results:
- Captured substrate binding, conversion, and product release in CAII.
- Identified an unexpected product binding configuration linked to sub-nanosecond water rearrangement.
- Detailed the structure and dynamics of active-site water during catalysis.
Conclusions:
- Proposed a comprehensive catalytic mechanism for CAII.
- Demonstrated that CAII utilizes active-site water structure and dynamics for diffusion-limited efficiency.
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