ArticleScientific reports2020
The physical origin of rate promoting vibrations in enzymes revealed by structural rigidity.
Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Detecting Vibrational Energy Transfer into an Enzyme Active Site via a Transition State Analog.The journal of physical chemistry letters · 2026Article
- How far can you go? Extrapolating values of catalytic activity from known protein landscapes in natural and directed evolution.Chemical Society reviews · 2026Review
- A Foundational Shift in Models for Enzyme Function.Journal of the American Chemical Society · 2025Review
- Anisotropic dynamics of an interfacial enzyme active site observed using tethered substrate analogs and ultrafast 2D IR spectroscopy.The Journal of chemical physics · 2023Article
- Phonon-assisted electron-proton transfer in [FeFe] hydrogenases: Topological role of clusters.Biophysical journal · 2023Article
- Some Clues about Enzymes from Psychrophilic Microorganisms.Microorganisms · 2022Review
- Energy Bilocalization Effect and the Emergence of Molecular Functions in Proteins.Frontiers in molecular biosciences · 2021Article
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Authors and funding
1 author.
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Abstract
Enzymes are the most efficient catalysts known to date. However, decades of research have failed to fully explain the catalytic power of enzymes, and most of the current attempts to uncloak the details of atomic motions at active sites remain incomplete. Here, a straightforward manner for understanding the interplay between the complex or irregular enzyme topology and dynamical effects at catalytic sites is introduced, by revealing how fast localized vibrations form spontaneously in the stiffest parts of the scaffold. While shedding light on a physical mechanism that allowed the selection of the picosecond (ps) timescale to increase the catalytic proficiency, this approach exposes the functional importance of localized motions as a by-product of the stability-function tradeoff in enzyme evolution. From this framework of analysis-directly accessible from available diffraction data-experimental strategies for engineering the catalytic rate in enzymatic proteins are proposed.
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Registered trials
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