What are the signatures of tunnelling in enzyme-catalysed reactions?
Open accessAbstract
Computed tunnelling contributions and correlations between apparent activation enthalpy and entropy are explored for the interpretation of enzyme-catalysed H-transfer reactions.
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A definitive experimental hallmark of tunnelling is a temperature-independent rate at low temperature, where the rate of classical over-the-barrier hopping becomes negligible, leaving only the quantum contribution.
“Since a definitive experimental hallmark of tunnelling is a temperature-independent rate at low temperature, the rate of classical over-the-barrier hopping becomes negligible at low temperatures, leaving only the quantum contribution 37,38 .”
From An open quantum systems approach to proton tunnelling in DNA (2022) · cites this paper as [38]
The supplied passages contain only the title and bibliographic details. Searches for temperature-independent rates, cryogenic temperatures, and classical over-the-barrier contributions returned no relevant full-text passage; the substantive match was confined to the abstract, which is not admissible evidence under the stated rubric. (LLM, conf=0.66)
Experimental — accuracy not yet measuredA strong dependence of the reaction rate on the reduced mass of the system can indicate tunnelling.
“A strong dependence of the reaction rate on the reduced mass of the system can indicate tunnelling.”
From An open quantum systems approach to proton tunnelling in DNA (2022) · cites this paper as [38]
The only passage returned from our copy is the paper’s title and author metadata (no section or page). Searches for reduced mass, reaction rate, and isotope-related mass dependence found no substantive passage, so the claim cannot be verified from our copy. (LLM, conf=0.75)
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An open quantum systems approach to proton tunnelling in DNA
Slocombe, L., Sacchi, M., & Al-Khalili, J. (2022) · Communications Physics · doi:10.1038/s42005-022-00881-8 · Cited by 122 · see citing works
- Authors
- Johannissen, L. O., Iorgu, A. I., Scrutton, N. S., & Hay, S.
- Affiliations
- University of Manchester (GB)
- Corresponding author
- Hay, Sam
- Venue
- Faraday Discussions
- Publisher
- Royal Society of Chemistry (RSC)
- Published
- 2020
- Volume
- 221
- Pages
- 367-378
- ISSN
- 1359-6640 (ISSN-L)
- 1364-5498
- OpenAlex
- W2944511215
- Cited by
- 12
- References
- 0
- Citations by year
- 2026: 1 · 2025: 3 · 2023: 1 · 2022: 1 · 2021: 4 · 2020: 1 · 2019: 1
- FWCI
- 0.69
- Type
- journal article
- Language
- en
- Open access
- Licence
- Locations
- Faraday Discussions (publishedVersion)
- PubMed (publishedVersion)
- Research Explorer (The University of Manchester) (publishedVersion, other-oa)
- Funders
- Biotechnology and Biological Sciences Research Council (BB/M007065/1, BB/S003320/1)
- Topics
- Physical Sciences › Chemistry › Organic Chemistry › Chemical Reaction Mechanisms
- Physical Sciences › Chemistry › Physical and Theoretical Chemistry › Chemical Reactions and Mechanisms
- Physical Sciences › Chemistry › Physical and Theoretical Chemistry › Advanced Physical and Chemical Molecular Interactions
- Keywords
- quantum tunneling, enzyme catalysis, hydrogen tunneling, kinetic isotope effects, activation enthalpy, activation entropy, Marcus theory, enzyme variants, temperature dependence of reaction rate
- MeSH terms
- Enzymes, Hydrogen, Kinetics, Quantum Theory, Thermodynamics, Biocatalysis
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