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Nuclear quantum tunnelling in enzymatic reactions – an enzymologist's perspective

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Johannissen, Linus O., Hay, Sam, Scrutton, Nigel S.·2015·Physical Chemistry Chemical Physics
DOI 10.1039/c5cp00614g
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Abstract

The roles of nuclear quantum tunnelling and dynamics in enzyme reactions are discussed in this perspective on 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 [37]

    Section 2 models the classical over-barrier rate as temperature-dependent and the observed rate as a sum of classical and tunnelling contributions, supporting the distinction between the two pathways. But it does not identify a temperature-independent rate at low temperature as a definitive experimental hallmark, or establish that only the quantum contribution remains there. Section 2 instead says there is no direct experimental measure for the degree of tunnelling and discusses the kinetic isotope effect as an approximation. (LLM, conf=0.84)

    Experimental — accuracy not yet measured

  • A 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 [37]

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Authors
Johannissen, L. O., Hay, S., & Scrutton, N. S.
Affiliations
University of Manchester (GB)
Corresponding author
  • Hay, Sam
  • Scrutton, Nigel S.
ORCID
Venue
Physical Chemistry Chemical Physics
Publisher
Royal Society of Chemistry (RSC)
Published
2015
Volume
17
Issue
46
Pages
30775-30782
ISSN
  • 1463-9076 (ISSN-L)
  • 1463-9084
DOI
10.1039/c5cp00614g
OpenAlex
W2060777103
Cited by
22
References
100
Citations by year
2025: 4 · 2023: 5 · 2022: 1 · 2021: 1 · 2020: 2 · 2019: 1 · 2017: 2 · 2016: 6
FWCI
1.82
Type
journal article
Language
en
Open access
Licence
cc-by
Locations
  • Physical Chemistry Chemical Physics (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • Research Explorer (The University of Manchester) (submittedVersion, cc-by)
Funders
Engineering and Physical Sciences Research Council (EP/J020192/1)
Topics
  • Physical Sciences › Chemistry › Physical and Theoretical Chemistry › Chemical Reactions and Mechanisms
  • Physical Sciences › Chemistry › Organic Chemistry › Chemical Reaction Mechanisms
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Keywords
enzyme catalysis, protein dynamics, substrate-borne vibrations, quantum-classical coupling, reaction coordinate
MeSH terms
Enzymes, Hydrogen, Kinetics, Quantum Theory, Substrate Specificity, Biocatalysis

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