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the claim

Enzyme-substrate quantum tunneling reactions require macroscopic physical considerations for spatial positioning

the verdict
SUPPORTED
the evidence backs this
Recorded sources
4 sources for · 0 against

Counts group repeated records of the same source within each side. They do not measure evidence strength or source independence.

Is it true that enzyme-substrate quantum tunneling reactions require macroscopic physical considerations for spatial positioning?

Yes. Enzyme-substrate quantum tunneling reactions are strongly dependent on macroscopic physical considerations, such as protein conformational dynamics and spatial positioning, which modulate barrier widths and distances to facilitate tunneling.

Verdict: SUPPORTED · 4 sources for, 0 against · Last checked

The analysis

The retrieved papers consistently support the premise that quantum tunneling in enzymatic reactions is inextricably linked to protein conformational dynamics, structural ensembles, and the precise spatial positioning of donor and acceptor atoms. Papers [0], [1], [3], and [5] emphasize that macroscopic protein motions, active-site electrostatics, and distance gating are essential for establishing the conformational states necessary for hydrogen tunneling. No papers refute the claim.

Evidence for · 4
Hydrogen Tunneling Links Protein Dynamics to Enzyme Catalysis
2013
Demonstrates that thermodynamically equilibrated protein motions control H-donor and -acceptor distances to create conformational ensembles suitable for quantum tunneling.
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Klinman, J. P. & Kohen, A. (2013). Hydrogen Tunneling Links Protein Dynamics to Enzyme Catalysis. doi.org. https://doi.org/10.1146/annurev-biochem-051710-133623

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More for · 3
Enzyme activation by urea reveals the interplay between conformational dynamics and substrate binding: a single-molecule FRET study
2024
Shows that enzyme conformational dynamics and urea-induced structural changes directly regulate substrate positioning and catalytic efficacy.
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Scheerer, D., Levy, D., Casier, R., Riven, I., Mazal, H., & Haran, G. (2024). Enzyme activation by urea reveals the interplay between conformational dynamics and substrate binding: a single-molecule FRET study. doi.org. https://doi.org/10.1101/2024.09.01.610662

New Insight into Quantum Mechanical Hydrogen Tunneling in Enzymes.
2026
Highlights how protein dynamics, vibrational gating, and electrostatics modulate barrier width to sustain tunneling-derived rate enhancements.
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Robinson, C., Yuen, M., Brough, H., Johannissen, L. O., & Hay, S. (2026). New Insight into Quantum Mechanical Hydrogen Tunneling in Enzymes.. doi.org. https://doi.org/10.1021/acs.biochem.5c00769

Quantum mechanics/molecular mechanics studies of triosephosphate isomerase-catalyzed reactions: effect of geometry and tunneling on proton-transfer rate constants.
2002
Indicates that local atomic motions, such as donor-acceptor vibrations within active sites, directly determine the magnitude of quantum tunneling.
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Cui, Q. & Karplus, M. (2002). Quantum mechanics/molecular mechanics studies of triosephosphate isomerase-catalyzed reactions: effect of geometry and tunneling on proton-transfer rate constants.. doi.org. https://doi.org/10.1021/ja0118439

Receipt History
first checked05 Aug 2026
judged → SUPPORTED · 9105 Aug 2026
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