{"schema":"pubphys.bundle/1","record":{"author":{"account_ref":null,"orcid":null},"builds_on":[],"content_schema":"pubphys.content.revision/1","content_sha256":"e227d71c357d3e9a9df02f9f5771bc28f42e1a50c628763d30322b7f2d418975","created":"2026-10-03T07:17:58Z","files":[],"origin":{"assisted_by":[],"kind":"seed"},"parents":["5475cf5dc5b1a72283d26dc95dc6e00d7ea4e00096a7c6492e409a1816eeb011"],"salt":"3a38e235d79e8e871773eab822ebe001e5e406f2402e73de3ab4f4c199fb904a","schema":"pubphys.record/2","site":"pubphys.com","target":null,"type":"revision"},"content":{"answer_type":"yes-no","assisted_by":[],"external_id":"bio.quantum-biology.enzyme-tunneling-dynamics","kind":"well-posed","literature_status":"contested","n":"1","parents":[],"plain":"Many enzymes move a hydrogen atom by quantum tunneling, passing through rather than over an energy barrier, as seen from how much the reaction slows when hydrogen is replaced by heavier deuterium. Whether specific fast protein motions speed the reaction, or the protein only sets the shape of the barrier, is disputed.","posed_since":"","precise":"For hydrogen-transfer enzymes such as soybean lipoxygenase-1 (kinetic isotope effect $k_H/k_D\\sim 80$ near 300 K, nearly temperature-independent) and dihydrofolate reductase, determine whether non-equilibrium protein motions on fs to ps timescales coupled to the donor-acceptor distance contribute to the rate beyond what equilibrium transition-state or Marcus-like tunneling theory with thermally sampled distances gives. An answer is a quantitative partition of the rate into equilibrium and dynamical contributions, with the dynamical part shown to be zero or nonzero beyond error.","problem_ref":null,"references":"","settled_by":"Heavy-enzyme (isotopically labeled protein) and vibrational-excitation experiments that alter protein dynamics without altering the free-energy surface, matched by path-integral simulations with and without the dynamical coupling.","status_note":"","title":"Do fast protein vibrations drive hydrogen tunneling in 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