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.
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.