The role of proton tunneling in biological catalysis remains an open question usually addressed with the tools of biochemistry. Here, we map the proton motion in a hydrogen-bonded system into a problem of pseudo-spins to allow us to approach the problem using quantum information theory and thermodynamics. We investigate the dynamics of the quantum correlations generated through two hydrogen bonds between a prototypical enzyme and a substrate , and discuss the possibility of utilizing these correlationsas a resource in the catalytic power of the enzyme . In particular, we show that classical changes induced in the binding site of the enzyme spreads the quantum correlations among all of the four hydrogen-bonded atoms  . If the enzyme suddenly returns to its initial state after the binding stage, the substrate ends in a quantum superposition state. Environmental effects can then naturally drive the reaction in the forward direction from the substrate to the product without needing the additional catalytic stage that is usually assumed to follow the binding stage . We find that in this scenario the enzyme lowers the activation energy to a much lower value than expected in biochemical reactions .
The role of proton tunneling in biological catalysis is investigated here within the frameworks of quantum information theory and thermodynamics. We consider the quantum correlations generated through two hydrogen bonds between a substrate and a prototypical enzyme that first catalyzes the tautomerization of the substrate to move on to a subsequent catalysis , and discuss how the enzyme can derive its catalytic potency from these correlations . In particular, we show that classical changes induced in the binding site of the enzyme spreads the quantum correlations among all of the four hydrogen-bonded atoms thanks to the directionality of hydrogen bonds . If the enzyme rapidly returns to its initial state after the binding stage, the substrate ends in a new transition state corresponding to a quantum superposition. Open quantum system dynamics can then naturally drive the reaction in the forward direction from the major tautomeric form to the minor tautomeric form without needing any additional catalytic activity . We find that in this scenario the enzyme lowers the activation energy so much that there is no energy barrier left in the tautomerization, even if the quantum correlations quickly decay .
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remains an open question usually addressed with the tools of biochemistry. Here, we map the proton motion in a hydrogen-bonded system into a problem of pseudo-spins to allow us to approach the problem using
is investigated here within the frameworks of
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investigate the dynamics of the
consider the
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prototypical enzyme and a substrate
substrate and a prototypical enzyme that first catalyzes the tautomerization of the substrate to move on to a subsequent catalysis
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the possibility of utilizing these correlationsas a resource in the catalytic power of the enzyme
how the enzyme can derive its catalytic potency from these correlations
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thanks to the directionality of hydrogen bonds
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suddenly
rapidly
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quantum superposition state. Environmental effects
new transition state corresponding to a quantum superposition. Open quantum system dynamics
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substrate to the product without needing the additional catalytic stage that is usually assumed to follow the binding stage
major tautomeric form to the minor tautomeric form without needing any additional catalytic activity
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to a much lower value than expected in biochemical reactions
so much that there is no energy barrier left in the tautomerization, even if the quantum correlations quickly decay