Proton tunnelling in hydrogen bonds and its implications in an induced-fit model of enzyme catalysis
| Autor: | Onur Pusuluk, Vlatko Vedral, Tristan Farrow, Cemsinan Deliduman, Keith Burnett |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
General Mathematics Quantum superposition FOS: Physical sciences General Physics and Astronomy 010402 general chemistry 01 natural sciences Enzyme catalysis 03 medical and health sciences Open quantum system Physics - Chemical Physics Quantum information Quantum Research Articles Quantum tunnelling Chemical Physics (physics.chem-ph) Quantum Physics Quantitative Biology::Biomolecules Chemistry Quantitative Biology::Molecular Networks General Engineering Substrate (chemistry) Biomolecules (q-bio.BM) Tautomer 0104 chemical sciences 030104 developmental biology Quantitative Biology - Biomolecules Chemical physics FOS: Biological sciences Quantum Physics (quant-ph) |
| Zdroj: | Proceedings of the Royal Society A: Mathematical, Physical and Engineering Sciences. 474(2218) |
| ISSN: | 1471-2946 1364-5021 |
| Popis: | 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. 15 pages, 4 figures. Authors postprint version |
| Databáze: | OpenAIRE |
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