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Quantum entanglement shared in hydrogen bonds and its usage as a resource in molecular recognition

Department of Physics, İstanbul Technical University, Maslak, İstanbul 34469, Turkey

Corresponding author.

Department of Physics, İstanbul Technical University, Maslak, İstanbul 34469, Turkey

Centre for the Mathematics and Theoretical Physics of Quantum, Non-Equilibrium Systems, School of Mathematical Sciences, The University of Nottingham, University Park Campus, Nottingham NG7 2RD, UK

E-mail Address: [email protected]

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, and

Cemsinan Deliduman

Department of Physics, Mimar Sinan Fine Arts University, Şişli, İstanbul 34380, Turkey

E-mail Address: [email protected]

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https://doi.org/10.1142/S0217984918503086Cited by:9 (Source: Crossref)

Abstract

Quantum tunneling events occurring through biochemical bonds are capable of generating quantum correlations between bonded systems, which in turn makes the conventional second law of thermodynamics approach insufficient to investigate these systems. This means that the utilization of these correlations in their biological functions could give an evolutionary advantage to biomolecules to an extent beyond the predictions of molecular biology that are generally based on the second law in its standard form. To explore this possibility, we first compare the tunneling assisted quantum entanglement shared in the ground states of covalent and hydrogen bonds. Only the latter appears to be useful from a quantum information point of view. Also, significant amounts of quantum entanglement can be found in the thermal state of hydrogen bond. Then, we focus on an illustrative example of ligand binding in which a receptor protein or an enzyme is restricted to recognize its ligands using the same set of proton-acceptors and donors residing on its binding site. In particular, we show that such a biomolecule can discriminate between $3^{n} - 1$ agonist ligands if it uses the entanglement shared in $n$ intermolecular hydrogen bonds as a resource in molecular recognition. Finally, we consider the molecular recognition events encountered in both the contemporary genetic machinery and its hypothetical primordial ancestor in pre-DNA world, and discuss whether there may have been a place for the utilization of quantum entanglement in the evolutionary history of this system.

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References

1. S. Lloyd, Phys. Rev. A 39 (1989) 5378. Web of Science, ADS, Google Scholar
2. T. Sagawa and M. Ueda, Phys. Rev. Lett. 109 (2012) 180602. Web of Science, ADS, Google Scholar
3. J. V. Koski, V. F. Maisi, T. Sagawa and J. P. Pekola, Phys. Rev. Lett. 113 (2014) 030601. Web of Science, ADS, Google Scholar
4. M. Horodecki and J. Oppenheim, Nat. Commun. 4 (2013) 2059. Web of Science, ADS, Google Scholar
5. F. G. S. L. Brandão, M. Horodecki, N. H. Y. Ng, J. Oppenheim and S. Wehner, Proc. Natl. Acad. Sci. USA 112 (2015) 3275. Web of Science, ADS, Google Scholar
6. R. van der Meer, N. H. Y. Ng and S. Wehner, Phys. Rev. A 96 (2017) 062135. Web of Science, ADS, Google Scholar
7. M. N. Bera, A. Riera, M. Lewenstein and A. Winter, Nat. Commun. 8 (2017) 2180. Web of Science, ADS, Google Scholar
8. M. H. Partovi, Phys. Rev. E 77 (2008) 021110. Web of Science, ADS, Google Scholar
9. D. Jennings and T. Rudolph, Phys. Rev. E 81 (2010) 061130. Web of Science, ADS, Google Scholar
10. K. Micadei, J. P. S. Peterson, A. M. Souza, R. S. Sarthour, I. S. Oliveira, G. T. Landi, T. B. Batalhão, R. M. Serra and E. Lutz, Reversing the Thermodynamic Arrow of Time using Quantum Correlations, arXiv:1711.03323v1 [quant-ph]. Google Scholar
11. L. Pauling, The Nature of the Chemical Bond (Cornell University Press, Ithaca, NY, 1960). Google Scholar
12. S. J. Grabowski, Chem. Rev. 111 (2011) 2597. Web of Science, Google Scholar
13. X. Li, L. Liu and H. B. Schlegel, J. Am. Chem. Soc. 124 (2002) 9639. Web of Science, Google Scholar
14. C. F. Guerra, F. M. Bickelhaupt, J. G. Snijders and E. J. Baerends, Chem.-Eur. J 5 (1999) 3581. Web of Science, Google Scholar
15. C. F. Guerra, F. M. Bickelhaupt, J. G. Snijders and E. J. Baerends, J. Am. Chem. Soc. 122 (2000) 411. Google Scholar
16. T. van der Wijst, C. F. Guerra, M. Swart and F. M. Bickelhaupt, Chem. Phys. Lett. 426 (2006) 415. Web of Science, ADS, Google Scholar
17. W. W. Cleland, P. A. Frey and J. A. Gerlt, J. Biol. Chem. 273 (1998) 25529. Web of Science, Google Scholar
18. B. Schiøtt, B. B. Iversen, G. K. H. Madsen, F. K. Larsen and T. C. Bruice, Proc. Natl. Acad. Sci. USA 95 (1998) 12799. Web of Science, ADS, Google Scholar
19. C. N. Schutz and A. Warshel, Proteins 55 (2004) 711. Web of Science, Google Scholar
20. A. Warshel, P. K. Sharma, M. Kato, Y. Xiang, H. Liu and M. H. M. Olsson, Chem. Rev. 106 (2006) 3210. Web of Science, Google Scholar
21. M. Elias, A. Wellner, K. Goldin-Azulay, E. Chabriere, J. A. Vorholt, T. J. Erb and D. S. Tawfik, Nature 491 (2012) 134. Web of Science, ADS, Google Scholar
22. M. V. Hosur, R. Chitra, S. Hegde, R. R. Choudhury, A. Das and R. V. Hosur, Crystallogr. Rev. 19 (2013) 3. Web of Science, Google Scholar
23. P. O. Löwdin, Rev. Mod. Phys. 35 (1963) 724. Web of Science, ADS, Google Scholar
24. G. Villani, Chem. Phys. 316 (2005) 1. Web of Science, Google Scholar
25. G. Villani, Chem. Phys. 324 (2006) 438. Web of Science, Google Scholar
26. G. Villani, Phys. Chem. Chem. Phys. 12 (2010) 2664. Web of Science, Google Scholar
27. G. Villani, J. Phys. Chem. B 114 (2010) 9653. Web of Science, Google Scholar
28. O. O. Brovarets and D. M. Hovorun, J. Biomol. Struct. Dyn. 32 (2014) 127. Web of Science, Google Scholar
29. O. O. Brovarets and D. M. Hovorun, J. Biomol. Struct. Dyn. 32 (2014) 1474. Web of Science, Google Scholar
30. O. O. Brovarets and D. M. Hovorun, J. Biomol. Struct. Dyn. 33 (2015) 2716. Web of Science, Google Scholar
31. A. D. Godbeer, J. S. Al-Khalili and P. D. Stevenson, Phys. Chem. Chem. Phys. 17 (2015) 13034. Web of Science, Google Scholar
32. N. Turaeva and V. Brown-Kennerly, Chem. Phys. 461 (2015) 106. Web of Science, Google Scholar
33. C. H. Bennett, D. P. DiVincenzo, J. Smolin and W. K. Wootters, Phys. Rev. A 54 (1996) 3824. Web of Science, ADS, Google Scholar
34. M. Żukowski, A. Zeilinger, M. A. Horne and A. K. Ekert, Phys. Rev. Lett. 71 (1993) 4287. Web of Science, ADS, Google Scholar
35. S. Bose, V. Vedral and P. L. Knight, Phys. Rev. A 57 (1998) 822. Web of Science, ADS, Google Scholar
36. C. H. Bennett, G. Brassard, C. Crépeau, R. Jozsa, A. Peres and W. K. Wootters, Phys. Rev. Lett. 70 (1993) 1895. Web of Science, ADS, Google Scholar
37. P. Schimmel, R. Giegé, D. Moras and S. Yokoyama, Proc. Natl. Acad. Sci. USA 90 (1993) 8763. Web of Science, ADS, Google Scholar
38. L. Ribas de Pouplana and P. Schimmel, J. Biol. Chem. 276 (2001) 6881. Web of Science, Google Scholar
39. S. Shaul, D. Berel, Y. Benjamini and D. Graur, RNA 16 (2010) 141. Web of Science, Google Scholar