Quantum Optoelectronics

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Photonic molecules defined by SU-8 photoresist strips on a photonic crystal waveguide

Optics Express Optical Society of America (2018)

Authors:

ROBERT TAYLOR, S Lennon, F Brossard, L Nuttall, J Wu, J Griffiths

Nitride Single Photon Sources

2018 IEEE PHOTONICS CONFERENCE (IPC) (2018)

Authors:

T Zhu, JC Jarman, Christopher X Ren, Fengzai Tang, CC Kocher, TJ Puchtler, Benjamin PL Reid, T Wang, Saroj K Patra, Stefan Schulz, Robert A Taylor, RA Oliver

Vectorial fluorescence emission from microsphere coupled to gold mirror

Advanced Optical Materials 6 (22), 1801025

Authors:

Adarsh B Vasista, Sunny Tiwari, Deepak K Sharma, Shailendra K Chaubey, GV Pavan Kumar

Abstract:

Entanglement between living bacteria and quantized light witnessed by Rabi splitting

Journal of Physics Communications IOP Publishing 2:10 (2018) 101001

Authors:

C Marletto, DM Coles, T Farrow, V Vedral

Proton tunnelling in hydrogen bonds and its implications in an induced-fit model of enzyme catalysis

Proceedings of the Royal Society A: Mathematical, Physical and Engineering Sciences Royal Society 474:2218 (2018) 20180037

Authors:

O Pusuluk, Tristan Farrow, C Deliduman, K Burnett, Vlatko Vedral

Abstract:

The role of proton tunnelling 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 catalyses 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.