Quantum Sensing of Electron Transfer Pathways in Natural Photosynthesis Using Time-Resolved High-Field Electron Paramagnetic Resonance/Electron–Nuclear Double Resonance Spectroscopy

Photosynthetic integral membrane reaction center (RC) proteins capture and convert sunlight into chemical energy via efficient charge separation achieved through a series of rapid, photoinitiated electron transfer steps. These fast electron transfers create an entangled spin qubit (radical) pair that contains detailed information about the weak magnetic interactions, structure, and dynamics of localized protein environments involved in charge separation events. Herein, we investigate how these entangled electron spin qubits interact with nuclear spins of the protein environment using the high spectral resolution of 130 GHz electron paramagnetic resonance (EPR) and electron–nuclear double resonance (ENDOR). Spectroscopic interrogation enabled the observation and probing of protons located in the electron transfer pathway between the membrane-spanning electron pair P+QA– (where P+ is the primary donor, a special pair of bacteriochlorophylls, and QA is the primary quinone acceptor) in the bacterial RC. Spectroscopic analysis reveals hydrogen-bonding interactions involved in regulating the route that light-induced electrons travel through the RC protein during charge separation.

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