2016/04/29 by Davinder Singh, Shubhrangshu Dasgupta, Singh, Davinder +1
Biochemistry, Genetics and Molecular Biology · Chemistry · Physics and Astronomy · #Biological Physics (physics.bio-ph) #Chemical Physics (physics.chem-ph) #FOS: Physical sciences #Molecular spectroscopy and chirality #Photosynthetic Processes and Mechanisms #Quantum Physics (quant-ph) #Spectroscopy and Quantum Chemical Studies
paper · pdf · doi:10.48550/arxiv.1605.00920
openalex publication_date 2016/04/29 · openalex created_date 2025/10/10 · openalex updated_date 2026/07/28
To explain experimentally observed oscillatory dynamics of highly efficient process of excitation energy transfer (EET) in Fenna-Matthews-Olson (FMO) complex, most theoretical models assume the same local protein environment around all the bacteriochlorophyll-a (BChla) sites, contradictory to the structural analysis of FMO complex. Using different values of pigment-protein couplings for different BChla sites, measured in the adiabatic limit of electron transfer, we theoretically investigate the effect of inhomogeneous local protein environment on excitation energy transfer. By employing non-Markovian master equation we demonstrate that the asymmetric system-bath coupling leads to the results consistent with the experimental observations. Quantum dynamical simulation suggests that the correlated fuctuations preserve the oscillation of excitation for long time-scales. Further different BChla sites have asymmetric time-scales of oscillations of excitation due to in-homogeneous pigment-protein couplings also.