Rerouting excitation transfers in the Fenna-Matthews-Olson complex.

We investigate, using the hierarchy method, the entanglement and the excitation transfer efficiency of the Fenna-Matthews-Olson (FMO) complex under two different local modifications: the suppression of transitions between particular sites and localized changes to the protein environment. We find that inhibiting the connection between site 5 and site 6, or completely disconnecting site 5 from the complex, leads to a dramatic enhancement of the entanglement between site 6 and site 7. Similarly, the transfer efficiency actually increases if site 5 is entirely disconnected from the complex. We further show that if sites 5 and 7 are conjointly removed, the efficiency falls. This suggests that while not contributing to the transport efficiency in a normal complex, site 5 may introduce a redundant transport route in case of damage to site 7. Our results suggest an overall robustness of the excitation-energy transfer in the FMO complex under mutations, local defects, and other abnormal situations.

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