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The Fenna Mathews Olson (FMO) complex of green sulphur bacteria is an exampleof a photosynthetic pigment protein complex, in which the electronic propertiesof the pigments are modified by the protein environment to promote efficientexcitonic energy transfer from antenna complexes to the reaction centres. Manyof the electronic properties of the FMO complex can be extracted from knowledgeof the static crystal structure. However, the recent observation and analysisof long lasting quantum dynamics in the FMO complex point to protein dynamicsas a key factor in protecting and generating quantum coherence under laboratoryconditions. While fast inter and intra molecular vibrations have beeninvestigated extensively, the slow dynamics which effectively determine theoptical inhomogeneous broadening of experimental ensembles has received lessattention. Our study employs constrained geometric dynamics to study theflexibility in the protein network by efficiently generating the accessibleconformational states from the published crystal structure. Statistical andprinciple component analysis reveal highly correlated low frequency motionsbetween functionally relevant elements, including strong correlations betweenpigments that are excitonically coupled. Our analysis reveals a hierarchy ofstructural interactions which enforce these correlated motions, from the levelof monomer monomer interfaces right down to the alpha helices, beta sheets andpigments. In addition to inducing strong spatial correlations across theconformational ensemble, we find that the overall rigidity of the FMO complexis exceptionally high. We suggest that these observations support the idea ofhighly correlated inhomogeneous disorder of the electronic excited states,which is further supported by the remarkably low variance of the excitoniccouplings of the conformational ensemble.

photosynthesis research

Constrained geometric dynamics of the Fenna-Matthews-Olson complex: The  role of correlated motion in reducing uncertainty in excitation energy  transfer