Diatoms generate a large portion
of the oxygen produced on earth
due to their exceptional light-harvesting properties involving fucoxanthin
and chlorophyll-binding proteins (FCP). At the same time, an efficient
adaptation of these complexes to fluctuating light conditions is necessary
to protect the diatoms against photodamage. So far, structural and
dynamic data for the interaction between FCP and the photoprotective
LHCX family of proteins in diatoms are lacking. In this computational
study, we provide a structural basis for a remarkable pH-dependent
adaptation at the molecular level. Upon binding of the LHCX1 protein
to the FCP complex together with a change in pH, conformational changes
within the FCP protein result in a variation of the electronic coupling
in a specific chlorophyll-fucoxanthin pair, leading to a change in
the exciton transfer rate by almost an order of magnitude. A common
strategy for photoprotection between diatoms and higher plants is
identified and discussed.
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