Conformational energetics of a partially symmetrized photosynthetic reaction centre

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The partially symmetrized mutant reaction centre from the photosynthetic bacterium Rhodobacter capsulatus, named D LL, lacks the L-branch electron acceptor bacteriopheophytin (BPh L), thus rendering it of particular interest for experiments on primary excited states in photosynthesis. Here we present the results of conformational energy calculations on the D LL mutant and several BPh L-binding revertants. The calculations provide an explanation for the relative BPh L binding properties of the proteins in terms of interactions involving two residues in the binding pocket, these being a tryptophan and a methionine in the D LL protein.