Allophycocyanin and energy transfer

Biochimica Et Biophysica Acta
Robert MacColl

Abstract

Allophycocyanin is a biliprotein located in the core of the phycobilisome. The biliprotein is isolated and purified as a trimer (alpha3beta3), where a monomer is an alphabeta structure. Each alpha and beta subunit has a single noncyclic tetrapyrrole chromophore, called phycocyanobilin. The trimer of allophycocyanin has an unusual absorption maximum at 650 nm with a shoulder at 620 nm, while the monomer has an absorption maximum at 615 nm. Two explanations have been proposed for the 650-nm maximum. In one, this maximum is produced by the interaction of a particular local protein environment for three of the chromophores, causing them to red shift, while the other three chromophores are at a higher energy. Energy is transferred from the high- to the low-energy chromophores by Förster resonance energy transfer, the donor-acceptor model. In the second proposal, there is strong exciton coupling between two chromophores of the trimer that closely approach across the monomer-monomer interface. The strong interaction causes exciton splitting and a red shift in the absorption. There are three of these strongly coupled chromophore pairs, and energy is transferred between the two-exciton states of a pair by internal conversion. A variety ...Continue Reading

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