Energy-transfer and exciton-state relaxation processes in allophycocyanin

Abstract

The authors have employed picosecond spectroscopic techniques to characterize the photophysics of the phycocyanobilin chromophores in linker-free allophycocyanin isolated from the cyanobactrium Synechococcus PCC 6301 (AN112 mutant). In analogy with the known structure of the related phycobiliprotein C-phycocyanin, allophycocyanin is probably organized as a ringlike homotrimer; the monomeric units are composed of an {alpha} and a {beta} subunit, each of which binds a phycocyanobilin chromophore via a thioether linkage to a cysteine residue at amino acid position 84. The authors observe bidirectional excitation transfer in the {alpha}{beta} monomer between the {alpha}84 and {beta}84 chromophores with a 140-ps time constant. The authors assign an ultrafast (<2-ps time constant) anisotropy and photobleaching transient observed only in ({alpha}{beta}){sub 3} trimers to an interexciton level transition; the transient occurs with a polarization change that is consistent with a transition between the orthogonal upper and lower exciton states. The upper exciton state also relaxes directly to the ground state through a decay process with a 45-ps time constant. They attribute the heterogeneous relaxation of the upper exciton state through these two paths to an inhomogeneous broadening due to site heterogeneity, which was previously observed in C-phycocyanin in hole-burning experiments at low temperature. Excitation transfer amongmore » the degenerate lower exciton states is detected in terms of a 70-ps anisotropy decay observed in the photobleaching and stimulated emission. The interexcition level transition rapidly concentrates excitation in the lower exciton state of allophycocyanin ({alpha}{beta}){sub 3} trimers; this kind of spectral relaxation process may be important in facilitating directional excitation transfer in reaction center/light-harvesting protein assemblies. 47 refs., 8 figs.« less