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Sandström, A.; Gillbro, T.; Sundström, V.; Fischer, R. and Scheer, Hugo (March 1988): Picosecond time-resolved energy transfer within C-phycocyanin aggregates of Mastigocladus laminosus. In: Biochimica et Biophysica Acta (BBA) - Bioenergetics, Vol. 933, No. 1: pp. 42-53 [PDF, 815kB]


We have investigated by picosecond absorption experiments how the size of C-phycocyanin aggregates from Mastigocladus laminosus influences the excitation energy transfer kinetics. Going from C-phycocyanin monomers to trimers the lifetime of the faster energy transfer component decreased from 57 ± 4 to 27 ± 4 ps over most of the wavelength range (580–645 nm) studied. This change was interpreted as the opening of fast transfer channels (α-84 → β-84 and/or β-84 → β-84) between two adjacent monomers in the trimeric unit. The 57 ps lifetime is probably due mainly to the β-155 → β-84 energy transfer step. The intermediate lifetime decreased from about 300 ps in the monomer to 100–120 ps in the trimer. The former is believed to be dominated by the equilibration process α-84 a3 β-84, while the latter probably represents the time required for the excitation energy to reach thermodynamic equilibrium within the trimer. The lifetime of the longest components was about 1 ns in both systems. This indicates that the chromophores in these C-phycocyanin complexes are more exposed to non-radiative processes (like, for instance, isomerization) compared to the chromophores in intact phycobilisomes, where this lifetime typically is about 1.8 ns. The anisotropy relaxation closely followed the isotropic lifetimes in both systems. The anisotropy after the initial fast relaxation, r(∞), was 0.29 ± 0.04 in monomers and decreased to 0.15 ± 0.03 in trimers. Measurements of the steady-state fluorescence excitation anisotropy gave the same results within the experimental error.

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