The influence of aggregation and temperature on the excited state kinetics of C-phycocyanin from Mastiqocladus laminosus has been studied. Polarized fluorescence decay curves have been recorded using a synchronously pumped dye laser in conjunction with a synchroscan streak camera. The experimental data for all samples can be fit satisfactorily assuming a biexponential decay law. Fluorescence depolarization times have been interpreted in terms of energy transfer among the different chromophores. The influence of temperature is only moderate on the intra­molecular relaxation, but pronounced on the rates of energy transfer. Both are dependent on the size of the aggregate. The biexponential decay of the α-subunit containing only one chromophore, indicates the presence of different subsets of chromophores in these samples. The results are discussed in terms of variations of the chromophore arrangements upon temperature induced changes in the protein conformation.

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SummaryThe (Y-and &subunits of C-phycocyanin from Mastigocladus laminosus were prepared according to revised procedures. Both subunits are isolated as dimers, which can be dissociated into monomers with detergent mixtures. The fluorescence decay kinetics are similar for the respective monomers and dimers. In no case could they be fitted by only one (o-subunit) or two exponentials (P-subunit) which are predicted by theory for samples with a unique chromophore-protein arrangement containing one and two chromophores, respectively. It is suggested that there exists a heterogeneity among the chromophores of the subunits, which may persist in the highly aggregated complexes present in cyanobacterial antennas.

The transient absorption recovery induced in phycocyanin trimers by picosecond pulses of variable wavelength (570-620 nm) has been recorded and analyzed by applying a least-squares multi-exponential fit procedure. The results suggest that in native PC trimers the chromophores exhibit a microheterogeneity with the effect that the derived apparent lifetimes are functions of excitation and probing wavelength. It is suggested that, due to strong excitonic coupling between a-84 and β-84 chromophores, the lifetime of the terminal acceptor state is reduced to about 900 ps; the apparent energy transfer time from chromophore β-155 to a-84 and β-84 chromophores varies between 20-50 ps depending on the actual chromophore-protein arrangement (microheterogeneity)