Energy transfer and trapping in red-chlorophyll-free photosystem I from Synechococcus WH 7803.

We report for the first time steady-state and time-resolved emission properties of photosystem I (PSI) complexes isolated from the cyanobacterial strain Synechococcus WH 7803. The PSI complexes from this strain display an extremely small fluorescence emission yield at 77 K, which we attribute to the absence of so-called red antenna chlorophylls, chlorophylls with absorption maxima at wavelengths longer than those of the primary electron donor P700. Emission measurements at room temperature with picosecond time resolution resulted in two main decay components with lifetimes of about 7.5 and 18 ps and spectra peaking at about 685 nm. Especially in the red flanks, these spectra show consistent differences, which means that earlier proposed models for the primary charge separation reactions based on ultrafast (∼1 ps) excitation equilibration processes cannot describe the data. We show target analyses of a number of alternative models and conclude that a simple model (Ant2)* ↔ (Ant1/RC)* → RP2 can explain the time-resolved emission data very well. In this model, (Ant2)* represents chlorophylls that spectrally equilibrate in about 7.5 ps and in which RP2 represents the "final" radical pair P700(+)A0(-). Adding an equilibrium (Ant1/RC)* ↔ RP1, in which RP1 represents an "intermediate" radical pair A(+)A0(-), resulted in the same fit quality. We show that the simple model without RP1 can easily be extended to PSI complexes from cyanobacteria with one or more pools of red antenna chlorophylls and also that the model provides a straightforward explanation of steady-state emission properties observed at cryogenic temperatures.

In the unicellular red alga Rhodella violacea iron deficiency induces an accumulation of uncoupled LHC.

Iron plays a key role in the synthesis and functioning of the photosynthetic apparatus. Conditions of partial iron deficiency that lead to a relatively stable phenotype were established and the effects of starvation studied in the unicellular red alga, Rhodella violacea. Synthesis of the photosynthetic pigments were found to decrease, with phycobiliproteins being affected to a lesser extent than chlorophyll a. Biophysical, biochemical and immunological approaches were used to show that the PSI content is highly diminished and the PSII/PSI stoichiometry increased by a factor of 5 compared to standard conditions. Meanwhile light-harvesting complex (LHC) was still assembled in the thylakoid membranes at unchanged levels. The use of translation inhibitors for either nuclear- or plastid-encoded polypeptides revealed that uncoupled LHC may be responsible for the high wavelength-fluorescence contribution observed around 700-710 nm. There is no evidence for the synthesis of new chlorophyll-protein complexes.