Monolayer films of phycobilisome-thylakoid membrane complexes isolated from Spirulina platensis were prepared at air/aqueous solution interface by using the Langmuir-Blodgett technique. The film preparation was optimized with 0.5 M phosphate buffer (pH 7.0) as sub-phase at 20 °C. The monolayer was transferred into grids and into mica surface for observing the surface image of the complexes by transmission electron microscopy and atomic force microscope, respectively. The shape of complexes was disk-like with the diameter of about 50 nm and the thickness of about 35 nm. The absorption and fluorescence spectra of the complexes in the monolayer were consistent with those in buffer solution, which suggests that the complexes in the monolayer preserve the basic functional groups of photosynthetic apparatus and can be used as a model to investigate the structural connection and functional association of the light-harvesting antenna with the reaction centres. and D.-H. Li ... [et al.].
The kinetic component (39 ps) for the energy transfer from a phycobilisome (PBS) to the photosystems was temperature-dependent while the components related to the kinetic processes within PBS, photosystem 2 (PS2) or PS1 were temperature-independent. The 39 ps component possessed the amplitude maximum at 647 nm but the minimum at 715 nm (room temperature) or 685 nm (0 °C), suggesting a direct energy transfer from C-phycocyanin to PS1 at room temperature but to PS2 at 0 °C. The temperature-induced kinetic change originated from a position shift of PBS along the thylakoid membrane. and Y. Li ... [et al.].