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We developed a fluorescence confocal microscope equipped with a hemispherical solid immersion lens (SIL) and apply it to study the optical properties of light-harvesting complexes. We demonstrate that the collection efficiency of the SIL-equipped microscope is significantly improved, as is the spatial resolution, which reaches 600 nm. This experimental setup is suitable for detailed studies of physical phenomena in hybrid nanostructures. In particular, we compare the results of fluorescence intensity measurements for a light-harvesting peridinin-chlorophyll-protein (PCP) complex with and without the SIL.
Eleven proteins belonging to photosystem II (PSII) bind photosynthetic pigments in the form of thylakoid membrane-associated pigment-protein complexes. Five of them (PsbA, PsbB, PsbC, PsbD and PsbS) are assigned to PSII core complex while the remaining six (Lhcb1, Lhcb2, Lhcb3, Lhcb4, Lhcb5 and Lhcb6) constitute, along with their pigments, functional complexes situated more distantly with regard to P680 - the photochemical center of PSII. The main function of the pigment-binding proteins is to harvest solar energy and deliver it, in the form of excitation energy, ultimately to P680 although individual pigment-proteins may be engaged in other photosynthesis-related processes as well. The aim of this review is to present the current state of knowledge regarding the structure, functions and degradation of this family of proteins.
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