Structure and molecular organization of the photosynthetic accessory pigments of cyanobacteria and red algae |
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Authors: | Glazer Alexander N |
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Institution: | (1) Department of Bacteriology and Immunology, University of California, 94720 Berkeley, California, USA |
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Abstract: | Summary Cyanobacteria (blue-green algae) and Rhodophyta (red algae) contain high concentrations of photosynthetic accessory pigments (phycobiliproteins) which trap light energy in the region between 400 and 650 nm. The electronic excitation energy is then transferred along a chain of these pigments to the reaction center chlorophyll of Photosystem II by a radiationless induced resonance process.Unlike the protein-chlorophyll complexes in the photosynthetic lamellae, the phycobiliproteins are readily soluble in aqueous solution, can be isolated in a variety of assembly forms, and crystallize readily. These properties facilitate the study of the structure of these proteins by chemical, physical, and immunological methods, as well as by X-ray diffraction and electron microscopy.The brilliantly colored phycobiliproteins are a homologous family of conjugated proteins of differing spectroscopic properties. The basic structural unit in these proteins is a monomer of 30,000–40,000 daltons made up of two dissimilar polypeptide chains, and . Each subunit carries covalently linked tetrapyrrole prosthetic groups related to the bile pigment biliverdin.The distinctive spectroscopic properties of each phycobiliprotein are a consequence of the chemical structure of the bile pigment it carries, and of the influence of the conformation and aggregation state of the protein on the spectra of these prosthetic groups.
In vivo, the phycobiliproteins are organized into particles, phycobilisomes, attached in a regular array to the outer surface of the photosynthetic lamellae. Studies on phycobilisomes, and on intact cells, indicate the following pathway of energy transfer.Phycoerythrin Phycocyanin ( max 560 nm) ( max 620 nm) Allophycocyanin Allophycocyanin B ( max 650 nm)( max 671 nm) Chlorophyll a ( max 680 nm)The amounts of the various phycobiliproteins in the cell are influenced by the intensity and energy distribution of the incident radiation. The phenomena of intensity adaptation and complementary chromatic adaptation yield insights into the structure of phycobilisomes and the molecular basis of the plasticity of the structure of this light-harvesting system.Invited article. |
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