| Abstract: | 1. The peridinin.chlorophyll a.protein complex from Amphidinium carterae (Plymouth 450) shows spectroscopic characteristic (absorption, CD, fluorescence polarization, lifetime and energy transfer) essentially identical with peridinin.chlorophyll a.protein complexes from Glenodinium sp., Gonyaulax polyedra and Amphidinium rhyncocephaleum. 2. The apoprotein of peridinin.chlorophyll a.protein complexes is globular, with an isotropic rotational relaxation time (e.g. 33 ns for the A. caterae peridinin.chlorophyll a.protein), as deduced from the dynamic depolarization data. 3. The chromophores (4 peridinins and 1 chlorophyll a for peridinin.chlorophyll a.protein complexes from Glenodinium sp., G. polyedra and A. rhyncocephaleum and 9 and 2, respectively, for peridinin.chlorophyll a.protein of A. carterae) are accommodated in a hydrophobic crevice and not exposed to the solvent. The surface of the protein is highly hydrophilic. 4. No evidence for chlorophyll-chlorophyll interactions in the A. carterae peridinin.chlorophyll a.protein was obtained. This implies that binding crevices for two chlorophylls and half of peridinins (four to five) are located at some distance from each other. 5. The peridinin.chlorophyll a.protein complexes function as the photosynthetic antenna pigment. In addition, peridinins effectively protect chlorophyll a from photodecomposition. |
