Abstract
A light-harvesting chlorophyll a/b-protein complex (LHCP) was isolated directly from thylakoid membranes of marine green alga,Bryopsis corticulans, by two consecutive runs of liquid chromatography. The trimeric form of the light-harvesting complex has been obtained by sucrose gradient ultracentrifugation. The result of SDS-PAGE shows that the light-harvesting complex is composed of at least five apoproteins in which a protein with apparent molecular weight of about 31 kD was never found in the major light-harvesting complex (LHC II) from higher plants. The isolatedBryopsis corticulans light-harvesting complex contains a specific carotenoid, siphonaxanthin, as well as chlorophyll (Chl)a, Chlb, neoxanthin and violaxanthin. Siphonaxanthin which is present in the light-harvesting siphonaxanthin-chlorophylla/b-protein complex ofBryopsis corticulans is responsible for enhanced absorption in the blue-green region (530 nm). Efficient energy transfer from both siphonaxanthin and Chlb to Chla inBryopsis corticulans LHCP, which has similar absorption and fluorescence emission spectra to those of the lutein-chlorophylla/b-protein of higher plants, proved that molecular arrangement of the light-harvesting pigments was highly ordered in theBryopsis corticulans LHCP. The siphonaxanthin-chlorophyll a/b-proteins allow enhanced absorption of blue-green light, the predominant light available in deep ocean waters or shaded subtidal marine habitats.
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Chen, H., Shen, S., He, J. et al. A light-harvesting siphonax-anthin-chlorophylla/b-protein complex of marine green alga,Bryopsis corticulans . Chin. Sci. Bull. 49, 1936–1941 (2004). https://doi.org/10.1007/BF03184285
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DOI: https://doi.org/10.1007/BF03184285