A light-harvesting chlorophyll a/b-protein complex (LHCP) was isolated directly from thylakoid mem-branes of marine green alga, Bryopsis corticulans, by two consecutive runs of liquid chromatography. The trimeric form...A light-harvesting chlorophyll a/b-protein complex (LHCP) was isolated directly from thylakoid mem-branes 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 ma-jor light-harvesting complex (LHC Ⅱ) from higher plants. The isolated Bryopsis corticulans light-harvesting complex contains a specific carotenoid, siphonaxanthin, as well as chlorophyll (Chl) a, Chl b, neoxanthin and violaxanthin. Si-phonaxanthin which is present in the light-harvesting sipho-naxanthin-chlorophyll a/b-protein complex of Bryopsis corticulans is responsible for enhanced absorption in the blue-green region (530 nm). Efficient energy transfer from both siphonaxanthin and Chl b to Chl a in Bryopsis corticu-lans LHCP, which has similar absorption and fluorescence emission spectra to those of the lutein-chlorophyll a/b-protein of higher plants, proved that molecular arrangement of the light-harvesting pigments was highly ordered in the Bryopsis corticulans LHCP. The siphonaxanthin-chlorophyll a/b-pro- teins allow enhanced absorption of blue-green light, the pre-dominant light available in deep ocean waters or shaded subtidal marine habitats.展开更多
文摘A light-harvesting chlorophyll a/b-protein complex (LHCP) was isolated directly from thylakoid mem-branes 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 ma-jor light-harvesting complex (LHC Ⅱ) from higher plants. The isolated Bryopsis corticulans light-harvesting complex contains a specific carotenoid, siphonaxanthin, as well as chlorophyll (Chl) a, Chl b, neoxanthin and violaxanthin. Si-phonaxanthin which is present in the light-harvesting sipho-naxanthin-chlorophyll a/b-protein complex of Bryopsis corticulans is responsible for enhanced absorption in the blue-green region (530 nm). Efficient energy transfer from both siphonaxanthin and Chl b to Chl a in Bryopsis corticu-lans LHCP, which has similar absorption and fluorescence emission spectra to those of the lutein-chlorophyll a/b-protein of higher plants, proved that molecular arrangement of the light-harvesting pigments was highly ordered in the Bryopsis corticulans LHCP. The siphonaxanthin-chlorophyll a/b-pro- teins allow enhanced absorption of blue-green light, the pre-dominant light available in deep ocean waters or shaded subtidal marine habitats.
