A light-harvesting siphonax-anthin-chlorophyll a／b-protein complex of marine green alga, Bryopsis corticulans

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 SDSPAGE 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 isolated Bryopsis corticulans light-harvesting complex contains a specific carotenoid, siphonaxanthin, as well as chlorophyll (Chl) a, Chl b, neoxanthin and violaxanthin. Siphonaxanthin which is present in the light-harvesting siphonaxanthin-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 corticulans 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-proteins allow enhanced absorption of blue-green light, the predominant light available in deep ocean waters or shaded subtidal marine habitats.

A light-harvesting siphonax-anthin-chlorophylla/b-protein complex of marine green alga,Bryopsis corticulans

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 isolated Bryopsis corticulans light-harvesting complex contains a specific carotenoid, siphonaxanthin, as well as chlorophyll (Chl) a, Chl b, neoxanthin and violaxanthin. Siphonaxanthin which is present in the light-harvesting siphonaxanthin-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 corticulans 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 predominant light available in deep ocean waters or shaded subtidal marine habitats.