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Characterization of the Main Light-Harvesting Chlorophyll a／b-Protein Complex of Green Alga, Bryopsis corticulans

Acta Botanica Sinica 2004年第10期46卷 1192-1199页

作者： CHENHuil SHENShi-Hua GONGYan-Dao HEJun-Fang WANGGuang-Ce LILiang-Bi KUANGTing-Yun KeyLaboratoryofPhotosynthesisandEnvironmentalMolecularPhysiology InstituteofBotanyTheChineseAcademyofSciencesBeijing100093China DepartmentofBiologicalSciencesandBiotechnology TsinghuaUniversityBeijing100084China StateKeyLaboratoryofTransientOpticsandTechnology Xi＇anInstituteofOpticsandPrecisionMechanicsTheChineseAcademyofSciencesXi＇an710068China KeyLaboratoryofExperimentalMarineBiology InstituteofOceanologyTheChineseAcademyofSciencesQingdao266071China

The main light-harvesting chlorophyll a/b -protein complex (LHC Ⅱ) has been isolated directly from thylakoid membranes of shiphonous 8Teen alga, Bryopsis corticulans Setch. by using two consecutive runs of anion exchange and gel-filtration chromatography. Monomeric and trimeric subcomplexes of LHC Ⅱ were obtained by using sucrose gradient ultracentrifugation. Pigment analysis by reversed-phase high performance liquid chromatography showed that chlorophyll a (Chl a), chlorophyll b (Chl b), neoxanthin, violaxanthin and siphonaxanthin were involved in LHC Ⅱ from B. corticulans. The properties of electronictransition of monomeric LHC Ⅱ showed similarities to those of trimeric LHC Ⅱ. Circular dichroism spectroscopy showed that strong intramolecular interaction of excitonic dipoles between Chl a and between Chl b exist in one LHC Ⅱ apoprotein, while the intermolecular interaction of these dipoles can be intensified in the trimeric structure. The monomer has high efficient energy transfer from Chl b and siphonaxanthin to Chl a similarly to that of the trimer. Our results suggest that in B. corticulans, LHC Ⅱ monomer has high ordered pigment organization that play effective physiological function as the trimer, and thus it might be also a functional organization existing in thylakoid membrane of ***.

关键词：光收获叶绿素蛋白质复合体绿藻羽藻属

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

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Chinese Science Bulletin 2004年第18期49卷 1936-1941页

作者： CHENHui SHENShihua HEJunfang LENGJing LILiangbi KUANGTingyun KeyLaboratoryofPhotosynthesisandEnvironmentalMolecularPhysiology InstituteofBotanyChineseAcademyofSciencesBeijing100093China StateKeyLaboratoryofTransientOpticsandTechnology Xi'anInstituteofOpticsandMechanicsChineseAcademyofSciences.Xi'an710068China

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.

关键词：叶绿素-蛋白质合成物管藻黄素类囊体液相色谱法羽藻属绿藻类

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