Search results for "Mantoniella"
showing 7 items of 7 documents
Purification and identification of chlorophyll c1 from the green alga Mantoniella squamata
1987
Abstract The prasinophycean alga Mantoniella squamata contains besides chlorophyll a and b a third chlorophyll c -like pigment in its light-harvesting antenna. This third chlorophyll was purified by reverse phase and polyethylene chromatography in order to identify its chemical structure. The absorption and fluorescence spectra were measured not only from the doubly purified pigment, but also from its Mg-free derivates. The spectra were compared with those of authentic chlorophyll c and of Mg-2,4-desethyl-2,4-divinylpheoporphyrin a 5 monomethyl ester which was isolated from Rhodobacter capsulata . The results show that the pigment from Mantoniella agrees best with chlorophyll c 1 . In order…
Energy transfer and pigment composition in three chlorophyll b-containing light-harvesting complexes isolated from Mantoniella squamata (Prasinophyce…
1986
Light-harvesting Chl a/b protein complexes were isolated from the higher plant Sinapis alba, the green alga Chlorella fusca, and the prasinophycean alga Mantoniella squamata by mild gel electrophoresis. The energy transfer from chlorophyll b and the accessory xanthophyll was measured by means of fluoresence spectroscopy at 77 K. The pigment composition of the isolated antenna complexes was determined by high performance liquid chromatography in order to calculate the number of light absorbing molecules per chlorophyll a in the different light-harvesting complexes. These results were complemented by the quantitation of the pigments in total thylakoids as well as in the different electrophore…
Comparative analysis of the composition of two chlorophyll-b-containing light-harvesting complexes.
1990
The major light-harvesting complexes from Mantoniella squamata (Prasinophyceae) and from Chlorella fusca (Chlorophyceae) were analyzed with respect to polypeptide composition and pigmentation. It was found that the polypeptides of Mantoniella are smaller than those of Chlorella and bind twice the amount of pigment. We assume that the amount of pigment per polypeptide is of ecological as well as of taxonomical importance.
Reconstitution of Light-Harvesting Complexes from Chlorella fusca (Chlorophyceae) and Mantoniella squamata (Prasinophyceae)
1993
Abstract Reconstitution experiments of light-harvesting complexes were performed with the green alga Chlorella fusca and the chlorophyll c-containing prasinophyte Mantoniella squamata using a modified method according to Plumley and Schmidt [Proc. N atl. Acad. Sei. U .S.A . 84, 146 -150 (1987)]. Changing the pigment supply quantitatively or qualitatively in the reconstitution mixture homologous and heterologous reconstitutes were obtained. In contrast to higher plants, light-harvesting polypeptides from green algae are able to bind the chlorophylls as well as the xanthophylls in different stoichiometries. Heterologous reconstitutes of M . squamata polypeptides give further evidence for a r…
The Existence of Chlorophyll c in the Chl b‐Containing, Light‐Harvesting Complex of the Green Alga Mantoniella squamata (Prasinophyceae)
1988
The prasinophycean alga Mantoniella contains, in addition to Chl a and b, at least a third green pigment which is functionally active in the light-harvesting antenna. This third Chl was isolated in order to elucidate its chemical structure. The absorption and fluorescence spectra were measured not only from the purified pigment but also from its pheophytin and its methylpheophorbide. The spectra were compared with those of authentic Chl c-1 and c-2, which were isolated from the diatom Nitzschia sp. and with Mg-DVPP (purified from Rhodobacter). The results show that the pigment from Mantoniella compares best with Chl c-1. In order to clarify the spectral data, Chl c-1 and c-2, Mg-DVPP, and t…
Reconstitution and Pigment Exchange
2007
Polypeptide sequence of the chlorophyll a/b/c-binding protein of the prasinophycean alga Mantoniella squamata.
1994
The primary structure of the Chla/b/c-binding protein from Mantoniella squamata is determined. This is the first report that protein sequencing reveals one modified amino acid resulting in a LHCP-specific TFA-cleavage site. The comparison of the sequence of Mantoniella with other Chla/b-and Chla/c-binding proteins shows that the modified amino acid is located in a region which is highly conserved in all these proteins. The alignment also reveals that the LHCP of Mantoniella is related to the Chla/b-binding proteins. Finally, possible Chl-binding regions are discussed.