Dimeric carotenoid interaction in the light-harvesting antenna of purple phototrophic bacteria.
The carotenoid content of intracytoplasmic membrane vesicles isolated from purple phototrophic bacteria was reduced to a variable extent by mild extraction with light petroleum. Using preparations obtained from Rhodobacter capsulatus strains that contained the Light Harvesting System I (LHI) complex as the only major photosynthetic holochrome, it was shown that the visible circular dichroism of the carotenoids increased with the square of the membrane carotenoid content, as expected from being caused by dimeric exciton interaction. No chirality resulting from twists of the individual planar chromophore was detected. Therefore the contribution to carotenoid optical activity of non-degenerate interactions with bacteriochlorophyll or the apoprotein does not appear to be significant. The broadening of the absorption band of the bound pigment, caused by the splitting of the monomer transition, was demonstrated in membrane vesicles of both Rb, capsulatus and Rhodospirillum rubrum as a decrease of the fine structure of the band. Furthermore, the dimeric organization of the carotenoid pigments in the bacterial LHI complex accounted for the observed quantitative relationship between the fine structure of the band and the carotenoid content of the membrane.
Zurdo
J
J
Centro de Investigaciones Biológicas del C.S.I.C., Velázquez, Madrid, Spain.
Lozano
R M
RM
Fernandez-Cabrera
C
C
Ramirez
J M
JM
D002338:Carotenoids / Q000378:metabolism*; D002942:Circular Dichroism; D045342:Light-Harvesting Protein Complexes; D045322:Photosynthetic Reaction Center Complex Proteins / Q000378:metabolism*; D016354:Rhodobacter capsulatus / Q000378:metabolism*; D012247:Rhodospirillum rubrum / Q000378:metabolism; D013057:Spectrum Analysis
D045342:Light-Harvesting Protein Complexes; D045322:Photosynthetic Reaction Center Complex Proteins; D002338:Carotenoids