Abstract
The chlorosome of the green photosynthetic bacterium, Chloroflexus aurantiacus, contains rod elements composed of Bchl c complexed with a 5.6 kDa protein. This protein, termed the Bchl c-binding protein, dimerizes to form subunits which assemble into rods. This Bchl c pigment-protein complex functions in harvesting light and transferring energy with nearly 100 percent efficiency to the Bchl-a located in the chlorosome baseplate, the cytoplasmic membrane (CM), and finally to the reaction center. Surrounding the rod elements is a special envelope which appears in electron micrographs to have characteristics of an unusual lipid protein monolayer. Two proteins, Mr 11,000 and 18,000 KDa, are closely associated with the surface of rthe chlorosome and appear to be integral components of this envelope (1,2,3,4).
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Redlinger, T.E., Theroux, S.J., Driscoll, D.L., Robinson, S.J., Fuller, R.C. (1990). Assembly of Chlorosomes during Photosynthetic Development in Chloroflexus aurantiacus . In: Drews, G., Dawes, E.A. (eds) Molecular Biology of Membrane-Bound Complexes in Phototrophic Bacteria. FEMS Symposium. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-0893-6_32
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