Abstract
Chloroflexus aurantiacus is a thermophilic green photosynthetic bacterium containing a reaction center with a pigment composition different from that of purple bacteria; the reaction center is deficient in carotenoids and instead of four bacteriochlorophylls (BChls) and two bacteriopheophytins (BPhs) it contains 3 BChls and 3 BPhs (Blankenship et al., 1984). Similarly, the protein composition of Ch1.aurantiacus RC is quite peculiar: (a) it is composed of only two protein subunits (L, M); (b) peptide-mapping of these two polypeptides indicates a high degree of structural similarity; (c) it is the smallest functionally active RC thus far and (d) it shows thermal stability (Shiozawa et al. 1987; Schiozawa et al., 1989; Pierson et al., 1983). Conversely, the photochemical and early electron-transfer reactions, as determined by fast spectroscopy and circular dichroism in RCs preparations, suggest many similarities with the purple bacteria counterpart (Kirmaier and Holten, 1987). In addition, several aspects of secondary electron transport (Zannoni and Ingledew, 1985) and the light-dependent energy trasducing machinery of Chloroflexus (Venturoli and Zannoni, 1987) can be brought back to previous observations in purple non-sulphur bacteria.
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Venturoli, G., Feick, R., Trotta, M., Zannoni, D. (1990). Thermodynamic and Kinetic Features of the Redox Carriers Operating in the Photosynthetic Electron Transport of 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_50
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DOI: https://doi.org/10.1007/978-1-4757-0893-6_50
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