Abstract
Cytochrome bc 1 complexes have been isolated from wild type Rhodopseudomonas viridis and Rhodospirillum rubrum and purified by affinity chromatography on cytochrome c-Sepharose 4B. Both complexes are largely free of bacteriochlorophyll and carotenoids and contain cytochromes b and c 1 in a 2:1 molar ratio. For the Rps. viridis complex, evidence has been obtained for two spectrally distinct b-cytochromes. The R. rubrum complex contains a Rieske iron-sulfur protein (present in approximately 1:1 molar ratio to cytochrome c 1) and catalyzes an antimycin A- and myxothiazol- sensitive electron transfer from duroquinol to equine cytochrome c or R. rubrum cytochrome c 2. Although an attempt to prepare a cytochrome bc 1 complex from the gliding green bacterium Chloroflexus aurantiacus was not successful, membranes isolated from phototrophically grown Cfl. aurantiacus were shown to contain a Rieske iron-sulfur protein and protoheme (the prosthetic group of b-type cytochromes).
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© 1986 Martinus Nijhoff/Dr. W. Junk Publishers, Dordrecht
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Wynn, R.M., Gaul, D.F., Choi, WK., Shaw, R.W., Knaff, D.B. (1986). Isolation of cytochrome bc 1 complexes from the photosynthetic bacteria Rhodopseudomonas viridis and Rhodospirillum rubrum . In: Amesz, J., Hoff, A.J., Van Gorkum, H.J. (eds) Current topics in photosynthesis. Springer, Dordrecht. https://doi.org/10.1007/978-94-009-4412-1_18
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DOI: https://doi.org/10.1007/978-94-009-4412-1_18
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