Abstract
The specific succinate dehydrogenase (EC 1.3.99.1 succinate: phenazine methosulfate oxidoreductase) activity of membranes of aerobically grown Rhodospirillum rubrum was found to be 4–7-fold greater than that of membranes from phototrophically grown cells. The enzymes obtained from cells grown under both conditions were compared in crossed immunoelectrophoresis and were shown to have the same electrophoretic mobility and immunological identity. As succinate dehydrogenase activity is associated with chromatophore membrane in phototrophically grown R. rubrum, this study demonstrates the presence of a chromatophore-specific component in aerobic cells. The succinate dehydrogenase activity of Triton extracts of membranes from phototrophic cells was subject to photoinactivation. The succinate dehydrogenase extracted from the membranes from aerobic cells was photoinactivated only if a bacteriochlorophyll a extract was added to the enzyme preparation. As this photopigment-dependent photoinactivation was inhibited by NaN3 or by a N2 atmosphere, it is attributed to the effects of singlet oxygen sensitized by bacteriochlorophyll a.
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Abbreviations
- SDH:
-
succinate dehydrogenase
- CIE:
-
crossed immunoelectrophoresis
- BChl:
-
bacteriochlorophyll a
- PMS:
-
phenazine methosulfate
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Collins, M.L.P., Hughes, C.A.N. Identity of succinate dehydrogenase in chemotrophically and phototrophically grown Rhodospirillum rubrum . Arch. Microbiol. 136, 7–10 (1983). https://doi.org/10.1007/BF00415601
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DOI: https://doi.org/10.1007/BF00415601