Abstract
In this paper we attempt a functional and spectral characterization of the membrane-bound cytochromes involved in respiratory electron transport by membranes from cells of Chloroflexus aurantiacus grown in the dark under oxygen saturated conditions. We conclude that the NADH-dependent respiration is carried out by a branched respiratory chain leading to two oxidases which differ in sensitivity to CN- and CO. The two routes also show a different sensitivity to the ubiquinone analogue, HQNO, the pathway through the cytochrome c oxidase being fully blocked by 5 μM HQNO, whereas the “alternative” one is insensitive to this inhibitor. The cytochrome c oxidase containing branch is composed by at least two c-type haems with E m 7.0 of +130 and +270 mV (α bands at 550/553 nm and 549 nm, respectively), plus a b-type cytochrome with E m 7.0 of +50 mV (α band at 561 nm). From this, and previous work, we conclude that respiratory and photosynthetic electron transport components are assembled together and function on a single undifferentiated plasma membrane.
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Abbreviations
- HQNO:
-
heptylhydroxy-quinoline-N-oxide
- UHDBT:
-
undecyl-hydroxydioxobenthiazole
- Q/b-c :
-
ubiquinol/cytochrome c oxidoreductase complex
- BChl:
-
bacteriochlorophyll
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Zannoni, D., Fuller, R.C. Functional and spectral characterization of the respiratory chain of Chloroflexus aurantiacus grown in the dark under oxygen-saturated conditions. Arch. Microbiol. 150, 368–373 (1988). https://doi.org/10.1007/BF00408309
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DOI: https://doi.org/10.1007/BF00408309