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Location of the electron accepting site of a b type cytochrome oxidase in purified chromatophore membranes and spheroplast membrane vesicles from photosynthetically grown rhodopseudomonas sphaeroides



Location of the electron accepting site of a b type cytochrome oxidase in purified chromatophore membranes and spheroplast membrane vesicles from photosynthetically grown rhodopseudomonas sphaeroides



Plant & Cell Physiology 25(5): 769-774



Purified chromatophore membranes and spheroplast membrane vesicles were prepared from R. sphaeroides by the method of Michels and Konings (1978). The cytochrome c oxidase activity of the spheroplast membrane vesicles was about 15-fold higher on a bacteriochlorophyll basis than that of the chromatophore membranes. The cytochrome c oxidase activity of the chromatophore membranes was greatly stimulated (about 10-fold) by an addition of Triton X-100 (0.1%), but there was less stimulated (about 1.5-fold) in the case of spheroplasts. The pH optimum of the oxidase activities of the spheroplast membrane vesicles and of chromatophore membranes treated with 0.1% Triton X-100, and the salt dependencies of the activity of both preparations were the same. The membrane-bound b-type cytochrome oxidase of this bacterium accepts electrons from ferrocytochrome c on the periplasmic side of the membrane (on the outer surface of the spheroplast membrane vesicles). These results also are consistent with the fact that cytochrome c2 is located in the periplasmic space in this bacterium.

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