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- W2023595944 abstract "Membrane fragments from exponential phase cells of Rhodospirillum rubrum, grown aerobically in the dark, can be obtained by incubation with lysozyme (EC 3.2.1.17) at pH 7.3 in Tris buffer, followed by disruption in a French Pressure cell and purification by sucrose gradient centrifugation. Average oxidase activities with NADH and succinate as substrates are 250 and 180 mμmoles O2 absorbed per min per mg protein, respectively. Other electron donors give comparable values. Regardless of the electron donor used, there is marked inhibition by CO, which is photoreversible. Low temperature difference spectra (dithionite, reduced minus ferricyanide, oxidized) show the α-peak of c-type cytochromes and an asymmetrical α-peak of b-type cytochromes. The latter peak is composed of contributions from at least two separate b-type cytochromes. The first is a b-type cytochrome of low potential associated apparently with the succinate dehydrogenase activity, the second present in lesser amounts is a high potential, CO-binding cytochrome with a protohaem prosthetic group. No a-type cytochrome is present. Evidence is presented which supports the conclusion that this CO-binding pigment is the functional oxidase of dark-grown R. rubrum and is not related to Rhodospirillum haem protein, the variant c-type cytochrome present in light-grown cells, but absent, on the basis of spectrochemical and immunochemical assays, from dark-grown cells." @default.
- W2023595944 created "2016-06-24" @default.
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- W2023595944 date "1965-03-01" @default.
- W2023595944 modified "2023-09-25" @default.
- W2023595944 title "The oxidase system of heterotrophically-grown rhodospirillum rubrum" @default.
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- W2023595944 doi "https://doi.org/10.1016/0005-2787(65)90560-5" @default.
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