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- W2005941741 abstract "Summary The thermoacidophilic and aerobic archaebacterium Sulfolobus acidocaldarius was less sensitive to uncouples or inhibitors of energy transducing membranes than other acidophiles. About 10−4M azide or cyanide was necessary to inhibit the growth completely. NADH oxidase, cytochrome a and two types of ATPase (neutral and acidic) were detected in the membrane fraction. Cytochrome a appeared to be the main cytochrome in Sulfolobus. Using horse heart cytochrome c, oxidase activity was observed with a Km of 24 μM. The activity was inhibited by about 50% by either 10−5 M azide or cyanide. These results indicate cytochrome a to be the terminal oxidase of the respiratory chain. Neutral ATPase was activated slightly by sulfate. This enzyme was acid-labile. Acid ATPase had an optimum pH of 2.5. It was inhibited by sulfate and extremely stable against acid and high temperature. The sensitivity to various inhibitors suggests that both Sulfolobus ATPases differ from F1 and other transport ATPases. Neutral ATPase is similar to that reported in Thermoplasma (Searcy et al., 1982). Acid ATPase was solubilized from membranes and partially purified by repeated DEAE Sephacel chromatography. Activities to hydrolyze ATP, ADP and PPi were copurified, suggesting that these acitvities are derived from an identical enzyme." @default.
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- W2005941741 date "1986-05-01" @default.
- W2005941741 modified "2023-09-27" @default.
- W2005941741 title "Membrane-bound ATPase and electron transport system of Sulfolobus acidocaldarius" @default.
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- W2005941741 doi "https://doi.org/10.1016/s0723-2020(86)80030-3" @default.
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