Wilson E, Farley T M, Takemoto J Y
J Biol Chem. 1985 Aug 25;260(18):10288-92.
Tritium-labeled 3-azidosalicyl-N-(n-octadecyl)amide was synthesized and used as a photoaffinity probe for the antimycin-binding site in both purified ubiquinone-cytochrome b-c1 oxidoreductase and chromatophore vesicles from the photosynthetic bacterium Rhodopseudomonas sphaeroides. In both systems, a prominently labeled protein had a molecular weight of 11,000. Binding to this protein was inhibited by preincubation of the reaction mixture with antimycin prior to addition of the radioactive analog and subsequent irradiation. The antimycin analog, 3-azidosalicyl-N-(n-octadecyl)amide, inhibited succinate-cytochrome c reductase activity in chromatophore vesicles by 50% at a concentration of 150 nmols/mg of protein.
合成了氚标记的3-叠氮基水杨酰-N-(正十八烷基)酰胺，并将其用作纯化的泛醌-细胞色素b-c1氧化还原酶和光合细菌球形红假单胞菌的载色体囊泡中抗霉素结合位点的光亲和探针。在这两个系统中，一个显著标记的蛋白质分子量为11,000。在加入放射性类似物并随后照射之前，将反应混合物与抗霉素预孵育可抑制与该蛋白质的结合。抗霉素类似物3-叠氮基水杨酰-N-(正十八烷基)酰胺在浓度为150 nmol/mg蛋白质时，可使载色体囊泡中的琥珀酸-细胞色素c还原酶活性抑制50%。
