Science. 1981 Feb 27;211(4485):937-40. doi: 10.1126/science.211.4485.937.
Binding of the 4-azido analog of the herbicide atrazine to pea chloroplast membranes was compared with that of atrazine. When [(14)C]azidoatrazine was treated with 300-nanometer ultraviolet light in situ, reversibility of binding was lost in proportion to the duration of irradiation. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of chloroplast membranes irradiated in the presence of [(l4)C]-azidoatrazine indicated radioactivity in only one region, corresponding to a protein with a molecular weight of approximately 32,000. Azidoatrazine is a photoaffinity reagent for the triazine binding site in chloroplasts and serves as a label to identify this site, which may be the apoprotein of the secondary electron acceptor in photosystem II.
与脒唑啉除草剂相比，研究了 4-叠氮基类似物与豌豆叶绿体膜的结合情况。当[14C]叠氮脒唑啉在原位用 300nm 紫外线处理时，结合的可逆性随着照射时间的延长而相应地丧失。在[14C]叠氮脒唑啉存在下照射的叶绿体膜的十二烷基硫酸钠-聚丙烯酰胺凝胶电泳仅显示一个区域的放射性，对应于分子量约为 32000 的蛋白质。叠氮脒唑啉是叶绿体中三嗪结合部位的光亲和试剂，可作为标记物来鉴定该部位，该部位可能是光系统 II 中次级电子受体的脱辅基蛋白。
