硝化单胞菌属（Nitrosomonas europaea）将硝吡咯烷（Nitrapyrin）氧化为 6-氯烟酸（6-Chloropicolinic Acid）。
Oxidation of Nitrapyrin to 6-Chloropicolinic Acid by the Ammonia-Oxidizing Bacterium Nitrosomonas europaea.
机构信息
Department of Genetics and Cell Biology, University of Minnesota, St. Paul, Minnesota 55108.
出版信息
Appl Environ Microbiol. 1992 Jul;58(7):2321-5. doi: 10.1128/aem.58.7.2321-2325.1992.
Abstract
Suspensions of Nitrosomonas europaea catalyzed the oxidation of the commercial nitrification inhibitor nitrapyrin [2-chloro-6-(trichloromethyl)-pyridine]. Rapid oxidation of nitrapyrin (at a concentration of 10 muM) required the concomitant oxidation of ammonia, hydroxylamine, or hydrazine. The turnover rate was highest in the presence of 10 mM ammonia (0.8 nmol of nitrapyrin per min/mg of protein). The product of the reaction was 6-chloropicolinic acid. By the use of O(2), it was shown that one of the oxygens in 6-chloropicolinic acid came from diatomic oxygen and that the other came from water. Approximately 13% of the radioactivity of [2,6-C]nitrapyrin was shown to bind to cells. Most (94%) of the latter was bound indiscriminately to membrane proteins. The nitrapyrin bound to membrane proteins may account for the observed inactivation of ammonia oxidation.
摘要
欧洲亚硝化单胞菌悬浮体催化了商业硝化抑制剂硝呋吡嗪[2-氯-6-(三氯甲基)-吡啶]的氧化。硝呋吡嗪（浓度为 10 μM）的快速氧化需要同时氧化氨、羟胺或肼。在 10 mM 氨（0.8 nmol 硝呋吡嗪/分钟/毫克蛋白）存在下，周转率最高。反应的产物是 6-氯烟酸。通过使用 O(2)，表明 6-氯烟酸中的一个氧来自双原子氧，另一个氧来自水。表明[2,6-C]硝呋吡嗪的约 13%放射性与细胞结合。后者的大部分（94%）无差别地结合到膜蛋白上。与膜蛋白结合的硝呋吡嗪可能解释了观察到的氨氧化失活。
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