反硝化菌“环裂无色杆菌”中铜蛋白的性质及电子转移特异性
Properties and electron transfer specificity of copper proteins from the denitrifier "Achromobacter cycloclastes".
作者信息
Liu M Y, Liu M C, Payne W J, Legall J
出版信息
J Bacteriol. 1986 May;166(2):604-8. doi: 10.1128/jb.166.2.604-608.1986.
Abstract
A blue copper protein (Mr 12,000) was purified from cells of "Achromobacter cycloclastes" grown as a denitrifier. When reduced, the blue copper protein transferred electrons to the copper protein nitrite reductase purified from the same cells, whereas a variety of cytochromes from denitrifiers failed to do so. Inclusion of a protease inhibitor, phenylmethylsulfonyl fluoride, in the buffers employed during preparation yielded purified blue copper protein with 18 more amino acid residues and two times more specific enzyme activity than other researchers have found.
摘要
从以反硝化菌形式生长的“解环无色杆菌”细胞中纯化出一种蓝色铜蛋白（分子量12,000）。还原后，该蓝色铜蛋白将电子转移至从同一细胞中纯化出的铜蛋白亚硝酸还原酶，而来自反硝化菌的多种细胞色素则无法做到这一点。在制备过程中使用的缓冲液中加入蛋白酶抑制剂苯甲基磺酰氟，得到的纯化蓝色铜蛋白比其他研究人员发现的多18个氨基酸残基，比活性是其他研究人员发现的两倍。
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