专性甲基营养菌的“甲胺氧化酶”系统
The 'methylamine oxidase' system of an obligate methylotroph.
作者信息
Auton K A, Anthony C
机构信息
Department of Biochemistry, University of Southampton, U.K.
出版信息
Biochem J. 1989 May 15;260(1):75-9. doi: 10.1042/bj2600075.
The terminal respiratory oxidase was solubilized from membranes of organism 4025, an obligate methylotroph. The partially purified oxidase is probably a cytochrome co. It does not oxidize amicyanin, but it oxidizes 'azurin' and cytochromes cH and cL. By using a complete 'methylamine oxidase' system reconstituted from pure methylamine dehydrogenase, purified oxidase and soluble blue copper proteins and cytochromes, it was confirmed that amicyanin is essential for methylamine oxidation; it could not be replaced by 'azurin' or cytochrome cH or cL. It was shown that the usual mediator between amicyanin and the oxidase is cytochrome cH, with 'azurin' able to replace it during growth at the high copper concentrations required for optimum growth of this unusual methylotroph.
终端呼吸氧化酶是从专性甲基营养菌4025的细胞膜中溶解出来的。部分纯化的氧化酶可能是一种细胞色素c。它不氧化氨腈蓝蛋白，但能氧化“天青蛋白”以及细胞色素cH和cL。通过使用由纯甲胺脱氢酶、纯化的氧化酶、可溶性蓝色铜蛋白和细胞色素重构的完整“甲胺氧化酶”系统，证实氨腈蓝蛋白对甲胺氧化至关重要；它不能被“天青蛋白”或细胞色素cH或cL替代。结果表明，氨腈蓝蛋白与氧化酶之间通常的介质是细胞色素cH，在这种不寻常的甲基营养菌最佳生长所需的高铜浓度下生长时，“天青蛋白”能够替代它。
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