Purification and characterization of the single-component nitric oxide reductase from Ralstonia eutropha H16
Purification and characterization of the single-component nitric oxide reductase from Ralstonia eutropha H16
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DOI：
10.1016/s0014-5793(99)01315-0
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发表时间：
1999-10-22
期刊：
影响因子：
3.5
通讯作者：
Friedrich, B
中科院分区：
文献类型：
--
作者：
Cramm, R;Pohlmann, A;Friedrich, B
采用两步层析法从真养罗尔斯通氏菌（Ralstonia eutropha）中纯化一氧化氮（NO）还原酶。与常见的NO还原酶不同，该酶由75 kDa的单个亚基组成，该亚基含有高自旋和低自旋血红素B，但缺乏血红素c。每个酶分子鉴定出一个额外的铁原子，可能是三价非血红素铁，而还原的细胞色素c作为电子供体是无效的，在2-甲基-1，4-萘醌存在下，NO以2.3 μ mol/min/mg蛋白质的比活性被还原，（C）1999欧洲生物化学学会联合会。
Nitric oxide (NO) reductase was purified from Ralstonia eutropha (formerly Alcaligenes eutrophus) using a two step chromatographic procedure. Unlike the common NO reductases, the enzyme consists of a single subunit of 75 kDa which contains both high-spin and low-spin heme b, but lacks heme c, One additional iron atom, probably a ferric non-heme iron, was identified per enzyme molecule, Whereas reduced cytochrome c was ineffective as electron donor, NO was reduced at a specific activity of 2.3 mu mol/min per mg of protein in the presence of 2-methyl-1,4-naphthoquinol, (C) 1999 Federation of European Biochemical Societies.