PURIFICATION AND SOME PROPERTIES OF RUSTICYANIN, A BLUE COPPER PROTEIN INVOLVED IN IRON(II) OXIDATION FROM THIOBACILLUS-FERROOXIDANS
PURIFICATION AND SOME PROPERTIES OF RUSTICYANIN, A BLUE COPPER PROTEIN INVOLVED IN IRON(II) OXIDATION FROM THIOBACILLUS-FERROOXIDANS
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DOI：
10.1042/bj1740497
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发表时间：
1978-01-01
影响因子：
4.1
通讯作者：
BOXER, DH
中科院分区：
文献类型：
--
作者：
COX, JC;BOXER, DH
采用(NH4)2SO4分级沉淀和离子交换层析的方法，从嗜化性细菌氧化亚铁硫杆菌的细胞中分离纯化了含铜蓝蛋白。该蛋白在低pH条件下稳定，由一条相对分子质量为16,500的多肽链组成，含0.79(.+-)。0.28)g原子的铜/摩尔。该蛋白质不含精氨酸残基，在287、450、597和750 nm处有最大吸光度，与天青素基本相似。分离的蛋白质被Fe2+以1：1的化学计量比直接还原为铜。Fe2+还原时，450、597和750 nm处的吸收峰消失，320 nm处出现新的吸收带。这些结果与黄花青素是呼吸铁氧化过程中Fe2+电子的初始受体是一致的。
The blue copper-containing protein rusticyanin was purified to homogeneity from cells of the chemolithotrophic bacterium T. ferrooxidans by (NH4)2SO4 fractionation and ion-exchange chromatography. The protein, which is stable at low pH, consists of a single polypeptide chain of MW 16,500 and possesses 0.79 (.+-. 0.28) g-atom of Cu/mol. The protein, which does not contain arginine residues, has optical absorbance maxima at 287, 450, 597 and 750 nm and is generally similar to azurin. The isolated protein is reduced directly by Fe2+ with a 1:1 stoicheiometry to Cu. On reduction by Fe2+ the absorption peaks at 450, 597 and 750 nm are abolished, with the appearance of a new absorption band at 320 nm. The results obtained are consistent with rusticyanin being the initial acceptor of electrons from Fe2+ during respiratory iron oxidation.