氧化亚铁硫杆菌中参与亚铁氧化的蓝色铜蛋白——锈铁氧化还原蛋白的纯化及某些性质
The purification and some properties of rusticyanin, a blue copper protein involved in iron(II) oxidation from Thiobacillus ferro-oxidans.
作者信息
Cox J C, Boxer D H
出版信息
Biochem J. 1978 Aug 15;174(2):497-502. doi: 10.1042/bj1740497.
Abstract
The 'blue' copper-containing protein rusticyanin was purified to homogeneity from cells of the chemolithotrophic bacterium Thiobacillus ferro-oxidans by (NH4)SO4 fractionation and ion-exchange chromatography. The protein, which is stable at low pH, consists of a single polypeptide chain of mol. wt. 16500 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.
摘要
通过硫酸铵分级分离和离子交换色谱法，从化能自养细菌氧化亚铁硫杆菌的细胞中纯化出了“蓝色”含铜蛋白锈胞蓝蛋白，使其达到同质状态。该蛋白在低pH值下稳定，由一条分子量为16500的单多肽链组成，每摩尔含有0.79（±0.28）克原子的铜。该蛋白不含精氨酸残基，在287、450、597和750纳米处有最大吸光度，总体上与天青蛋白相似。分离出的蛋白能被Fe²⁺以1:1的化学计量比直接还原为铜。被Fe²⁺还原后，450、597和750纳米处的吸收峰消失，在320纳米处出现新的吸收带。所得结果与锈胞蓝蛋白是呼吸性铁氧化过程中Fe²⁺电子的初始受体这一观点一致。
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