A new plant-type ferredoxin from halobacteria.
A new plant-type ferredoxin from halobacteria.
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来自盐细菌的新型植物型铁氧还蛋白。
DOI：
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发表时间：
1976
期刊：
影响因子：
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通讯作者：
D. Hall
中科院分区：
文献类型：
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作者：
L. Kerscher;D. Oesterhelt;R. Cammack;D. Hall
以盐杆菌为原料制备了稳定的2fe型铁氧还蛋白，并进行了色谱纯化。在另外三种盐杆菌中也发现了类似的铁氧还蛋白。铁氧还蛋白大量存在，约占可溶性蛋白总量的1%。从氨基酸组成计算出分子量为14800 +/- 200。铁氧还蛋白被发现含有铁原子和硫化物原子。蛋白质的中点氧化还原电位约为-345 mV。还原后的电子顺磁共振谱与植物和藻类的铁氧化还原蛋白相似，gx = 1.90, gy = 1.97, gz = 2.07。在光吸收光谱、旋光色散光谱和圆二色光谱中也观察到相同的相似性。然而，它似乎不介导叶绿体nadp光还原系统中的电子传递。细菌细胞提取物通过NADH催化铁氧还蛋白的还原。
A stable, 2Fe-type ferredoxin has been prepared from Halobacterium halobium and purified by chromatography. A similar ferredoxin was also found in three other Halobacteria. The ferredoxin is present in large amounts-about 1 percent of the total soluble protein. From amino acid composition a molecular weight of 14800 +/- 200 was calculated. The ferredoxin was found to contain two atoms each of iron and sulphide. The midpoint redox potential of the protein is about -345 mV. The electron paramagnetic resonance spectrum of the reduced form shows much similarity to plant and algal ferredoxins with gx = 1.90, gy = 1.97 and gz = 2.07. The same similarity is observed in the optical absorption, optical rotatory dispersion and circular dichroism spectra. However it does not seem to mediate electron transport in the NADP-photoreduction system of chloroplasts. Extracts of the bacterial cells catalyze the reduction of the ferredoxin by NADH.