ISOLATION AND CHARACTERIZATION OF SOLUBLE CYTOCHROMES, FERREDOXINS AND OTHER CHROMOPHORIC PROTEINS FROM THE HALOPHILIC PHOTOTROPHIC BACTERIUM ECTOTHIORHODOSPIRA-HALOPHILA
ISOLATION AND CHARACTERIZATION OF SOLUBLE CYTOCHROMES, FERREDOXINS AND OTHER CHROMOPHORIC PROTEINS FROM THE HALOPHILIC PHOTOTROPHIC BACTERIUM ECTOTHIORHODOSPIRA-HALOPHILA
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DOI：
10.1016/0005-2728(85)90094-5
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发表时间：
1985-01-01
期刊：
影响因子：
--
通讯作者：
MEYER, TE
中科院分区：
文献类型：
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作者：
MEYER, TE
一种细胞色素c-551和一对高氧化还原势铁氧化还蛋白(等高势铁S蛋白)是盐生外硫杆菌的主要可溶性电子传递蛋白。细菌铁还蛋白和细胞色素c‘’的含量也较低。除细胞色素c-551外，这些蛋白在色素科的紫色S细菌中普遍存在，在红螺科的紫色细菌中较少出现。除了细胞色素和铁氧还蛋白，嗜盐乳杆菌还合成了大量的黄色小蛋白，它的发色团光谱上类似于黄素，取代了8-甲基，如玫瑰黄素和产甲烷辅因子F-420，具有O2、N2或S取代基。一个紫色的蛋白质只得到了部分纯化，但它在光谱上与具有酪氨酸配体的铁蛋白相似，如转铁蛋白、儿茶酸双加氧酶，尤其是紫色酸性磷酸酶。以前在光养细菌中显然没有观察到黄色蛋白质或紫色蛋白质，但在某种程度上，它们可能是在极端嗜盐的生境中生存所必需的。包括嗜盐菌在内的嗜盐菌的唯一共同特征是它们的蛋白质具有非常酸性的性质。
A cytochrome c-551 and a pair of high redox-potential ferredoxins (iso-high-potential Fe-S proteins) were found to be the major soluble electron-transport proteins in Ectothiorhodospira halophila. Smaller amounts of bacterial ferredoxin and cytochrome c'' were also observed. With the exception of cytochrome c-551, these proteins are commonly encountered in the purple S bacteria, family Chromatiaceae and less frequently in the purple bacteria, family Rhodospirillaceae. In addition to the cytochromes and ferredoxins, E. halophila synthesizes substantial amounts of a small yellow-colored protein, which has a chromophore spectrally similar to flavins having O2, N2 or S substituents in place of the 8-methyl group such as roseoflavin and the methanogen cofactor F-420. A purple-colored protein was only partially purified, but it is spectrally similar to Fe proteins having a tyrosine ligand, such as transferrin, catechuate dioxygenase and especially the purple acid phosphatases. Neither the yellow protein nor the purple one was apparently previously observed in phototrophic bacteria, but may in some way be required for survival in extremely halophilic habitats. The only feature common to halophiles including E. halophila is the very acidic nature of their proteins.