Hase T, Wakabayashi S, Matsubara H, Evans M C, Jennings J V
J Biochem. 1978 May;83(5):1321-5. doi: 10.1093/oxfordjournals.jbchem.a132039.
We have determined the amino acid sequence of a ferredoxin from a photosynthetic green sulfur bacterium, Chlorobium thiosulfatophilum strain Tassajara. It contains 61 amino acid residues with 9 cysteines, and 8 of the 9 were located at positions corresponding to those in clostridial-type ferredoxins. Other structural features were closer to those of ferredoxins from another photosynthetic bacterium, C. limicola, than to those of non-photosynthetic bacteria. Compared with ferredoxin from Chromatium, a photosynthetic purple sulfur bacterium, all photosynthetic bacterial ferredoxins have a common region in the carboxyl-terminal half with several extra residues and a unique cysteine residue. We compared all the photosynthetic bacterial ferredoxins that have been sequenced and concluded that C. thiosulfatophilum ferredoxin is most closely related to C. limicola ferredoxin I.
我们已经确定了来自光合绿色硫细菌嗜硫绿菌属塔萨加拉菌株的一种铁氧化还原蛋白的氨基酸序列。它含有61个氨基酸残基和9个半胱氨酸,其中9个中的8个位于与梭菌型铁氧化还原蛋白中相应位置。与非光合细菌的铁氧化还原蛋白相比,其他结构特征更接近另一种光合细菌嗜硫栖热菌的铁氧化还原蛋白。与光合紫色硫细菌嗜硫红假单胞菌的铁氧化还原蛋白相比,所有光合细菌的铁氧化还原蛋白在羧基末端的一半都有一个共同区域,带有几个额外的残基和一个独特的半胱氨酸残基。我们比较了所有已测序的光合细菌铁氧化还原蛋白,得出结论:嗜硫绿菌的铁氧化还原蛋白与嗜硫栖热菌铁氧化还原蛋白I关系最为密切。