Wakabayashi S, Hase T, Wada K, Matsubara H, Suzuki K, Takaichi S
J Biochem. 1978 May;83(5):1305-19. doi: 10.1093/oxfordjournals.jbchem.a132038.
The amino acid sequences of two ferredoxins isolated from pokeweed, Phytolacca americana, were determined. Tryptic peptides of maleyl-carboxymethyl-ferredoxin I and carboxymethyl-ferredoxin II were prepared and analyzed. The large peptides were further digested with staphylococcal protease and chymotrypsin. Ferredoxins I and II were composed of 96 and 98 amino acid residues, respectively. Though ferredoxin I lacks tryptophan and methionine, ferredoxin II contains both of them. In a comparison of the amino acid sequences with those of other higher plant ferredoxins, ferredoxin I is one residue shorter than others at the carboxyl-terminus and ferredoxin II one longer than others at the amino-terminus. Ferredoxins I and II differ in 23 sites from each other and in 27 to 37 sites from other higher plant ferredoxins. This suggests that duplication of the ferredoxin gene occurred after the divergence of pokeweed from other higher plants. A phylogenetic tree including all other ferredoxins was constructed.
测定了从美洲商陆（Phytolacca americana）中分离出的两种铁氧化还原蛋白的氨基酸序列。制备并分析了马来酰 - 羧甲基 - 铁氧化还原蛋白I和羧甲基 - 铁氧化还原蛋白II的胰蛋白酶肽段。将大的肽段进一步用葡萄球菌蛋白酶和胰凝乳蛋白酶消化。铁氧化还原蛋白I和II分别由96和98个氨基酸残基组成。虽然铁氧化还原蛋白I缺乏色氨酸和甲硫氨酸，但铁氧化还原蛋白II同时含有这两种氨基酸。在将氨基酸序列与其他高等植物铁氧化还原蛋白的序列进行比较时，铁氧化还原蛋白I在羧基末端比其他蛋白短一个残基，而铁氧化还原蛋白II在氨基末端比其他蛋白长一个残基。铁氧化还原蛋白I和II在23个位点彼此不同，与其他高等植物铁氧化还原蛋白在27至37个位点不同。这表明铁氧化还原蛋白基因的复制发生在商陆与其他高等植物分化之后。构建了包含所有其他铁氧化还原蛋白的系统发育树。
