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红螺菌胞外铁氧化还原蛋白的结构:与梭菌铁氧化还原蛋白高度相似。

Structure of the extracellular ferredoxin from Rhodospirillum rubrum: close similarity to clostridial ferredoxins.

作者信息

Matsubara H, Inoue K, Hase T, Hiura H, Kakuno T, Yamashita J, Horio T

出版信息

J Biochem. 1983 May;93(5):1385-90. doi: 10.1093/oxfordjournals.jbchem.a134273.

Abstract

The amino acid sequence of an [8Fe-8S] ferredoxin isolated from the culture medium of Rhodospirillum rubrum, a photosynthetic purple non-sulfur bacterium, was determined by a combination of various conventional procedures. The sequence was A-Y-K-I-E-E-T-C-I-S-C-G-A-C-A-A-E-C-P-V-N-A-I-E-Q-G-D-T-I-F-V-V-N-A-D-T-C-I-D-C - G-N-C-A-N-V-C-P-V-G-A-P-V-A-E (55 amino acid residues). It lacked methionine, leucine, histidine, arginine, and tryptophan. The molecular weight was calculated to be 5,568 excluding iron and sulfur atoms. The distribution of 8 cysteine residues was exactly the same as that of clostridial-type ferredoxin, suggesting retention of the duplication of the bacterial ancestral ferredoxin gene. The extracellular ferredoxin of R. rubrum was compared with other ferredoxins observed in closely related photosynthetic bacteria and the evolutionary significance of this ferredoxin is discussed.

摘要

通过多种传统方法相结合,确定了从光合紫色非硫细菌红螺菌培养基中分离出的一种[8Fe-8S]铁氧化还原蛋白的氨基酸序列。该序列为A-Y-K-I-E-E-T-C-I-S-C-G-A-C-A-A-E-C-P-V-N-A-I-E-Q-G-D-T-I-F-V-V-N-A-D-T-C-I-D-C - G-N-C-A-N-V-C-P-V-G-A-P-V-A-E(55个氨基酸残基)。它不含甲硫氨酸、亮氨酸、组氨酸、精氨酸和色氨酸。计算出的分子量(不包括铁和硫原子)为5568。8个半胱氨酸残基的分布与梭菌型铁氧化还原蛋白完全相同,这表明细菌祖先铁氧化还原蛋白基因的重复得以保留。将红螺菌的细胞外铁氧化还原蛋白与在密切相关的光合细菌中观察到的其他铁氧化还原蛋白进行了比较,并讨论了这种铁氧化还原蛋白的进化意义。

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