来自极端嗜盐菌——死海嗜盐杆菌的2Fe-2S铁氧化还原蛋白的氨基酸序列。

Amino acid sequence of 2Fe-2S ferredoxin from an extreme halophile, Halobacterium of the Dead Sea.

作者信息

Hase T, Wakabayashi S, Matsubara H, Mevarech M, Werber M M

出版信息

Biochim Biophys Acta. 1980 May 29;623(1):139-45. doi: 10.1016/0005-2795(80)90016-1.

Abstract

The primary structure of the 2Fe-2S ferredoxin from Halobacterium of the Dead Sea was determined and it consisted of 128 amino acid residues including an N epsilon-acetyllysyl residue. Due to a high degree of sequence homology between this ferredoxin and the one from Halobacterium halobium, all tryptic peptides could be aligned in order. Only 20 amino acid differences were observed between these two halobacterial ferredoxins. The distribution of cysteinyl residues involved in the iron chelation was similar to that of chloroplast-type ferredoxins.

摘要

测定了死海嗜盐杆菌2Fe-2S铁氧化还原蛋白的一级结构，它由128个氨基酸残基组成，包括一个Nε-乙酰赖氨酰残基。由于这种铁氧化还原蛋白与嗜盐栖嗜盐杆菌的铁氧化还原蛋白之间存在高度的序列同源性，所有胰蛋白酶肽段都可以依次排列。这两种嗜盐杆菌铁氧化还原蛋白之间仅观察到20个氨基酸差异。参与铁螯合的半胱氨酰残基的分布与叶绿体型铁氧化还原蛋白相似。