Abreu Isabel A, Xavier António V, LeGall Jean, Cabelli Diane E, Teixeira Miguel
Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Rua da Quinta Grande 6, 2780-156 Oeiras, Portugal.
J Biol Inorg Chem. 2002 Jun;7(6):668-74. doi: 10.1007/s00775-002-0363-1. Epub 2002 Apr 18.
A superfamily of mononuclear iron proteins, originally named desulfoferrodoxin and neelaredoxin, has been identified by in vivo and in vitro studies as scavengers of the superoxide anion radical. These proteins, whose genes are present in all the so-far known genomes from anaerobes and in the microaerophilic pathogen Treponema pallidum, show not only a considerable amino acid sequence identity but, most importantly, a common active iron site, Fe[His(4)CysGlu], in the oxidized state which loses the glutamate ligand in the reduced form. The experimental evidence for the activity of these proteins as superoxide dismutases or as donor:superoxide oxidoreductases is discussed in this Commentary, giving particular emphasis to the neelaredoxin from the hyperthermophilic archaeon Archaeoglobus fulgidus.
一类单核铁蛋白超家族，最初被命名为脱硫铁氧化还原蛋白和尼尔拉氧化还原蛋白，通过体内和体外研究已被鉴定为超氧阴离子自由基的清除剂。这些蛋白质的基因存在于所有迄今已知的厌氧菌基因组以及微需氧病原体梅毒螺旋体的基因组中，它们不仅显示出相当高的氨基酸序列同一性，而且最重要的是，在氧化态下有一个共同的活性铁位点Fe[His(4)CysGlu]，在还原态时会失去谷氨酸配体。本述评讨论了这些蛋白质作为超氧化物歧化酶或作为供体：超氧化物氧化还原酶活性的实验证据，特别强调了嗜热古菌嗜热栖热袍菌中的尼尔拉氧化还原蛋白。
