Berndt Carsten, Christ Loïck, Rouhier Nicolas, Mühlenhoff Ulrich
Department of Neurology, Medical Faculty, Heinrich-Heine University, Merowingerplatz1a, 40225 Düsseldorf, Germany.
Université de Lorraine, INRAE, IAM, F-54000 Nancy, France.
Biochim Biophys Acta Bioenerg. 2021 Jan 1;1862(1):148317. doi: 10.1016/j.bbabio.2020.148317. Epub 2020 Sep 24.
Among the thioredoxin superfamily of proteins, the observation that numerous glutaredoxins bind iron-sulphur (Fe/S) clusters is one of the more recent and major developments concerning their functional properties. Glutaredoxins are present in most organisms. All members of the class II subfamily (including most monothiol glutaredoxins), but also some members of the class I (mostly dithiol glutaredoxins) and class III (land plant-specific monothiol or dithiol glutaredoxins) are Fe/S proteins. In glutaredoxins characterised so far, the [2Fe2S] cluster is coordinated by two active-site cysteine residues and two molecules of non-covalently bound glutathione in homo-dimeric complexes bridged by the cluster. In contrast to dithiol glutaredoxins, monothiol glutaredoxins possess no or very little oxidoreductase activity, but have emerged as important players in cellular iron metabolism. In this review we summarise the recent developments of the most prominent Fe/S glutaredoxins in eukaryotes, the mitochondrial single domain monothiol glutaredoxin 5, the chloroplastic single domain monothiol glutaredoxin S14 and S16, the nuclear/cytosolic multi-domain monothiol glutaredoxin 3, and the mitochondrial/cytosolic dithiol glutaredoxin 2.
在硫氧还蛋白超家族中，众多谷氧还蛋白能结合铁硫（Fe/S）簇这一发现是有关其功能特性的最新重大进展之一。谷氧还蛋白存在于大多数生物体中。II类亚家族的所有成员（包括大多数单硫醇谷氧还蛋白），以及I类（大多为双硫醇谷氧还蛋白）和III类（陆地植物特有的单硫醇或双硫醇谷氧还蛋白）的一些成员都是Fe/S蛋白。在目前已表征的谷氧还蛋白中，[2Fe2S]簇由两个活性位点半胱氨酸残基和两个非共价结合的谷胱甘肽分子配位，形成由该簇桥接的同二聚体复合物。与双硫醇谷氧还蛋白不同，单硫醇谷氧还蛋白没有或只有很少的氧化还原酶活性，但已成为细胞铁代谢中的重要参与者。在本综述中，我们总结了真核生物中最突出的Fe/S谷氧还蛋白的最新进展，包括线粒体单结构域单硫醇谷氧还蛋白5、叶绿体单结构域单硫醇谷氧还蛋白S14和S16、核/胞质多结构域单硫醇谷氧还蛋白3以及线粒体/胞质双硫醇谷氧还蛋白2。
