Class I ribonucleotide reductases: metallocofactor assembly and repair in vitro and in vivo.
Class I ribonucleotide reductases: metallocofactor assembly and repair in vitro and in vivo.
复制标题
I类核糖核苷酸还原酶：金属生物活性剂组装和体外修复。
DOI：
10.1146/annurev-biochem-061408-095817
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发表时间：
2011
影响因子：
16.6
通讯作者：
Stubbe J
中科院分区：
文献类型：
--
作者：
Cotruvo JA;Stubbe J
许多酶的活性所必需的金属辅助因子的结合是翻译后修饰的主要机制。在单核和双核非血红素铁和锰辅助因子的情况下，这些过程所需的细胞机制在很大程度上仍然难以捉摸。此外，许多金属辅助因子可以转化为非活性形式，它们的修复途径最近才被发现。I类核糖核苷酸还原酶（RNRs）催化核苷酸向脱氧核苷酸的转化，并需要双核金属簇的活性：一个feiiiiiii -酪氨酸自由基（Y•）辅助因子（Ia类），一个MnIIIMnIII-Y•辅助因子（Ib类）和一个MnIVFeIII辅助因子（Ic类）。Ia类、Ib类和Ic类rrna在结构上是同源的，并且含有几乎相同的金属配位位点。我们对这些RNRs的辅助因子在体外和体内产生的机制以及受损辅助因子的修复机制的最新进展，为了解大自然如何防止错金属化和协调高产量的活性团簇形成提供了见解。
Incorporation of metallocofactors essential for the activity of many enyzmes is a major mechanism of posttranslational modification. The cellular machinery required for these processes in the case of mono- and dinuclear nonheme iron and manganese cofactors has remained largely elusive. In addition, many metallocofactors can be converted to inactive forms, and pathways for their repair have recently come to light. The class I ribonucleotide reductases (RNRs) catalyze the conversion of nucleotides to deoxynucleotides and require dinuclear metal clusters for activity: an FeIIIFeIII-tyrosyl radical (Y•) cofactor (class Ia), a MnIIIMnIII-Y• cofactor (class Ib), and a MnIVFeIII cofactor (class Ic). The class Ia, Ib, and Ic RNRs are structurally homologous and contain almost identical metal coordination sites. Recent progress in our under-standing of the mechanisms by which the cofactor of each of these RNRs is generated in vitro and in vivo and by which the damaged cofactors are repaired is providing insight into how nature prevents mismetallation and orchestrates active cluster formation in high yields.