The prototypic class Ia ribonucleotide reductase from Escherichia coli: still surprising after all these years
The prototypic class Ia ribonucleotide reductase from Escherichia coli: still surprising after all these years
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DOI：
10.1042/bst20120081
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发表时间：
2012-06-01
影响因子：
3.9
通讯作者：
Drennan, Catherine L.
中科院分区：
文献类型：
--
作者：
Brignole, Edward J.;Ando, Nozomi;Drennan, Catherine L.
RNR（核糖核苷酸还原酶）是核酸代谢中的关键角色，可将核糖核苷酸转化为脱氧核糖核苷酸。因此，它们维持细胞内脱氧核糖核苷酸的平衡，以确保 DNA 复制和修复的保真度。研究最充分的 RNR 是来自大肠杆菌的 Ia 类酶，它采用两个亚基来催化其基于自由基的反应：β(2) 包含二铁酪氨酰自由基辅助因子，α(2) 包含活性位点。最近应用生物物理方法研究这种 RNR，揭示了寡聚状态对整体酶活性的重要性，并表明前所未有的亚基构型正在发挥作用。尽管从大肠杆菌提取物中分离出核苷酸还原酶活性已经过去了 50 年，但这种典型的 RNR 多年来仍然让我们感到惊讶。
RNRs (ribonucleotide reductases) are key players in nucleic acid metabolism, converting ribonucleotides into deoxyribonucleotides. As such, they maintain the intracellular balance of deoxyribonucleotides to ensure the fidelity of DNA replication and repair. The best-studied RNR is the class Ia enzyme from Escherichia coli, which employs two subunits to catalyse its radical-based reaction: beta(2) houses the diferric-tyrosyl radical cofactor, and alpha(2) contains the active site. Recent applications of biophysical methods to the study of this RNR have revealed the importance of oligomeric state to overall enzyme activity and suggest that unprecedented subunit configurations are in play. Although it has been five decades since the isolation of nucleotide reductase activity in extracts of E. coli, this prototypical RNR continues to surprise us after all these years.