Superoxide dismutases: ancient enzymes and new insights.
Superoxide dismutases: ancient enzymes and new insights.
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DOI：
10.1016/j.febslet.2011.10.048
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发表时间：
2012-03-09
期刊：
影响因子：
3.5
通讯作者：
Miller AF
中科院分区：
文献类型：
--
作者：
Miller AF
超氧化物歧化酶（SOD）催化超氧化物的失活。因此，随着含氧光合作用的进化，O2 变得普遍，SOD 变得非常重要。因此，SOD 的三种形式为了解当今携带它们的生物体和细胞器的进化提供了有趣的见解。尽管古代生物体使用依赖铁的 SOD，但环境的氧化使铁的生物利用度降低，并且更加危险。事实上，现代谱系更多地利用同源的锰依赖性 SOD。我们对大肠杆菌 Fe 取代的 MnSOD 以及大肠杆菌 FeSOD 氧化还原调节的研究揭示了进化如何适应 Fe 和 Mn 之间可能影响 SOD 性能的差异，在 SOD 蛋白中，其活性对一种或其他金属离子具有特异性。
Superoxide dismutases (SODs) catalyze the de-activation of superoxide. SODs therefore acquired great importance as O2 became prevalent following the evolution of oxygenic photosynthesis. Thus the three forms of SOD provide intriguing insights into the evolution of the organisms and organelles that carry them today. Although ancient organisms employed Fe-dependent SODs, oxidation of the environment made Fe less bio-available, and more dangerous. Indeed, modern lineages make greater use of homologous Mn-dependent SODs. Our studies on the Fe-substituted MnSOD of Escherichia coli, as well as redox tuning in the FeSOD of E. coli shed light on how evolution accommodated differences between Fe and Mn that could affect SOD performance, in SOD proteins whose activity is specific to one or other metal ion.