Iron and proteins for iron storage and detoxification
Iron and proteins for iron storage and detoxification
复制标题
DOI：
10.1023/b:biom.0000027692.24395.76
复制
发表时间：
2004-06-01
期刊：
影响因子：
3.5
通讯作者：
Stefanini, S
中科院分区：
文献类型：
--
作者：
Chiancone, E;Ceci, P;Stefanini, S
铁是大多数生物体所需要的，但由于稳定氧化态Fe（III）的低溶解度以及增强活性氧物质ROS的产生的倾向，铁是潜在有毒的。细菌采用与宿主相同的策略来抵消铁的反应性，即通过将金属螯合到铁蛋白（普遍存在的铁储存蛋白）中。铁蛋白是一种高度保守的中空球蛋白，由24个亚基组成，具有铁氧化酶活性，可以容纳多达4500个铁原子作为羟基氧化物胶束。还原时金属的释放可以改变微生物-宿主铁平衡，从而允许细菌克服铁限制。在细菌中，Dps（来自饥饿细胞的DNA结合蛋白）家族在铁储存-解毒中的相关性最近已被认识到。对来自无害李斯特菌的蛋白质的开创性研究表明，Dps蛋白具有铁蛋白样活性，最重要的是具有减弱ROS产生的能力。后一种功能允许缺乏过氧化氢酶的细菌病原体，例如。G.牙龈卟啉单胞菌，在有氧环境中生存，并抵抗过氧化应激。
Iron is required by most organisms, but is potentially toxic due to the low solubility of the stable oxidation state, Fe(III), and to the tendency to potentiate the production of reactive oxygen species, ROS. The reactivity of iron is counteracted by bacteria with the same strategies employed by the host, namely by sequestering the metal into ferritin, the ubiquitous iron storage protein. Ferritins are highly conserved, hollow spheres constructed from 24 subunits that are endowed with ferroxidase activity and can harbour up to 4500 iron atoms as oxy-hydroxide micelles. The release of the metal upon reduction can alter the microorganism-host iron balance and hence permit bacteria to overcome iron limitation. In bacteria, the relevance of the Dps (DNA-binding proteins from starved cells) family in iron storage-detoxification has been recognized recently. The seminal studies on the protein from Listeria innocua demonstrated that Dps proteins have ferritin-like activity and most importantly have the capacity to attenuate the production of ROS. This latter function allows bacterial pathogens that lack catalase, e. g. Porphyromonas gingivalis, to survive in an aerobic environment and resist to peroxide stress.