原核微生物铁超氧化物歧化酶的分子进化

Molecular Evolution of Fe-SOD from Prokaryotic Microorganisms

超氧化物歧化酶(superoxide dismutase,SOD)在维持生物体内超氧阴离子自由基产生与消除的动态平衡中起着重要的作用。铁超氧化物歧化酶(Fe-SOD)是原核生物和真核生物细胞器中专一的SOD酶,通过GenBank中搜集的原核生物Fe-SOD进行比对分析发现,Fe-SOD是相对保守的蛋白质,其中包含2个保守区域和1个可变区域,金属结合位点固定,Fe-SOD序列的比对可以反映物种间的进化关系,是研究原核生物分子进化的理想素材。

SOD （superoxide dismutase） plays an important role in the balance between the production and the elimi- nation of superoxide anion free radical, Fe-SOD is a specific SOD enzyme in organelle of eukaryotic and prokaryotic organisms; It was found through comparison and analysis of eukaryotic Fe-SODs collected through GenBank that Fe- SODs are relatively conservative proteins, included 2 conservative domains and one variable domain with the fixed metal-linking site. Fe-SODs＇ sequence comparison could reflect the evolution relation among species, and they are an ideal source material to study the biomolecular evolution of prokaryotic of organisms.