Ferric Reductase Activity of the ArsH Protein from Acidithiobacillus ferrooxidans
Ferric Reductase Activity of the ArsH Protein from Acidithiobacillus ferrooxidans
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氧化亚铁硫杆菌 ArsH 蛋白的三价铁还原酶活性
DOI：
10.4014/jmb.1101.01020
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发表时间：
2011-05-01
影响因子：
2.8
通讯作者：
Zeng, Jia
中科院分区：
文献类型：
--
作者：
Mo Hongyu;Chen, Qian;Zeng, Jia
arsH基因是细菌和真核生物抗砷系统之一。ArsH蛋白被注释为具有未知生物学功能的NADPH依赖性黄素单核苷酸（FMN）还原酶。在这里，我们报告的第一次，ArsH蛋白表现出较高的铁还原酶活性。G1u104是维持FMN辅因子稳定性的重要残基。ArsH蛋白可能在体内细胞溶质三价铁同化中发挥重要作用。
The arsH gene is one of the arsenic resistance system in bacteria and eukaryotes. The ArsH protein was annotated as a NADPH-dependent flavin mononucleotide (FMN) reductase with unknown biological function. Here we report for the first time that the ArsH protein showed high ferric reductase activity. G1u104 was an essential residue for maintaining the stability of the FMN cofactor. The ArsH protein may perform an important role for cytosolic ferric iron assimilation in vivo.