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嗜酸氧化亚铁硫杆菌 ArsH 蛋白的铁还原酶活性。

Ferric reductase activity of the ArsH protein from Acidithiobacillus ferrooxidans.

机构信息

College of Biology, Hunan University, Changsha, Hunan, P. R. China.

出版信息

J Microbiol Biotechnol. 2011 May;21(5):464-9. doi: 10.4014/jmb.1101.01020.

Abstract

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. Glu104 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.

摘要

arsH 基因是细菌和真核生物砷抗性系统的一种。ArsH 蛋白被注释为 NADPH 依赖的黄素单核苷酸(FMN)还原酶,但具有未知的生物学功能。在这里,我们首次报道 ArsH 蛋白表现出高的三价铁还原酶活性。Glu104 是维持 FMN 辅因子稳定性的必需残基。ArsH 蛋白可能在体内细胞质三价铁同化中发挥重要作用。

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