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Research article

J. Microbiol. Biotechnol. 2011; 21(5): 464-469

Published online May 28, 2011 https://doi.org/10.4014/jmb.1101.01020

Copyright © The Korean Society for Microbiology and Biotechnology.

Ferric Reductase Activity of the ArsH Protein from Acidithiobacillus ferrooxidans

Hongyu Mo 1, 2, Qian Chen 1, 2, Juan Du 1, Lin Tang 1, Fang Qin 1, Bo Miao 2, Xueling Wu 2 and Jia Zeng 1, 2*

1College of Biology, Hunan University, Changsha, Hunan 410082, P. R. China, 2Department of Bioengineering, Central South University, Changsha, Hunan 410083, P. R. China

Received: January 14, 2011; Accepted: March 10, 2011

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.

Keywords: Acidithiobacillus ferrooxidans, ArsH, Flavoprotein, Ferric reductase