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Ferric Reductase Activity of the ArsH Protein from Acidithiobacillus Ferrooxidans

Author: MoHongYu
Tutor: ZengJia
School: Central South University
Course: Biological Engineering
Keywords: Acidophilic Thiobacillus ferrooxidans ArsH Flavodoxin reductase Ferric reductase
CLC: Q936
Type: Master's thesis
Year: 2011
Downloads: 31
Quote: 0
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Abstract


The prevalence of arsenic resistance genes in bacteria and fungi , the study found four arsenic resistance gene ( arsB arsC acidophilic Thiobacillus thiooxidans , arsR and arsH ) , the first three of the functions of genes and their respective anti- arsenic mechanisms have been elaborated , however , arsH (?) the biological function of the gene was not clear . In order to study the function of the gene , the cloned from A. ferrooxidans bacteria arsH ( ? ) Gene expression in Escherichia coli by step affinity chromatography purified from acidophilic Thiobacillus ferrooxidans ArsH protein , the expression of the protein molecular weight 28KDa, containing FMN is a dependent on NADPH flavoprotein oxidoreductase , and we reported for the first time comes from acidophilic Thiobacillus ferrooxidans ArsH protein showed high iron reductase activity, was constructed by site-directed mutagenesis techniques protein mutants of ArsH , E104A , E104D , E104Q . By UV - visible scanning and activity assays confirmed that the glutamic acid residue 104 is required for maintaining the stability of FMN cofactors . ArsH protein in bacteria may play an important role in the metabolism of iron .

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CLC: > Biological Sciences > Microbiology > Microbial biochemistry
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