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− | + | <p>The second section in the perchlorate-reducing pathway in biological systems involves the degradation of the chlorite ion substrate. The isolated chlorite dismutase (Cld) enzyme from Ideonella dechloratans is capable of the metabolic breakdown of chlorite ion to oxygen gas and chloride ions. The characterized gene sequence of Cld is the basis for construction of our g-blocks, Cld+sp (plus signal peptide) and Cld-sp (minus signal peptide). Our study of Escherichia coli cells in a highly concentrated chlorite ion media reveals their extreme sensitivity to the strong oxidizing agent [insert source # here]. In an attempt to minimize intracellular damage, a periplasmic signal peptide is included in Cld+sp for the immediate degradation of the chlorite ion substrate before it could cross the inner plasma membrane. A comparison between the efficiency of Cld+sp and Cld-sp at oxygen production is discussed in a subsequent report</p> | |
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Revision as of 23:04, 16 October 2016
The second section in the perchlorate-reducing pathway in biological systems involves the degradation of the chlorite ion substrate. The isolated chlorite dismutase (Cld) enzyme from Ideonella dechloratans is capable of the metabolic breakdown of chlorite ion to oxygen gas and chloride ions. The characterized gene sequence of Cld is the basis for construction of our g-blocks, Cld+sp (plus signal peptide) and Cld-sp (minus signal peptide). Our study of Escherichia coli cells in a highly concentrated chlorite ion media reveals their extreme sensitivity to the strong oxidizing agent [insert source # here]. In an attempt to minimize intracellular damage, a periplasmic signal peptide is included in Cld+sp for the immediate degradation of the chlorite ion substrate before it could cross the inner plasma membrane. A comparison between the efficiency of Cld+sp and Cld-sp at oxygen production is discussed in a subsequent report