Summary: Disruption of the gene for the periplasmic cytochrome c in did not result in substantial alteration of rates of electron flow from physiological substrates to the reductases for nitrite, nitric oxide and nitrous oxide, thus confirming and extending earlier findings. In wild-type cells the chelating agent diethyldithiocarbamate (DDC) caused a partial inhibition of these electron transport processes. When the same concentrations of this inhibitor were added to a mutant of in which the gene for cytochrome c was specifically disrupted an almost complete inhibition of these reactions was observed. It is known from previous work with the closely related organism that DDC effectively and rapidly removes copper from the periplasmic pseudoazurin that is also found in Therefore, it is concluded that in the absence of cytochrome c, a copper protein, probably pseudoazurin, acts as the electron carrier between the cytochrome complex and the reductases for nitrite, nitric oxide and nitrous oxide. Cells with the gene for cytochrome c deleted continued to give a positive Nadi test.


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