ABSTRACT
Escherichia coli cytochrome c nitrite reductase is one of a large family of homologous enzymes that are particularly prevalent in pathogenic enterobacteria. The enzymes are periplasmic and in vivo may find themselves challenged by molecules that could enhance or compromise their performance. In the present study, we describe protein film voltammetry in which the activity of E. coli cytochrome c nitrite reductase is challenged by the presence of a number of small molecules. These results are discussed in light of the environment(s) that the enzyme may face before and after colonization of a human host.
Subject(s)
Cytochromes a1/metabolism , Cytochromes c1/metabolism , Escherichia coli Proteins/metabolism , Escherichia coli/enzymology , Nitrate Reductases/metabolism , Binding Sites , Cytochromes a1/antagonists & inhibitors , Cytochromes a1/genetics , Cytochromes c1/antagonists & inhibitors , Cytochromes c1/genetics , Escherichia coli Proteins/genetics , Humans , Nitrate Reductases/antagonists & inhibitors , Nitrate Reductases/genetics , Nitrites/metabolism , Oxidation-Reduction , PotentiometryABSTRACT
The recent structural characterization of the NrfA from Escherichia coli provides a framework to rationalize the spectroscopic and functional properties of this enzyme. Analyses by EPR and magnetic CD spectroscopies have been complemented by protein-film voltammetry and these are discussed in relation to the essential structural features of the enzyme.