PMID:16417502

Citation	Gwyer, JD, Richardson, DJ and Butt, JN (2006) Inhibiting Escherichia coli cytochrome c nitrite reductase: voltammetry reveals an enzyme equipped for action despite the chemical challenges it may face in vivo. Biochem. Soc. Trans. 34:133-5
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.
Links	PubMed Online version:10.1042/BST0340133
Keywords	Binding Sites; Cytochromes a1/antagonists & inhibitors; Cytochromes a1/genetics; Cytochromes a1/metabolism; Cytochromes c1/antagonists & inhibitors; Cytochromes c1/genetics; Cytochromes c1/metabolism; Escherichia coli/enzymology; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Humans; Nitrate Reductases/antagonists & inhibitors; Nitrate Reductases/genetics; Nitrate Reductases/metabolism; Nitrites/metabolism; Oxidation-Reduction; Potentiometry
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