Inhibiting Escherichia coli cytochrome c nitrite reductase:: voltammetry reveals an enzyme equipped for action despite the chemical challenges it may face in vivo

被引:9
|
作者
Gwyer, JD
Richardson, DJ
Butt, JN [1 ]
机构
[1] Univ E Anglia, Sch Chem Sci & Pharm, Ctr Met Prot Spect & Biol, Norwich NR4 7TJ, Norfolk, England
[2] Univ E Anglia, Sch Biol Sci, Ctr Met Prot Spect & Biol, Norwich NR4 7TJ, Norfolk, England
基金
英国生物技术与生命科学研究理事会;
关键词
cytochrome c nitrite reductase; Escherichia coli; haem; inhibitor of cytochrome c; nitrite reductase; protein film voltammetry;
D O I
10.1042/BST0340133
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:133 / 135
页数:3
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