Active-site models of bacterial nitric oxide reductase featuring tris-histidyl and glutamic acid mimics:: Influence of a carboxylate ligand on FeB binding and the heme Fe/FeB redox potential

被引：26
作者：
Collman, James P. [1 ]
Yan, Yi-Long [1 ]
Lei, Jianping [1 ]
Dinolfo, Peter H. [1 ]
机构：
[1] Stanford Univ, Dept Chem, Stanford, CA 94305 USA
来源：
INORGANIC CHEMISTRY | 2006年 / 45卷 / 19期
关键词：
D O I：
10.1021/ic0609150
中图分类号：
O61 [无机化学];
学科分类号：
070301 ; 081704 ;
摘要：
Active-site models of bacterial nitric oxide reductase (NOR) featuring a heme Fe and a trisimidazole- and glutaric acid-bound non-heme Fe (Fe-B) have been synthesized. These models closely replicate the proposed active site of native NORs. Examination of these models shows that the glutamic acid mimic is required for both FeB retention in the distal binding site and proper modulation of the redox potentials of both the heme and non-heme Fe's.
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收藏
页码：7581 / 7583
页数：3
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