%0 Journal Article
%A Collman, James P.
%A Yan, Yi-Long
%A Lei, Jianping
%A Dinolfo, Peter H.
%D 2006
%T 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
%U https://acs.figshare.com/articles/journal_contribution/Active_Site_Models_of_Bacterial_Nitric_Oxide_Reductase_Featuring_Tris_Histidyl_and_Glutamic_Acid_Mimics_Influence_of_a_Carboxylate_Ligand_on_Fe_sub_B_sub_Binding_and_the_Heme_Fe_Fe_sub_B_sub_Redox_Potential/3058894
%R 10.1021/ic0609150.s001
%2 https://acs.figshare.com/ndownloader/files/4764655
%K nitric oxide reductase
%K redox potentials
%K FeB Binding
%K heme Fe
%K FeB retention
%K Carboxylate Ligand
%K model
%K binding site
%K NOR
%X Active-site models of bacterial nitric oxide reductase (NOR)
featuring a heme Fe and a trisimidazole- and glutaric acid-bound
non-heme Fe (FeB) 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.
%I ACS Publications