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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
journal contribution
posted on 2006-09-18, 00:00 authored by James P. Collman, Yi-Long Yan, Jianping Lei, Peter H. DinolfoActive-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.