Active-site models of bacterial nitric oxide reductase featuring tris-histidyl and glutamic acid mimics: influence of a carboxylate ligand on Fe(B) binding and the heme Fe/Fe(B) redox potential.
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 Fe(B) retention in the distal binding site and proper modulation of the redox potentials of both the heme and non-heme Fe's.
Collman
James P
JP
Department of Chemistry, Stanford University, Stanford, California 94305-5080, USA. jpc@stanford.edu
Yan
Yi-Long
YL
Lei
Jianping
J
Dinolfo
Peter H
PH
D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism; D001665:Binding Sites; D040761:Biomimetic Materials / Q000737:chemistry / Q000378:metabolism*; D002264:Carboxylic Acids / Q000378:metabolism*; D018698:Glutamic Acid / Q000737:chemistry*; D006418:Heme / Q000737:chemistry / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007093:Imidazoles / Q000737:chemistry*; D007501:Iron / Q000737:chemistry / Q000378:metabolism*; D008024:Ligands; D008665:Metalloporphyrins / Q000737:chemistry*; D008958:Models, Molecular; D015394:Molecular Structure; D010084:Oxidation-Reduction; D010088:Oxidoreductases / Q000737:chemistry / Q000378:metabolism*
D001426:Bacterial Proteins; D002264:Carboxylic Acids; D007093:Imidazoles; D008024:Ligands; D008665:Metalloporphyrins; D018698:Glutamic Acid; D006418:Heme; D007501:Iron; D010088:Oxidoreductases; C034747:nitric-oxide reductase