Self-assembly of the 2-His-1-carboxylate facial triad in mononuclear iron(II) and zinc(II) models of metalloenzyme active sites.
A synthetic strategy involving the use of sterically hindered N-donor and terphenylcarboxylate ligands has been used to prepare complexes of iron(II) and zinc(II) that feature N2(carboxylate) donors. X-ray crystallographic and NMR data show that the 2-His-1-carboxylate facial triad found in metalloenzyme active sites is closely modeled by the mononuclear complexes. In addition, by virtue of the flexibility of the ligands used, the geometries and coordination environments of the complexes display carboxylate binding mode differences such as those seen in the enzymes.
Friese
Seth J
SJ
Department of Chemistry and Center for Metals in Biocatalysis, University of Minnesota, 207 Pleasant Street SE, Minneapolis, Minnesota 55455, USA.
Kucera
Benjamin E
BE
Que
Lawrence
L
Tolman
William B
WB
D040761:Biomimetic Materials / Q000737:chemistry; D001708:Biopterins / Q000031:analogs & derivatives / Q000737:chemistry; D002264:Carboxylic Acids / Q000737:chemistry*; D018360:Crystallography, X-Ray; D005296:Ferrous Compounds / Q000737:chemistry*; D006639:Histidine / Q000031:analogs & derivatives* / Q000737:chemistry; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D010651:Phenylalanine Hydroxylase / Q000737:chemistry*; D015032:Zinc / Q000737:chemistry*
D002264:Carboxylic Acids; D005296:Ferrous Compounds; D001708:Biopterins; D006639:Histidine; D010651:Phenylalanine Hydroxylase; C003402:sapropterin; D015032:Zinc