163894-42-6Relevant articles and documents
Models for α-keto acid-dependent non-heme iron enzymes: Structures and reactivity of [FeIICL(O2CCOPh)](ClO4) complexes
Chiou, Yu-Min,Que Jr., Lawrence
, p. 3999 - 4013 (2007/10/02)
The first iron(II)-α-ketocarboxylate complexes were synthesized with the use of tetradentate tripodal ligands tris[(6-methyl-2-pyridyl)methyl]amine (6TLA) and tris(2-pyridylmethyl)amine (TPA) and benzoylformate (BF) as the α-keto acid to model the putative iron-cofactor interaction in the active site of α-keto acid-dependent non-heme iron enzymes. [FeII(6TLA)(BF)](ClO4) (1) crystallizes in the triclinic system, space group P1 (no. 2) with cell constants a = 8.931(6) A?, b = 13.366(7) A?, c = 15.160(7) A?, α= 75.92(4)°, β = 81.06(5)°, γ = 70.78(5)°, V = 1652(4) A?3, and Z = 2; R = 0.071 and Rw = 0.082. [FeIIHTPA)(BF)(MeOH)](ClO4)·MeOH (2·MeOH) crystallizes in the orthorhombic system, space group Pca21 (no. 29) with cell constants a = 19.875(6) A?, b = 8.916(4) A?, c = 18.02(1) A?, V= 3193(4) A?3, and Z = 4; R = 0.054 and Rw = 0.056. The BF ligand chelates to the iron in 1 via one carboxylate oxygen and the carbonyl oxygen, but binds to the iron in 2 only through a carboxylate oxygen, with a methanol solvate occupying the other site. Both complexes react with dioxygen and quantitatively convert to decarboxylated complexes [FeII(6TLA)(OBz)]+ (5) and [FeII2O(TPA)2(OBz)2]2+ (6), respectively. Both 1 and 2 react with substrates 2,4-di-tert-butylphenol and triphenylphosphine under an O2 atmosphere to afford the corresponding biphenol and OPPh3, respectively. 18O2-labeling experiments show incorporation of one 18O atom into the respective benzoate products and one into the OPPh3. Kinetic studies on a series of [FeII(6TLA)(X-BF)](ClO4) complexes show pseudo-first-order disappearance of their characteristic color in the presence of excess dioxygen. The rate of the oxidative decarboxylation is sensitive to the nature of the phenyl substituent, exhibiting a Hammett ρ value of +1.07 which indicates a nucleophilic mechanism. A reaction mechanism is proposed consisting of dioxygen binding to the iron(II) center, forming an iron(III)-superoxide species, attack of the nascent superoxide on the BF keto carbon, oxidative decarboxylation affording the oxidizing species, and substrate oxidation. Complexes 1 and 2 represent the first structural and functional models for α-keto acid-dependent non-heme iron enzymes.