34557-72-7Relevant articles and documents
Linkage Isomers of 4-Methylimidazolate Mn(II) Porphyrinates: Hindered or Unhindered?
Zhao, Jianping,Qian, Fei,Guo, Wenping,Li, Jianfeng,Lin, Zeyuan
, p. 7465 - 7474 (2021/05/26)
Three different manganese(II) porphyrins have been exploited to react with 4-methylimidazolate (4-MeIm-), and the five-coordinate products are characterized by ultraviolet-visible, single-crystal X-ray, and electronic paramagnetic resonance spectroscopies. Interestingly, 4-MeIm- is found to bond to the metal center through either of the two N atoms (N1 or N3), which yielded two linkage isomers with either an unhindered or a hindered ligand conformation, respectively. Investigations revealed it is the large metal out-of-plane displacements (Δ24 and Δ4 ≥ 0.59 ?) that have rendered the equivalence of two isomers with a small energy difference (5.2-8.3 kJ/mol). The nonbonded intra- and intermolecular interactions thus become crucial factors in the balance of linkage isomerization. All of the products in both solution and solid states show the same characteristic resonances of high-spin Mn(II) (S = 5/2) with g⊥ ≈ 5.9 and g⊥ ≈ 2.0 at 4 K, consistent with the weak effects of the axial ligand on core conformation and metal electronic configurations. Zero-field splitting parameters obtained through simulations are also reported.
Method for synthesizing tetraaryl manganese porphyrin through synchronous aldehyde and pyrrole condensation and bivalent manganese salt oxidation insertion reaction
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Paragraph 0028-0029, (2020/09/08)
The invention discloses a method for synthesizing tetraaryl manganese porphyrin by synchronous aldehyde and pyrrole condensation and bivalent manganese salt oxidation insertion reaction. Aromatic aldehyde, pyrrole and manganese dichloride are refluxed in
Crystallographic identification of a series of manganese porphyrin complexes with nitrogenous bases
Lahanas, Nicole,Kucheryavy, Pavel,Lalancette, Roger A.,Lockard, Jenny V.
, p. 304 - 312 (2019/02/20)
Studying the axial ligation behavior of metalloporphyrins with nitrogenous bases helps to better understand not only the biological function of heme-based protein systems, but also the catalytic properties of porphyrin-based reaction sites in other biomim