Refernces
10.1021/ja3083818
The research discusses the interconversion of nitrogen oxides, nitrite (NO2?) and nitric oxide (NO), mediated by a heme/Copper (Cu) assembly, mimicking the active site of cytochrome c oxidase. The study focuses on the role of this assembly in cellular processes, particularly in oxygen sensing and nitric oxide signaling. Experiments involved the reaction of a partially reduced heme/Cu complex with nitrite to produce nitric oxide, with the heme acting as the reductant and CuII ion facilitating the process. Conversely, a μ-oxo heme-FeIII?O?CuII complex was used to oxidize NO back to nitrite. Reactants included the iron(II) complex (F8)FeII and a preformed copper(II)?nitrito complex [(tmpa)CuII(NO2)][B(C6F5)4], with reactions carried out under a nitrogen atmosphere in acetone at room temperature. Analyses used to characterize the products and monitor the reactions included UV?vis, electron paramagnetic resonance (EPR), and IR spectroscopies, as well as capillary electrophoresis for nitrite analysis. The research provides insights into the biological chemistry of nitrogen oxides and the role of heme/Cu assemblies in these redox reactions.
10.1021/acs.inorgchem.1c00755
The research investigates the formation and properties of linkage isomers in manganese(II) porphyrin complexes with 4-methylimidazolate (4-MeIm?). The study aims to understand the structural and electronic behavior of these complexes, particularly focusing on the impact of different bonding sites (N1 or N3) of 4-MeIm? on the ligand conformation and overall complex stability. The researchers synthesized various Mn(II) porphyrinates using different porphyrin ligands (TPP, TTP, and TMP) and characterized the products using UV?visible spectroscopy, single-crystal X-ray diffraction, and electron paramagnetic resonance (EPR) spectroscopy. They discovered that 4-MeIm? can bond to the metal center through either N1 or N3, resulting in two linkage isomers with either hindered or unhindered ligand conformations. The study concludes that the large metal out-of-plane displacements in these complexes significantly reduce the steric effects, allowing both isomers to exist with a small energy difference (5.2?8.3 kJ/mol). This finding highlights the importance of nonbonded interactions in stabilizing the linkage isomers and provides insights into the electronic and structural properties of Mn(II) porphyrinates, which are relevant for understanding heme proteins and designing new catalytic systems.
10.1016/S0040-4039(01)80738-3
The research aimed to achieve asymmetric syntheses of amino acids through the addition of cyanide to Schiff bases in the presence of a cyanide-modified hemin-copolymer. The purpose was to enhance the optical yields of resulting amino acids by utilizing the steric control provided by the hemin-copolymer, which contains a large π electron system and shows aromatic properties. The study concluded that the optical yields (80-95% e.e.) were significantly higher than those obtained without the hemin-copolymer, indicating that the hemin in the copolymer provided strong steric control in the asymmetric addition of the CN group. Key chemicals used in the process included hemin, divinylbenzene, 2-methyl-5-vinylpyridine for the preparation of the hemin-copolymer, potassium cyanide for CN-modification, optically active amines such as (R)- and (S)-1-phenyl-1-ethylamine, (R)-1-phenyl-1-propylamine, and (R)-1-naphthyl-1-ethylamine, aliphatic aldehydes, and anhydrous sodium sulfate in the preparation of Schiff bases. The synthesized amino acids were then converted to N-trifluoroacetyl amino acid isopropyl esters for enantiomeric excess determination by gas chromatography using a chiral stationary phase.
10.1016/j.ejmech.2012.03.007
The study investigates the synthesis and biological evaluation of a series of 2-aminopyrimidine based 4-aminoquinoline compounds designed to combat malaria, particularly against drug-resistant strains of Plasmodium falciparum. The researchers synthesized these compounds using a protocol that involved the transformation of 3,4-dihydropyrimidin-2(1H)-ones (DHPMs) into 2-aminopyrimidines linked to 4-aminoquinolines. The compounds were evaluated for their in vitro anti-plasmodial activity against both chloroquine-sensitive (CQS) and chloroquine-resistant (CQR) strains of P. falciparum. The study found that some of these compounds, notably 10r, exhibited potent anti-plasmodial activity, with IC50 values significantly lower than that of chloroquine (CQ), especially against the CQR strain. The structure-activity relationship (SAR) analysis revealed that the length and nature of the spacer connecting the pharmacophores, as well as the presence of substituents like nitro groups, influenced the compounds' potency. The mode of action studies indicated that these compounds bind to heme and m-oxo-heme, inhibiting the formation of b-hematin, similar to CQ. Additionally, the compounds showed binding affinity to DNA, particularly AT-rich DNA, suggesting another potential mechanism of action. Molecular docking analysis with Pf DHFR further supported the compounds' ability to interact with this enzyme, which is crucial for the parasite's DNA biosynthesis. Overall, the study highlights the potential of these hybrid compounds as new anti-malarial agents with activity against drug-resistant strains.