Abstract

This report describes how the coordination of FeCl2 with tris(pyridin-2-ylmethyl)amine (TPA) ligands offers the possibilty to activate the molecular dioxygen in biomimetic processes. . It includes all procedures taken to the case for major oxidation reactions carried out in Nature under particular conditions. The aim of the this paper is to present the outcome of a thorough study for complex coordinations with ligands substituted by groups known as electron donors. It demonstrates how ligands with methoxy substituents are likely to be demethylated, and therefore providing entities potentially useful in synthesis. Targeting in modulating the electronic properties at the metal center, a new type of ligand (MeO)2TPA has been prepared and the complex of (MeO)2TPAFeCl2 has been studied by uv-visble ; 1H RMN paramagnatic and conductometry. The effect of (MeO) group in α-substituted on the structure as well as the effect of substitution on the oxygenation of the complex has been verified. Afterwards, the reactivity of the complex towards molecular dioxygen in absence of substrat is checked by uvvisble, 1H RMN paramagnatic and radiocristallography. As well, the reactivity in presence of substrat is tested.

Highlights

  • Hydroxylation reactions, which take place in the presence of molecular oxygen, ferrous iron and tetrahydrobiopterin (BH4) [1], are found in several biological processes

  • Due to the sequential and structural homology and the similarity of the chemical transformations occurring by phenylalanine hydroxylase (PAH),Tyrosine hydroxylase (TyrH), and Tryptophan hydroxylase (TrpH), it is commonly believed that these three enzymes have a similar hydroxylation mechanism [1,9,10,11,12,13]

  • Synthesis of 2-methoxy-6-Methylpyridine [26]. : 6.10 g (153mmoles) of 60% NaH are washed with hexane and the mineral oil is extracted several times under argon until obtaining NaH without oil. 12 g (70mmoles) of 2-Bromo-6-Methylpyridine are dissolved in 80 ml of DMF, the solution is added to the NaH gradually over 15 minutes

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Summary

Introduction

Hydroxylation reactions, which take place in the presence of molecular oxygen, ferrous iron and tetrahydrobiopterin (BH4) [1], are found in several biological processes. Tryptophan hydroxylase (TrpH), catalyzes the transformation of L-Tryptophan to 5Hydroxytryptophan (Serotonin, 5-HT) as shown, Serotonin is known to play important roles in many biological functions [1,2,3,4,5,6,7,8]. Due to the sequential and structural homology and the similarity of the chemical transformations occurring by phenylalanine hydroxylase (PAH),Tyrosine hydroxylase (TyrH), and Tryptophan hydroxylase (TrpH), it is commonly believed that these three enzymes have a similar hydroxylation mechanism [1,9,10,11,12,13]. Revised Manuscript received on September 25, 2021.

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