Photoperiod regulates the daily profiles of tryptophan hydroxylase-2 gene expression the raphe nuclei of rats

Malek, Zeina; Labban, Louay

doi:10.1080/00207454.2020.1782903

Cited by 24 publications

(11 citation statements)

References 32 publications

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“…Almost all methanotrophs express the copper-containing pMMO enzyme. In certain methanotrophic organisms, the expression of the soluble sMMO form has also been observed, such as in Trichosporon methylosinus and Methylococcus capsulatus [22][23][24][25][26][27][28][29]. Unlike pMMO, sMMO is much more stable and easier to purify from a structural standpoint [28][29][30][31][32].…”

Section: -Ecologymentioning

confidence: 99%

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Review of a Few Selected Examples of Intermolecular Dioxygenases Involving Molecular Oxygen and Non-Heme Iron Proteins

Thallaj¹

2023

IJAPSR

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Molecular oxygen and non-heme iron proteins (NHIPs) are proteins that have an iron atom bound to one or more oxygen atoms, and are found in bacteria, archaea, and some eukaryotes. NHIPs are involved in a variety of biological processes, such as respiration, electron transfer, and catalysis. They can be categorized into two classes: cytochrome proteins, which are involved in electron transfer, and oxygenases, which catalyze the oxidation of substrates by utilizing molecular oxygen. NHIPs are critical for multiple biological processes, and their impairment has been associated with diseases such as anemia, cancer, and neurological disorders.

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Section: -Ecologymentioning

confidence: 99%

“…Reference 32 MMOR (Membrane-Bound Oxidoreductase) facilitates the transfer of two electrons from NADH (Nicotinamide Adenine Dinucleotide) to MMOH (Methyl Viologen) through the use of two prosthetic groups: an Fe2S2 cluster and FAD (Flavin Adenine Dinucleotide) [30].…”

Section: Schema 17 : Mmoh Mmor and Mmob Subunit Relationships And Sub...mentioning

confidence: 99%

Review of a Few Selected Examples of Intermolecular Dioxygenases Involving Molecular Oxygen and Non-Heme Iron Proteins

Thallaj¹

2023

IJAPSR

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“…However, in the majority of cases, hydroperoxides are used as oxygen donating agents [4][5][6][7][8][9][10][11][12][13][14][15][16].…”

Section: Introductionmentioning

confidence: 99%

“…Molecular oxygen has been well used, however, but it only reacts with ferrous compounds which are already coordinated with substrates which activate the metal, such as catechols or thiolates for example [8][9][10][11][12][13][14][15]. Another well studied enzyme in biological systems is tryptophan hydroxylase, which catalyzes a key step in serotonin biosynthesis and plays important roles in the circadian rhythms .…”

Section: Introductionmentioning

confidence: 99%

Ligands tris(2-pyridylmethyl)amine with nitrile group in α-substituted and the corresponding FeCl2 complexes

Thallaj

2022

Preprint

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We have synthesized the mono, bis and tris nitrile at the α position ligands in the tris(2-pyridylmethyl) amine (TPA) series, respectively CNTPA, (CN)2TPA and (CN)3TPA. Nitrile at the α position of these nitrogen-containing tripods shifts the oxidation potential of the ligand by comparison with the TPA ligand, it is observed that the oxidation potentials of the ligands increase regularly with the number of nitrile groups. For each group added, the oxidation potential is increased by an average of 110mV / ECS. This reflects the strong electron-withdrawing effect of the nitrile groups.. The crystal structure analysis of the dichloroferrous complexes with CNTPA and (CN)2TPA reveals that the iron lies in a distorted octahedral geometry comparable to that already found in TPAFeCl2. All spectroscopic data indicate that the geometry is retained in solution. These three isostructural complexes all react with molecular dioxygen to yield µ-oxo diferric complexes as stable compounds. Upon reduction, all µ-oxo diferric complexes convert back into the starting ferrous species. The oxygenation reaction parallels the well known formation of µ-oxo derivatives from dioxygen in chemistry of porphyrins reported almost three decades ago. The crystal structure analysis is reported for each of these three µ-oxo compounds. With TPA, a symmetrical structure is obtained for a dicationic compound, the tripod coordinating in the (κ4-N) coordination mode. With CNTPA, the compound is a neutral µ-oxo di-ferric complex. When oxygenation is carried out on the (CN)2TPA complex, a neutral asymmetrical compound is obtained. The striking point within the series of ferrous precursors is the effect of the ligand on the kinetics of oxygenation of the complexes. Whereas the parent complex undergo full oxygenation over 14 hours, the mono nitrile ligand provides a complex that has fully reacted over 14 hours, the reaction time being only 2 hours for the complex with the dinitriles ligand,and for trinitriles ligand it will tack 30min. Thus electron-deficiency ( Lewis acidity at the metal centre) seems to govern the kinetics of oxygenation. This strongly suggests coordination of the dioxygen as an initial step in the process leading to formation of µ-oxo diferric compounds, by contrast with un unlikely outer sphere reduction of dioxygen, that generally occurs at very negative potentials. Finally, we report that cyclohexane is catalytically converted into cyclohexanone when reacted with dioxygen in the presence of zinc amalgam, and that the conversion rate also parallels the Lewis acidity at the metal center, with the best rate obtained for with (CN)2TPAFeCl2.

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“…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 5-Hydroxytryptophan (Serotonin, 5-HT) as shown in Figure 1, 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].…”

mentioning

confidence: 99%

Ferrous Complexes with Bis Meo in Α Substituted Tris Pyridin 2 Ylmethyl Amine Ligands Effect of the Bis Meo in Α Substituents in Dioxygen Activation and Biomimetic Reactivity

Thallaj¹

2021

IJAC

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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.

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Photoperiod regulates the daily profiles of tryptophan hydroxylase-2 gene expression the raphe nuclei of rats

Cited by 24 publications

References 32 publications

Review of a Few Selected Examples of Intermolecular Dioxygenases Involving Molecular Oxygen and Non-Heme Iron Proteins

Review of a Few Selected Examples of Intermolecular Dioxygenases Involving Molecular Oxygen and Non-Heme Iron Proteins

Ligands tris(2-pyridylmethyl)amine with nitrile group in α-substituted and the corresponding FeCl2 complexes

Ferrous Complexes with Bis Meo in Α Substituted Tris Pyridin 2 Ylmethyl Amine Ligands Effect of the Bis Meo in Α Substituents in Dioxygen Activation and Biomimetic Reactivity

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