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Ascorbic acid reprogrames epigenome and epitranscriptome by recycling Fe (III) into Fe (II) in the catalytic cycle of dioxygenases

ABSTRACT: This SuperSeries is composed of the SubSeries listed below.

ORGANISM(S): Homo sapiens

PROVIDER: GSE242760 | GEO | 2024/02/01

REPOSITORIES: GEO

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Ascorbic acid reprogrames epigenome and epitranscriptome by recycling Fe (III) into Fe (II) in the catalytic cycle of dioxygenases (m6A)

Project description:Ascorbic acid has been reported to stimulate DNA iterative oxidase TET enzymes, Jumonji C-domain-containinghistone demethylase and potentially RNA m6A demethylase FTO and ALKBH5 as a cofactor. Although ascorbic acid has been widely investigated in reprogramming DNA and histone methylation status in vitro, in cell lines and mouse models, its specific role in the catalytic cycle of dioxygenases remains enigmatic. Here we systematically investigated the stimulation of ascorbic towards TET2, ALKBH3, histone demethylases and FTO. We find that ascorbic acid reprograms epitranscrip-tome by erasing the hypermethylated m6A sites. Biochemistry and Electron spin resonance (ESR) assays demonstrate that ascorbic acid enters the active pocket of dioxygenases, reduces Fe (III), either incorporated upon protein synthesis or generated upon rebounding the hydroxyl radical during oxidation, into Fe (II). Finally, we propose a new model for the catalytic cycle of dioxygenases by adding in the essential dynamic cofactor, ascorbic acid. Ascorbic acid refreshes and regenerates inactive dioxygenase through recycling Fe (III) into Fe (II) in a dynamic “hit-and-run” manner.

2024-02-01 | GSE242758 | GEO

Ascorbic acid reprogrames epigenome and epitranscriptome by recycling Fe (III) into Fe (II) in the catalytic cycle of dioxygenases (RNA-Seq)

2024-02-01 | GSE242759 | GEO

Ascorbic acid reprogrames epigenome and epitranscriptome by recycling Fe (III) into Fe (II) in the catalytic cycle of dioxygenases

Project description:Ascorbic acid reprogrames epigenome and epitranscriptome by recycling Fe (III) into Fe (II) in the catalytic cycle of dioxygenases

| PRJNA1014456 | ENA

Ascorbic acid reprogrames epigenome and epitranscriptome by recycling Fe (III) into Fe (II) in the catalytic cycle of dioxygenases (m6A)

Project description:Ascorbic acid reprogrames epigenome and epitranscriptome by recycling Fe (III) into Fe (II) in the catalytic cycle of dioxygenases (m6A)

| PRJNA1014463 | ENA

Ascorbic acid reprogrames epigenome and epitranscriptome by recycling Fe (III) into Fe (II) in the catalytic cycle of dioxygenases (RNA-Seq)

Project description:Ascorbic acid reprogrames epigenome and epitranscriptome by recycling Fe (III) into Fe (II) in the catalytic cycle of dioxygenases (RNA-Seq)

| PRJNA1014464 | ENA

A synthetic model of the putative Fe(II)-iminobenzosemiquinonate intermediate in the catalytic cycle of o-aminophenol dioxygenases.

Project description:The oxidative ring cleavage of aromatic substrates by nonheme Fe dioxygenases is thought to involve formation of a ferrous-(substrate radical) intermediate. Here we describe the synthesis of the trigonal-bipyramdial complex Fe((Ph2)Tp)(ISQ(tBu)) (2), the first synthetic example of an iron(II) center bound to an iminobenzosemiquinonate (ISQ) radical. The unique electronic structure of this S = 3/2 complex and its one-electron oxidized derivative ([3](+)) have been established on the basis of crystallographic, spectroscopic, and computational analyses. These findings further demonstrate the viability of Fe(2+)-ISQ intermediates in the catalytic cycles of o-aminophenol dioxygenases.

| S-EPMC3324092 | biostudies-literature

Application of ascorbic acid to enhance trichloroethene degradation by Fe(III)-activated calcium peroxide.

Project description:The enhancement effect of an environmentally friendly reducing agent, ascorbic acid (AA), on trichloroethene (TCE) degradation by Fe(III)-activated calcium peroxide (CP) was evaluated. The addition of AA accelerated the transformation of Fe(III) to Fe(II), and the complexation of Fe(III)/Fe(II) with AA and its products alleviated the precipitation of dissolved iron. These impacts enhanced the generation of reactive oxygen species (ROSs). Investigation of ROSs using chemical probe tests, electron paramagnetic resonance (EPR) tests, and radical scavenger tests strongly confirm large production of hydroxyl radicals (HO•) that is responsible for TCE degradation. The generation of Cl- from the degraded TCE was complete in the enhanced CP/Fe(III)/AA system. The investigation of solution matrix effects showed that the TCE degradation rate decreases with the increase in solution pH, while Cl-, SO42- and NO3- anions have minor impact. Conversely, HCO3- significantly inhibited TCE degradation due to pH elevation and HO• scavenging. The results of experiments performed using actual groundwater indicated that an increase in reagent doses are required for effective TCE removal. In summary, the potential effectiveness of the CP/Fe(III)/AA oxidation system for remediation of TCE contaminated groundwater has been demonstrated. Additional research is needed to develop the system for practical implementation.

| S-EPMC5665388 | biostudies-literature

Evaluation of Fe(iii)EDTA reduction with ascorbic acid in a wet denitrification system.

Project description:The reduction of Fe(iii)EDTA to Fe(ii)EDTA is the core process in a wet flue gas system with simultaneous desulfurization and denitrification. Herein, at first, the reductant ascorbic acid (VC) was used for reducing Fe(iii)EDTA. The feasibility of Fe(iii)EDTA reduction with ascorbic acid was investigated at different Fe(iii)EDTA concentrations, various pH values, diverse temperatures, and different molar ratios of VC to Fe(iii)EDTA. The results showed that the Fe(ii)EDTA concentration increased with an increase in the initial Fe(iii)EDTA concentration. Furthermore, the reduction efficiency increased as the mole ratio of VC to Fe(iii)EDTA was increased, and all the Fe(iii)EDTA reduction efficiencies were close to 100% when the mole ratio was more than 0.5. On the other hand, an alkaline environment did not favor the conversion of Fe(iii)EDTA by VC. The Fe(iii)EDTA conversion slightly increased as the temperature was increased. Moreover, compared with other reduction systems, ascorbic acid (VC) was found to be more powerful in reducing Fe(iii)EDTA, especially in air. In addition, VC only exhibited powerful ability in the conversion of Fe(iii)EDTA to Fe(ii)EDTA and hardly reduced Fe(ii)EDTA-NO. Finally, the stoichiometry of Fe(iii)EDTA reduction by ascorbic acid was derived. Thus, our study would offer a bridge between foundational research and industrial denitration using the combination of Fe(ii)EDTA and VC.

| S-EPMC9069671 | biostudies-literature

Iron Catalyzed Double Bond Isomerization: Evidence for an Fe<sup>I</sup> /Fe<sup>III</sup> Catalytic Cycle.

Project description:Iron-catalyzed isomerization of alkenes is reported using an iron(II) β-diketiminate pre-catalyst. The reaction proceeds with a catalytic amount of a hydride source, such as pinacol borane (HBpin) or ammonia borane (H3 N⋅BH3 ). Reactivity with both allyl arenes and aliphatic alkenes has been studied. The catalytic mechanism was investigated by a variety of means, including deuteration studies, Density Functional Theory (DFT) and Electron Paramagnetic Resonance (EPR) spectroscopy. The data obtained support a pre-catalyst activation step that gives access to an η2 -coordinated alkene FeI complex, followed by oxidative addition of the alkene to give an FeIII intermediate, which then undergoes reductive elimination to allow release of the isomerization product.

| S-EPMC8048803 | biostudies-literature

2-oxoglutarate-dependent dioxygenases: A renaissance in attention for ascorbic acid in plants.

Project description:L-Ascorbic acid (ascorbate, Vitamin C) is an essential human micronutrient that is predominantly obtained from plants. It is known to work as the major antioxidant in plants, and it underpins several environmentally induced stresses due to its use as a co-factor by certain 2-oxoglutarate-dependent (2-OG) dioxygenases [2(OG)-dioxygenases]. It is important to understand the role of 2(OG)-dioxygenases in the biosynthesis of ascorbate. The present study examined contents of ascorbate and protein-protein interaction in nine T-DNA mutants of Arabidopsis containing an insert in their respective (2-OG) dioxygenase genes (At1g20270, At1g68080, At2g17720, At3g06290, At3g28490, At4g35810, At4g35820, At5g18900, At5g66060). In this study, the amount of ascorbate in five of the mutants was shown to be almost two-fold or more than two-fold higher than in the wild type. This result may be a consequence of the insertion of the T-DNA. The prediction of possible protein interactions between 2(OG)-dioxygenases and relevant ascorbate-function players may indicate the oxidative effects of certain dioxygenase proteins in plants. It is expected that certain dioxygenases are actively involved in the metabolic and biosynthetic pathways of ascorbate. This involvement may be of importance to increase ascorbate amounts in plants for human nutrition, and to protect plant species against stress conditions.

| S-EPMC7723244 | biostudies-literature

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