Interaction of Glutathione with Hydrogen Peroxide: A Kinetic Model

The kinetic characteristics of the interaction of N-acetylcysteine (ASH) with reactive oxygen species (ROS), peroxyl radicals and hydrogen peroxide were determined. It was found that in terms of activity ASH in these reactions is similar to glutathione GSH, the main endogenous bioantioxidant. The kinetics of heat release in the interaction of GSH and ASH with H 2 O 2 was studied for the fi rst time by isothermal calorimetry. It is shown that the kinetic curves of heat release and changes in specifi c heat release rates practically coincide for both thiols taken in the stoichiometric ratio in the known reaction 2 TSH + H 2 O 2  TSST + 2 H 2 O.This indicates the relative autonomy of the S-H and S-S bonds in thiols and disulfi des, which are not aff ected by other groups in the molecule. At pH<7, ASH, like GSH, interacts with H 2 O 2 to form thiyl radicals, which initiate thiol-ene reactions with unsaturated phenol resveratrol. Under the same conditions, ASH ensures nearly the same radical initiation rates as GSH, and thiyl radicals from ASH are close in activity to GS • in chain propagation reactions.

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“…15 Empirical functions of W i from thiol concentrations and H 2 O 2 for GSH (see lit. 10 ) and ASH can be represented as:…”

Section: Resultsmentioning

confidence: 99%

N-Acetylcysteine is an effective analog of glutathione in reactions with reactive oxygen species

et al. 2021

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“…The rate of reaction depends on the cellular GSH level and the ratio of GSH to H 2 O 2 concentrations [ 100 ]. Recently, Zinatullina et al [ 101 ] confirmed that the oxidation of GSH is accompanied by radical formation. GSH reacts with the majority of free radicals generating thiyl radicals.…”

Section: Glutathionementioning

confidence: 99%

Glutathione-Related Enzymes and Proteins: A Review

Vašková

Kočan²,

Vaško

et al. 2023

Molecules

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The tripeptide glutathione is found in all eukaryotic cells, and due to the compartmentalization of biochemical processes, its synthesis takes place exclusively in the cytosol. At the same time, its functions depend on its transport to/from organelles and interorgan transport, in which the liver plays a central role. Glutathione is determined as a marker of the redox state in many diseases, aging processes, and cell death resulting from its properties and reactivity. It also uses other enzymes and proteins, which enables it to engage and regulate various cell functions. This paper approximates the role of these systems in redox and detoxification reactions such as conjugation reactions of glutathione-S-transferases, glyoxylases, reduction of peroxides through thiol peroxidases (glutathione peroxidases, peroxiredoxins) and thiol–disulfide exchange reactions catalyzed by glutaredoxins.

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“…11 The fact that GSH and H 2 O 2 can react with each other, and the addition of single-responsive probes may disrupt cellular redox balance, potentially results in suspicion on this to some extent. 12 Dual responsive fluorescent probes for simultaneous GSH and H 2 O 2 detection can afford reliable evidence for this conclusion. Herein, we report a fluorescence resonance energy transfer (FRET) based GSH/H 2 O 2 dual responsive fluorogenic probe for simultaneous detection of GSH and H 2 O 2 via distinctive fluorescence channels.…”

mentioning

confidence: 92%