glutathione CAS NO.70-18-8

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about glutathione

glutathione (gsh) is an important antioxidant in plants, animals, fungi, and some bacteria and archaea, preventing damage to important heavy metals.[2] it is a tripeptide with a gamma peptide linkage between the carboxyl group of the glutamateside-chain and the amine group of cysteine (which is attached by normal peptide linkage to a glycine).

thiol groups are reducing agents, existing at a concentration around 5 mm in animal cells. glutathione reduces disulfide bonds formed within cytoplasmic proteins to cysteines by serving as an electron donor. in the process, glutathione is converted to its oxidized form, glutathione disulfide (gssg), also called l-(–)-glutathione.

once oxidized, glutathione can be reduced back by glutathione reductase, using nadph as an electron donor. the ratio of reduced glutathione to oxidized glutathione within cells is often used as a measure of cellular toxicity.

glutathione exists in both reduced (gsh) and oxidized (gssg) states. in the reduced state, the thiol group of cysteine is able to donate a reducing equivalent (h++ e−) to other unstable molecules, such as reactive oxygen species. in donating an electron, glutathione itself becomes reactive, but readily reacts with another reactive glutathione to form glutathione disulfide (gssg). such a reaction is probable due to the relatively high concentration of glutathione in cells (up to 5 mm in the liver).

gsh can be regenerated from gssg by the enzyme glutathione reductase (gsr): nadph reduces fad present in gsr to produce a transient fadh-anion. this anion then quickly breaks a disulfide bond (cys58 - cys63) and leads to cys63's nucleophilically attacking the nearest sulfide unit in the gssg molecule (promoted by his467), which creates a mixed disulfide bond (gs-cys58) and a gs-anion. his467 of gsr then protonates the gs-anion to form the first gsh. next, cys63 nucleophilically attacks the sulfide of cys58, releasing a gs-anion, which, in turn, picks up a solvent proton and is released from the enzyme, thereby creating the second gsh. so, for every gssg and nadph, two reduced gsh molecules are gained, which can again act as antioxidants scavenging reactive oxygen species in the cell.

in healthy cells and tissue, more than 90% of the total glutathione pool is in the reduced form (gsh) and less than 10% exists in the disulfide form (gssg). an increased gssg-to-gsh ratio is considered indicative of oxidative stress.

glutathione has multiple functions:

it is the major endogenous antioxidant produced by the cells, participating directly in the neutralization of free radicals and reactive oxygen compounds, as well as maintaining exogenous antioxidants such as vitamins c and e in their reduced (active) forms.

regulation of the nitric oxide cycle is critical for life, but can be problematic if unregulated.

it is used in metabolic and biochemical reactions such as dna synthesis and repair, protein synthesis, prostaglandin synthesis, amino acid transport, and enzyme activation. thus, every system in the body can be affected by the state of the glutathione system, especially the immune system, the nervous system, the gastrointestinal system, and the lungs.