PMID 10501216 Inhibitors of mitochondrial respiration, iron II, and
hydroxyl radical evoke release and extracellular hydrolysis of glutathione
in rat striatum and substantia nigra: potential implications to Parkinsons
disease.
It is interesting that a very early event in the pathogenesis of
Parkinson's disease is a massive loss of GSH in the substantia nigra
pars compacta that is not accompanied by corresponding increases of GSSG
levels.
RECYCLING of GLUTATHIONE: Reduced (anti-oxidized) glutathione (GSH) is used
by glutathione peroxidase (a selenium dependent enzyme) (Tellurium is
antagonistic to selenium, they compete.). GSH is used to detoxify hydrogen
peroxide. In this process the oxidation power of hydrogen peroxide is
transferred to oxidized glutathione (GSSG). GSSG is recycled by glutathione
reductase using NADPH from Complex I.( which is inhibited by MPTP and
Tellurium.)
So the GSH is decreased trying to detoxify hydrogen peroxide made by
Fe3+ iron and dopamine. But something breaks down because it never
becomes GSSG.
PMID 9494575 Dairyl chalcogenides as selective inhibitors of thioredoxin
and potential antitumor agents.
Human glutathione reductase was inhibited by one dinitro organotellurium
(dimethyltelluride or N-Methyl-tellurium) that had an over 20-fold
selectivity compared to thioredoxin reductase.
Dr. James Thomas - Oxidative stress produces both glutathione disulfide in
the glutathione cycle and S-thiolated proteins like glutaredoxin in the
protein cycle. These oxidized materials are continuously reduced by
cellular metabolism that provides reducing power of the glutathione cycle
through glutathione reductase and for the protein cycle through small
proteins like glutaredoxin and thioredoxin. Protein
S-thiolation/dethiolation is research in the reversible formation of
disulfide adducts between protein sulfhydryl and the sulfhydryl of
glutathione.
Tellurium is a sulphur-like metal, that is highly mutagenic.
