Abnormalities of hydrogen sulfide and glutathione pathways in mitochondrial dysfunction PY2021 IR95 cysteine, sulfur
https://www.sciencedirect.com/science/article/pii/S2090123220300643
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Fig. 2. Transsulfuration and H2S oxidation pathways. In the transsulfuration pathway (in orange), the enzymes cystathionine β-synthase (CBS) and cystationine γ-ligase (CSE) use cysteine as a substrate for the synthesis of sulfides (H2S). The same cysteine is used by glutamate cysteine ligase (GCL) for the synthesis of GSH in the glutathione pathway (not shown). In the mitochondrial H2S oxidation (in red), sulfide-quinone oxidoreductase (SQR) converts sulfide into thiosulfate by transferring two electrons from H2S to CoQ. Thiosulfate is then converted into sulfite by thiosulfate sulfurtransferase (TST) and persulfide dioxygenase (ETHE1), a reaction that requires glutathione (GSH) as an electron acceptor. Excess sulfite is converted into sulfate by sulfite oxidase (SUOX). 3-MP = 3-mercaptopyruvate, 3-MST = 3-mercaptopyruvate sulfurtransferase, CoQ Ox = Coenzyme Q oxidized, CoQRed = Coenzyme Q reduced.
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