EC - Glutathionyl-hydroquinone reductase

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IntEnz Enzyme Nomenclature


Accepted name:
glutathionyl-hydroquinone reductase
Other names:
pcpF (gene name)
yqjG (gene name)
Systematic name:
2-(glutathione-S-yl)-hydroquinone:glutathione oxidoreductase



This type of enzymes, which are found in bacteria, halobacteria, fungi, and plants, catalyse the glutathione-dependent reduction of glutathionyl-hydroquinones. The enzyme from the bacterium Sphingobium chlorophenolicum can act on halogenated substrates such as 2,6-dichloro-3-(glutathione-S-yl)-hydroquinone and 2,3,5-trichloro-6-(glutathione-S-yl)-hydroquinone. Substrates for these enzymes are often formed spontaneously by interaction of benzoquinones with glutathione.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB


  1. Huang, Y., Xun, R., Chen, G., Xun, L.
    Maintenance role of a glutathionyl-hydroquinone lyase (PcpF) in pentachlorophenol degradation by Sphingobium chlorophenolicum ATCC 39723.
    J. Bacteriol. 190: 7595-7600 (2008). [PMID: 18820023]
  2. Xun, L., Belchik, S. M., Xun, R., Huang, Y., Zhou, H., Sanchez, E., Kang, C., Board, P. G.
    S-Glutathionyl-(chloro)hydroquinone reductases: a novel class of glutathione transferases.
    Biochem. J. 428: 419-427 (2010). [PMID: 20388120]
  3. Lam, L. K., Zhang, Z., Board, P. G., Xun, L.
    Reduction of benzoquinones to hydroquinones via spontaneous reaction with glutathione and enzymatic reaction by S-glutathionyl-hydroquinone reductases.
    Biochemistry 51: 5014-5021 (2012). [PMID: 22686328]
  4. Green, A. R., Hayes, R. P., Xun, L., Kang, C.
    Structural understanding of the glutathione-dependent reduction mechanism of glutathionyl-hydroquinone reductases.
    J. Biol. Chem. 287: 35838-35848 (2012). [PMID: 22955277]

[EC created 2017]