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