Structural highlights
Function
YQJG_ECOLI Catalyzes glutathione (GSH)-dependent reduction of glutathionyl-hydroquinones (GS-HQs) to the corresponding hydroquinones. Can use a variety of GS-HQs as substrates, such as GS-p-hydroquinone (GS-HQ), GS-hydroxy-p-hydroquinone (GS-HHQ), GS-methyl-p-hydroquinone (GS-MHQ), GS-menadiol, and GS-trichloro-p-hydroquinone (GS-TriCH). Also displays GSH-dependent disulfide-bond reduction activity toward HED (2-hydroxyethyl disulfide), and is able to catalyze DMA (dimethylarsinate) reduction. Exhibits no GSH transferase activity with 1-chloro-2,4-dinitrobenzene (CDNB).[1] [2] [3]
References
- ↑ Xun L, Belchik SM, Xun R, Huang Y, Zhou H, Sanchez E, Kang C, Board PG. S-Glutathionyl-(chloro)hydroquinone reductases: a novel class of glutathione transferases. Biochem J. 2010 May 27;428(3):419-27. doi: 10.1042/BJ20091863. PMID:20388120 doi:http://dx.doi.org/10.1042/BJ20091863
- ↑ Lam LK, Zhang Z, Board PG, Xun L. Reduction of benzoquinones to hydroquinones via spontaneous reaction with glutathione and enzymatic reaction by S-glutathionyl-hydroquinone reductases. Biochemistry. 2012 Jun 26;51(25):5014-21. doi: 10.1021/bi300477z. Epub 2012 Jun, 13. PMID:22686328 doi:http://dx.doi.org/10.1021/bi300477z
- ↑ Green AR, Hayes RP, Xun L, Kang C. Structural understanding of the glutathione-dependent reduction mechanism of glutathionyl-hydroquinone reductases. J Biol Chem. 2012 Oct 19;287(43):35838-48. doi: 10.1074/jbc.M112.395541. Epub, 2012 Sep 6. PMID:22955277 doi:http://dx.doi.org/10.1074/jbc.M112.395541
