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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 

DT-diaphorase catalyzes N-denitration and redox cycling of tetryl.

Rat liver DT-diaphorase (EC 1.6.99.2) catalyzed reductive N-denitration of tetryl (2,4,6-tri-nitrophenyl-N-methylnitramine) and 2,4-dinitrophenyl-N-methylnitramine, oxidizing the excess of NADPH. The reactions were accompanied by oxygen consumption and superoxide dismutase-sensitive reduction of added cytochrome c and reductive release of Fe2+ from ferritin. Quantitatively, the reactions of DT-diaphorase proceeded like single-electron reductive N-denitration of tetryl by ferredoxin:NADP+ reductase (EC 1.18.1.2) (Shah, M.M. and Spain, J.C. (1996) Biochem. Biophys. Res. Commun. 220, 563-568), which was additionally checked up in this work. Thus, although reductive N-denitration of nitrophenyl-N-nitramines is a net two-electron (hydride) transfer process, DT-diaphorase catalyzed the reaction in a single-electron way. These data point out the possibility of single-electron transfer steps during obligatory two-electron (hydride) reduction of quinones and nitroaromatics by DT-diaphorase.[1]

References

  1. DT-diaphorase catalyzes N-denitration and redox cycling of tetryl. Anusevicius, Z., Sarlauskas, J., Nivinskas, H., Segura-Aguilar, J., Cenas, N. FEBS Lett. (1998) [Pubmed]
 
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