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DT‐diaphorase catalyzes N‐denitration and redox cycling of tetryl
Author(s) -
Anusevičius Žilvinas,
Šarlauskas Jonas,
Nivinskas Henrikas,
Segura-Aguilar Juan,
Č≐nas Narimantas
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)01115-6
Subject(s) - chemistry , diaphorase , electron transfer , redox , oxidizing agent , hydride , nad+ kinase , medicinal chemistry , photochemistry , inorganic chemistry , enzyme , biochemistry , organic chemistry , hydrogen
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 Fe 2+ 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.