In higher plants, NAD(P)H:quinone reductase (NQR) is the only flavoreductase known to reduce quinone substrates directly to hydroquinones by a two-electron reaction mechanism. This enzymatic activity is believed to protect aerobic organisms from the oxidative action of semiquinones. For this reason plant NQR has recently been suggested to be related to animal DT- diaphorase. A cDNA clone for NQR of Arabidopsis thaliana was identified, expressed in Escherichia coli, purified and characterized. Its amino acid sequence was found related to a number of putative proteins, mostly from prokaryotes, with still undetermined function. Conversely, in spite of the functional homology, sequence similarity between plant NQR and animal DT- diaphorase was limited and essentially confined to the flavin binding site.

Cloning and heterologous expression of NAD(P)H :quinone oxido reductase of Arabidopsis thalianaI, a functional homologue of animal DT-diaphorase / F. Sparla, G. Tedeschi, P. Pupillo, P. Trost. - In: FEBS LETTERS. - ISSN 0014-5793. - 463:3(1999), pp. 382-386. [10.1016/S0014-5793(99)01625-7]

Cloning and heterologous expression of NAD(P)H :quinone oxido reductase of Arabidopsis thalianaI, a functional homologue of animal DT-diaphorase

G. Tedeschi
Secondo
;
1999

Abstract

In higher plants, NAD(P)H:quinone reductase (NQR) is the only flavoreductase known to reduce quinone substrates directly to hydroquinones by a two-electron reaction mechanism. This enzymatic activity is believed to protect aerobic organisms from the oxidative action of semiquinones. For this reason plant NQR has recently been suggested to be related to animal DT- diaphorase. A cDNA clone for NQR of Arabidopsis thaliana was identified, expressed in Escherichia coli, purified and characterized. Its amino acid sequence was found related to a number of putative proteins, mostly from prokaryotes, with still undetermined function. Conversely, in spite of the functional homology, sequence similarity between plant NQR and animal DT- diaphorase was limited and essentially confined to the flavin binding site.
Settore BIO/10 - Biochimica
1999
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2434/181363
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