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NQO1  -  NAD(P)H dehydrogenase, quinone 1

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Disease relevance of NQO1

  • The order of the seven structural genes of the Paracoccus NADH-quinone oxidoreductase in the gene cluster is NQO7, NQO6, NQO5, NQO4, NQO2, NQO1, and NQO3 [1].
  • The above compounds acted as redox-cycling substrates for single-electron transferring NADPH:cytochrome P-450 reductase (P-450R) and ferredoxin:NADP(+) reductase (FNR), as well as substrates for the two-electron transferring flavoenzymes rat liver NAD(P)H:quinone oxidoreductase (NQO1) and Enterobacter cloacae NAD(P)H:nitroreductase (NR) [2].
 

High impact information on NQO1

  • Comparison of the deduced primary structures of the subunits with consensus sequences for the cofactor binding sites has predicted that NQO1, NQO2, NQO3, NQO9, and probably NQO6 subunits are cofactor binding subunits [3].
  • Studies were carried out under control conditions and with dicumarol, to inhibit NAD(P)H:quinone oxidoreductase 1 (NQO1), or cyanide, to inhibit mitochondrial electron transport [4].
  • The order of the 14 structural genes of the Paracoccus energy-transducing NADH-Q oxidoreductase in the gene cluster is NQ07, NQO6, NQO5, NQO2, NQO1, NQO3, NQO8, NQO9, NQO10, NQO11, NQO12, NQO13, and NQO14 [5].
  • In addition, nucleotide sequencing shows the presence of two unidentified reading frames between the NQO1 and NQO2 genes [6].
  • On the basis of the amino acid sequence, the NQO2 gene was found to be located 1.7 kilobase pairs upstream of the gene for NADH-binding subunit (NQO1) [6].
 

Biological context of NQO1

 

Analytical, diagnostic and therapeutic context of NQO1

  • In addition, the subunit stoichiometry of NQO1 through -6 of the membrane-bound P. denitrificans NDH-1 has been determined by radioimmunoassays [8].

References

  1. Gene cluster of the energy-transducing NADH-quinone oxidoreductase of Paracoccus denitrificans: characterization of four structural gene products. Xu, X., Matsuno-Yagi, A., Yagi, T. Biochemistry (1992) [Pubmed]
  2. Flavoenzyme-catalyzed redox cycling of hydroxylamino- and amino metabolites of 2,4,6-trinitrotoluene: implications for their cytotoxicity. Sarlauskas, J., Nemeikaite-Ceniene, A., Anusevicius, Z., Miseviciene, L., Julvez, M.M., Medina, M., Gomez-Moreno, C., Cenas, N. Arch. Biochem. Biophys. (2004) [Pubmed]
  3. Expression and characterization of the 66-kilodalton (NQO3) iron-sulfur subunit of the proton-translocating NADH-quinone oxidoreductase of Paracoccus denitrificans. Yano, T., Yagi, T., Sled, V.D., Ohnishi, T. J. Biol. Chem. (1995) [Pubmed]
  4. Impact of pulmonary arterial endothelial cells on duroquinone redox status. Merker, M.P., Bongard, R.D., Krenz, G.S., Zhao, H., Fernandes, V.S., Kalyanaraman, B., Hogg, N., Audi, S.H. Free Radic. Biol. Med. (2004) [Pubmed]
  5. DNA sequencing of the seven remaining structural genes of the gene cluster encoding the energy-transducing NADH-quinone oxidoreductase of Paracoccus denitrificans. Xu, X., Matsuno-Yagi, A., Yagi, T. Biochemistry (1993) [Pubmed]
  6. Characterization of the 25-kilodalton subunit of the energy-transducing NADH-ubiquinone oxidoreductase of Paracoccus denitrificans: sequence similarity to the 24-kilodalton subunit of the flavoprotein fraction of mammalian complex I. Xu, X.M., Matsuno-Yagi, A., Yagi, T. Biochemistry (1991) [Pubmed]
  7. Structural features of the 66-kDa subunit of the energy-transducing NADH-ubiquinone oxidoreductase (NDH-1) of Paracoccus denitrificans. Xu, X., Matsuno-Yagi, A., Yagi, T. Arch. Biochem. Biophys. (1992) [Pubmed]
  8. Structural studies of the proton-translocating NADH-quinone oxidoreductase (NDH-1) of Paracoccus denitrificans: identity, property, and stoichiometry of the peripheral subunits. Takano, S., Yano, T., Yagi, T. Biochemistry (1996) [Pubmed]
 
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