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Gene Review

qor  -  quinone oxidoreductase

Escherichia coli O157:H7 str. EDL933

 
 
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Disease relevance of qor

  • The CAA43 gene was cloned and shown to encode a protein of 333 amino acid residues (M(r) 35,788) that shared a significant sequence similarity with NADPH-dependent quinone oxidoreductase from Escherichia coli (38.2% identity) [1].
  • The proton-translocating reduced nicotinamide adenine dinucleotide- (NADH-) quinone oxidoreductase (NDH-1) of Paracoccus denitrificans is composed of at least 14 different subunits (NQO1-14) [2].
  • Membrane Topology Mapping of the Na+-Pumping NADH: Quinone Oxidoreductase from Vibrio cholerae by PhoA- Green Fluorescent Protein Fusion Analysis [3].
  • Overproduction, crystallization and preliminary X-ray diffraction analysis of a quinone oxidoreductase from Thermus thermophilus HB8 [4].
  • Low temperature EPR and MCD studies on cytochrome b-558 of the Bacillus subtilis succinate: quinone oxidoreductase indicate bis-histidine coordination of the heme iron [5].
 

High impact information on qor

  • Single crystals suitable for X-ray diffraction studies have been obtained from a soluble Escherichia coli NAD(P)H-dependent quinone oxidoreductase (QOR) of molecular mass 35 kDa [6].
  • The C-terminal sequence of HndA shows 27% identity with the C-terminal sequence of the 25-kDa subunit of NADH: quinone oxidoreductase from Paracoccus denitrificans, 33% identity with the C-terminal sequence of the 24-kDa subunit from Bos taurus complex I, and 32% identity with the entire sequence of C. pasteurianum [2Fe-2S] ferredoxin [7].
  • A multiple structure-based sequence alignment has been constructed for the three enzymes and extended to include zeta-crystallin, an eye lens structural protein with quinone oxidoreductase activity and high sequence identity to E. coli quinone oxidoreductase [8].
  • CEL1 was neither an endoglucanase, a cellobiohydrolase able to hydrolyze fluorogenic cellobiosides, a beta-glucosidase, a xylanase, nor a cellobiose: quinone oxidoreductase [9].
  • It seems likely that like FDH-N, FDH-Z functions physiologically as a formate: quinone oxidoreductase [10].
 

Analytical, diagnostic and therapeutic context of qor

References

  1. 2-Haloacrylate reductase, a novel enzyme of the medium chain dehydrogenase/reductase superfamily that catalyzes the reduction of a carbon-carbon double bond of unsaturated organohalogen compounds. Kurata, A., Kurihara, T., Kamachi, H., Esaki, N. J. Biol. Chem. (2005) [Pubmed]
  2. Exploring the membrane domain of the reduced nicotinamide adenine dinucleotide-quinone oxidoreductase of Paracoccus denitrificans: characterization of the NQO7 subunit. Bernardo, S.D., Yano, T., Yagi, T. Biochemistry (2000) [Pubmed]
  3. Membrane Topology Mapping of the Na+-Pumping NADH: Quinone Oxidoreductase from Vibrio cholerae by PhoA- Green Fluorescent Protein Fusion Analysis. Duffy, E.B., Barquera, B. J. Bacteriol. (2006) [Pubmed]
  4. Overproduction, crystallization and preliminary X-ray diffraction analysis of a quinone oxidoreductase from Thermus thermophilus HB8. Shimomura, Y., Sumiguchi-Agari, K., Masui, R., Kuramitsu, S., Fukuyama, K. Acta Crystallogr. D Biol. Crystallogr. (2002) [Pubmed]
  5. Low temperature EPR and MCD studies on cytochrome b-558 of the Bacillus subtilis succinate: quinone oxidoreductase indicate bis-histidine coordination of the heme iron. Fridén, H., Cheesman, M.R., Hederstedt, L., Andersson, K.K., Thomson, A.J. Biochim. Biophys. Acta (1990) [Pubmed]
  6. Crystallization and preliminary X-ray diffraction studies on a soluble Escherichia coli quinone oxidoreductase. Edwards, K.J., Thorn, J.M., Daniher, J.A., Dixon, N.E., Ollis, D.L. J. Mol. Biol. (1994) [Pubmed]
  7. Purification and characterization of the HndA subunit of NADP-reducing hydrogenase from Desulfovibrio fructosovorans overproduced in Escherichia coli. De Luca, G., Asso, M., Belaich, J.P., Dermoun, Z. Biochemistry (1998) [Pubmed]
  8. Structural and sequence comparisons of quinone oxidoreductase, zeta-crystallin, and glucose and alcohol dehydrogenases. Edwards, K.J., Barton, J.D., Rossjohn, J., Thorn, J.M., Taylor, G.L., Ollis, D.L. Arch. Biochem. Biophys. (1996) [Pubmed]
  9. CEL1: a novel cellulose binding protein secreted by Agaricus bisporus during growth on crystalline cellulose. Armesilla, A.L., Thurston, C.F., Yagüe, E. FEMS Microbiol. Lett. (1994) [Pubmed]
  10. A second phenazine methosulphate-linked formate dehydrogenase isoenzyme in Escherichia coli. Pommier, J., Mandrand, M.A., Holt, S.E., Boxer, D.H., Giordano, G. Biochim. Biophys. Acta (1992) [Pubmed]
 
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