The plasma membrane NADH oxidase of HeLa cells has hydroquinone oxidase activity.

@article{Kishi1999ThePM,
  title={The plasma membrane NADH oxidase of HeLa cells has hydroquinone oxidase activity.},
  author={Takeo Kishi and Dorothy M. Morr{\'e} and D. James Morré},
  journal={Biochimica et biophysica acta},
  year={1999},
  volume={1412 1},
  pages={
          66-77
        }
}
The plasma membrane NADH oxidase activity partially purified from the surface of HeLa cells exhibited hydroquinone oxidase activity. The preparations completely lacked NADH:ubiquinone reductase activity. However, in the absence of NADH, reduced coenzyme Q10 (Q10H2=ubiquinol) was oxidized at a rate of 15+/-6 nmol min-1 mg protein-1 depending on degree of purification. The apparent Km for Q10H2 oxidation was 33 microM. Activities were inhibited competitively by the cancer cell-specific NADH… Expand
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References

SHOWING 1-10 OF 60 REFERENCES
NADH oxidase of plasma membranes
TLDR
Because of its low basal activity, stimulation by growth factors and hormones, and the inhibition of growth in direct proportion to inhibition of the oxidase, the activity is a candidate as a rate-limiting step in the growth process. Expand
Requirement for coenzyme Q in plasma membrane electron transport.
TLDR
Evidence is consistent with a function for coenzyme Q in a trans-plasma membrane electron transport system which influences cell growth in rat hepatocyte and human erythrocyte plasma membranes. Expand
A growth factor- and hormone-stimulated NADH oxidase from rat liver plasma membrane.
TLDR
Evidence suggests that NADH oxidase of the plasma membrane is a unique oxidoreductase and may be important to the regulation of cell growth. Expand
Characterization of NADPH-dependent ubiquinone reductase activity in rat liver cytosol: effect of various factors on ubiquinone-reducing activity and discrimination from other quinone reductases.
TLDR
Results indicated that the NADPH-UQ reductase in rat liver cytosol is a flavoprotein that reduces UQ-10 by a two-electron reduction mechanism and is distinguishable from known microsomal and mitochondrial enzymes, as well as DT-diaphorase. Expand
NADH oxidase activity of HeLa plasma membranes inhibited by the antitumor sulfonylurea N-(4-methylphenylsulfonyl)-N'-(4-chlorophenyl) urea (LY181984) at an external site.
  • D. Morré
  • Chemistry, Medicine
  • Biochimica et biophysica acta
  • 1995
TLDR
It is demonstrated that the NADH oxidation site inhibited as a result of binding the active antitumor sulfonylurea LY181984 is at the external cell surface, which suggests two NADH sites or activity isoforms for the plasma membrane NADH oxidase. Expand
Reduction of ubiquinone in membrane lipids by rat liver cytosol and its involvement in the cellular defence system against lipid peroxidation.
TLDR
The NADPH-UQ reductase in cytosol was presumed to be responsible for maintaining the steady-state redox levels of intrACEllular UQ and thereby to act as an endogenous antioxidant in protecting intracellular membranes from lipid peroxidation that is inevitably induced in aerobic metabolism. Expand
Auxin-Stimulated NADH Oxidase Purified from Plasma Membrane of Soybean.
NADH oxidation by plasma membrane vesicles purified from hypocotyls of etiolated soybean seedlings by two-phase partition was stimulated 2- to 3-fold by auxins, indole-3-acetic acid,Expand
A drug-responsive and protease-resistant peripheral NADH oxidase complex from the surface of HeLa S cells.
Our laboratory described a ca. 34-kDa protein of the HeLa S cell surface that bound an antitumor sulfonylurea N-(4-methylphenylsulfonyl)-N'-(4-chlorophenyl) urea (LY181984) with high affinity andExpand
The Hormone-responsive NADH Oxidase of the Plant Plasma Membrane Has Properties of a NADH:Protein Disulfide Reductase*
TLDR
A cell surface location of the affected thiols demonstrated with detergents and impermeant thiol reagents suggests that the protein may have a different physiological role than oxidation of NADH, and may carry out some other role more closely related to the function of the auxin hormones in cell enlargement. Expand
Hormone- and growth factor-stimulated NADH oxidase
  • D. Morré
  • Biology, Medicine
  • Journal of bioenergetics and biomembranes
  • 1994
TLDR
A model is presented where the NADH oxidase functions as a thiol-disulfide oxidoreductase activity involved in the formation and breakage of disulfide bonds, postulated as being associated with physical membrane displacement as encountered in cell enlargement or in vesicle budding. Expand
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