the enzyme catalyzes a detoxification process. QR1 gene expression is induced in response to xenobiotics, oxidants, heavy metals, UV light, and ionisation radiation. The enzyme is part of an electrophilic-induced and/or oxidative stress-induced cellular defense mechanism that includes the induction of more than two dozen defensive genes
NAD(P)H:quinone oxidoreductase 1 in pancreatic cell lines metabolizes the heat shock protein 90 inhibitor 17-(allylamino)-17-demethoxygeldanamycin to the corresponding hydroquinone
the enzyme plays an essential role in maintaining a reduced ubiquinone-pool during infection (Plasmodium falciparum is the causative agents of malaria). The enzyme is not only essential to parasite survival in vivo but may also contribute to the severity and outcome of disease. Type II NADH:quinone oxidoreductase the membrane-bound respiratory enzyme differs from the canonical NADH:dehydrogenase (complex I), because it is not involved in the vectorial transfer of protons across membranes. In the electron transport chain of Plasmodium, the canonical multimeric complex I (NADH:dehydrogenase) found in mammalian mitochondria is absent, and, instead, the parasite possesses five quinone-dependent oxidoreductases, namely a type II NADH:quinone oxidoreductase (PfNDH2), a malate: quinone oxidoreductase (MQO), a dihydroorotate dehydrogenase (DHOD), a glycerol-3-phosphate dehydrogenase (G3PDH), and a succinate: quinone oxidoreductase (SDH). These enzymes link cytosolic metabolism to mitochondrial metabolism, generating reducing power (ubiquinol) for the bc1 complex and an aa3-type cytochrome oxidase, enabling proton pumping and energy conservation
NAD(P)H:quinone oxidoreductase 1 in pancreatic cell lines metabolizes the heat shock protein 90 inhibitor 17-(allylamino)-17-demethoxygeldanamycin to the corresponding hydroquinone
NQO1 activity colocalizes closely with Alzheimers disease pathology supporting a presumed role as an antioxidant system upregulated in response to the oxidative stress of the Alzheimers disease process
lack of NQO1 in male mice increases benzene-induced hematotoxicity but not genotoxicity or the DNA damage response. NQO1 appears critical in female mice for detoxifying the metabolites of benzene responsible for genotoxicity, hematotoxicity, and induction of the DNA damage response
the flavoprotein ferric reductase B, FerB, from Paracoccus denitrificans is one of two major enzymes able to reduce Fe(III)-ligand complexes when NADH is the electron donor. The protein is also active as a chromate reductase and, to a substantially greater extent, as a quinone reductase
the flavoprotein ferric reductase B, FerB, from Paracoccus denitrificans is one of two major enzymes able to reduce Fe(III)-ligand complexes when NADH is the electron donor. The protein is also active as a chromate reductase and, to a substantially greater extent, as a quinone reductase
the flavoprotein ferric reductase B, FerB, from Paracoccus denitrificans is one of two major enzymes able to reduce Fe(III)-ligand complexes when NADH is the electron donor. The protein is also active as a chromate reductase and, to a substantially greater extent, as a quinone reductase
the main cytotoxicity mechanism of antitumour aziridinyl-benzoquinones is their two-electron reduction to alkylating products by NAD(P)H:quinone oxidoreductase. In addition to the activation of NQO1 the oxidative stress, presumably initiated by single-electron enzymatic reduction, plays an important role in the cytotoxicity of aziridinyl-substituted quinones