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Volumn 205, Issue 1-4, 1998, Pages 52-58

Molecular characterization of NAD(P)H:quinone oxidoreductase of tobacco leaves

Author keywords

DT diaphorase; NAD(P)H:quinone oxidoreducatse; Nicotiana tabacum; Plasma membrane

Indexed keywords

AMINO ACID SEQUENCE; CELL MEMBRANE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME KINETICS; FLAVODEHYDROGENASE; HYDROQUINONE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE (PHOSPHATE) DEHYDROGENASE (QUINONE); SEMIQUINONE; TOBACCO;

EID: 0032442072     PISSN: 0033183X     EISSN: None     Source Type: Journal    
DOI: 10.1007/bf01279293     Document Type: Conference Paper
Times cited : (7)

References (33)
  • 2
    • 0029138474 scopus 로고
    • Involvement of ascorbic-acid and a b-type cytochrome in plant plasma membrane redox reactions
    • Asard H, Horemans N, Caubergs RJ (1995) Involvement of ascorbic-acid and a b-type cytochrome in plant plasma membrane redox reactions. Protoplasma 184: 36-41
    • (1995) Protoplasma , vol.184 , pp. 36-41
    • Asard, H.1    Horemans, N.2    Caubergs, R.J.3
  • 4
    • 0542444213 scopus 로고    scopus 로고
    • NADH-monodehydroascorbate oxidoreductase is one of the redox enzymes in spinach leaf plasma membranes
    • Bérczi A, Møller IM (1998) NADH-monodehydroascorbate oxidoreductase is one of the redox enzymes in spinach leaf plasma membranes. Plant Physiol 116: 1029-1036
    • (1998) Plant Physiol , vol.116 , pp. 1029-1036
    • Bérczi, A.1    Møller, I.M.2
  • 5
    • 0029059071 scopus 로고
    • Purification and characterization of an NADH hexacyanoferrate(III) reductase from spinach leaf plasma membrane
    • _ Fredlund KM, Møller IM (1995) Purification and characterization of an NADH hexacyanoferrate(III) reductase from spinach leaf plasma membrane. Arch Biochem Biophys 320: 65-72
    • (1995) Arch Biochem Biophys , vol.320 , pp. 65-72
    • Fredlund, K.M.1    Møller, I.M.2
  • 6
    • 0017277818 scopus 로고
    • Assay of proteins in the presence of interfering materials
    • Besandoun A, Weinstein D (1976) Assay of proteins in the presence of interfering materials. Anal Biochem 70: 241-250
    • (1976) Anal Biochem , vol.70 , pp. 241-250
    • Besandoun, A.1    Weinstein, D.2
  • 8
    • 0029153403 scopus 로고
    • Purification and characterization of a 1,4-benzoquinone reductase from the basidiomycete Phanaerochete chrysosporium
    • Brock BJ, Rieble S, Gold MH (1995) Purification and characterization of a 1,4-benzoquinone reductase from the basidiomycete Phanaerochete chrysosporium. Appl Environ Microbiol 61: 3076-3081
    • (1995) Appl Environ Microbiol , vol.61 , pp. 3076-3081
    • Brock, B.J.1    Rieble, S.2    Gold, M.H.3
  • 9
    • 0000324745 scopus 로고    scopus 로고
    • Nitrate reductase biochemistry comes of age
    • Campbell WH (1996) Nitrate reductase biochemistry comes of age. Plant Physiol 111: 355-361
    • (1996) Plant Physiol , vol.111 , pp. 355-361
    • Campbell, W.H.1
  • 10
    • 0029799910 scopus 로고    scopus 로고
    • Enhanced sensitivity of ubiquinone-deficient mutants of Saccharomyces cerevisiae to products of autoxidized polyunsaturated fatty acids
    • Do TQ, Schultz JR, Clarke CF (1996) Enhanced sensitivity of ubiquinone-deficient mutants of Saccharomyces cerevisiae to products of autoxidized polyunsaturated fatty acids. Proc Natl Acad Sci USA 93: 7534-7539
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 7534-7539
    • Do, T.Q.1    Schultz, J.R.2    Clarke, C.F.3
  • 11
    • 0002117840 scopus 로고
    • DT-diaphorase: A historical review
    • Ernster L (1987) DT-diaphorase: a historical review. Chem Scr 27A: 1-13
    • (1987) Chem Scr , vol.27 A , pp. 1-13
    • Ernster, L.1
  • 12
    • 0028317627 scopus 로고
    • Comparison of the stereospecificity and immunoreactivity of NADH-ferricyanide reductases in plant membranes
    • Fredlund KM, Struglics A, Widell S, Askerlund P, Kader JC, Møller IM (1994) Comparison of the stereospecificity and immunoreactivity of NADH-ferricyanide reductases in plant membranes. Plant Physiol 106: 1103-1106
    • (1994) Plant Physiol , vol.106 , pp. 1103-1106
    • Fredlund, K.M.1    Struglics, A.2    Widell, S.3    Askerlund, P.4    Kader, J.C.5    Møller, I.M.6
  • 13
    • 0344711032 scopus 로고
    • Post-column fluorometric detection system for liquid chromatographic analysis of amino and imino acids using o-phthalaldehyde/N-acetyl-L-cysteine reagent
    • Fujiara M, Ishida Y, Nimura N, Toyama A, Kinoshita T (1987) Post-column fluorometric detection system for liquid chromatographic analysis of amino and imino acids using o-phthalaldehyde/N-acetyl-L-cysteine reagent. Anal Biochem 16: 672-678
    • (1987) Anal Biochem , vol.16 , pp. 672-678
    • Fujiara, M.1    Ishida, Y.2    Nimura, N.3    Toyama, A.4    Kinoshita, T.5
  • 14
    • 0028035818 scopus 로고
    • The effect of calcium chelators on microsonial pyridine nucleotide-linkcd dehydrogenases of sugarbeet cells
    • Guerrini F, Lombini A, Bizarri M, Pupillo P (1994) The effect of calcium chelators on microsonial pyridine nucleotide-linkcd dehydrogenases of sugarbeet cells. J Exp Bot 45: 1227-1233
    • (1994) J Exp Bot , vol.45 , pp. 1227-1233
    • Guerrini, F.1    Lombini, A.2    Bizarri, M.3    Pupillo, P.4
  • 15
    • 0002783125 scopus 로고
    • On the mechanism of one- and two-electron transfer by flavin enzymes
    • Iyanagi T (1987) On the mechanism of one- and two-electron transfer by flavin enzymes. Chem Scr 27A: 31-36
    • (1987) Chem Scr , vol.27 A , pp. 31-36
    • Iyanagi, T.1
  • 16
    • 0014842505 scopus 로고
    • One-electron transfer reactions in biochemical systems V: Difference in the mechanism of quinone reduction by the NADH dehydrogenase and the NAD(P)H dehydrogenase (DT-diaphorase)
    • _ Yamazaki I (1970) One-electron transfer reactions in biochemical systems V: difference in the mechanism of quinone reduction by the NADH dehydrogenase and the NAD(P)H dehydrogenase (DT-diaphorase). Biochim Biophys Acta 216: 282-294
    • (1970) Biochim Biophys Acta , vol.216 , pp. 282-294
    • Yamazaki, I.1
  • 17
    • 0030829510 scopus 로고    scopus 로고
    • Evidence for the presence of GPI-anchored PM-NR in leaves of Beta vulgaris and for PM-NR in barley leaves
    • Kunze M, Riedel J, Lange V, Hurwitz R, Tischner R (1997) Evidence for the presence of GPI-anchored PM-NR in leaves of Beta vulgaris and for PM-NR in barley leaves. Plant Physiol Biochem 35: 507-512
    • (1997) Plant Physiol Biochem , vol.35 , pp. 507-512
    • Kunze, M.1    Riedel, J.2    Lange, V.3    Hurwitz, R.4    Tischner, R.5
  • 18
    • 0028305406 scopus 로고
    • Isolation of highly purified plant plasma membranes and separation of inside-out and right-side out vesicles
    • Larsson C, Sommarin M, Widell S (1994) Isolation of highly purified plant plasma membranes and separation of inside-out and right-side out vesicles. Methods Enzymol 228: 451-469
    • (1994) Methods Enzymol , vol.228 , pp. 451-469
    • Larsson, C.1    Sommarin, M.2    Widell, S.3
  • 19
    • 0029068515 scopus 로고
    • The three dimensional structure of NAD(P)H:quinone reductase, a flavoprotein involved in cancer chemoprotection and chemotherapy: Mechanism of the two-electron reduction
    • Li R, Bianchet MA, Talalay P, Amzel LM (1995) The three dimensional structure of NAD(P)H:quinone reductase, a flavoprotein involved in cancer chemoprotection and chemotherapy: mechanism of the two-electron reduction. Proc Natl Acad Sci USA 92: 8846-8850
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 8846-8850
    • Li, R.1    Bianchet, M.A.2    Talalay, P.3    Amzel, L.M.4
  • 20
    • 0001586031 scopus 로고
    • Purification and identification of a plasma membrane associated electron transport protein from maize (Zea mays) roots
    • Luster DG, Buckhout TJ (1989) Purification and identification of a plasma membrane associated electron transport protein from maize (Zea mays) roots. Plant Physiol 91: 1014-1019
    • (1989) Plant Physiol , vol.91 , pp. 1014-1019
    • Luster, D.G.1    Buckhout, T.J.2
  • 23
    • 0001143581 scopus 로고
    • On the mechanism of induction of cancer protective enzymes: A unifying proposal
    • Prochaska HJ, De Long MJ, Talalay P (1985) On the mechanism of induction of cancer protective enzymes: a unifying proposal. Proc Natl Acad Sci USA 82: 8232-8236
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 8232-8236
    • Prochaska, H.J.1    De Long, M.J.2    Talalay, P.3
  • 24
    • 0000569854 scopus 로고
    • Plant cell fractionation
    • Quail PH (1979) Plant cell fractionation. Annu Rev Plant Physiol 30: 425-484
    • (1979) Annu Rev Plant Physiol , vol.30 , pp. 425-484
    • Quail, P.H.1
  • 26
    • 0028140643 scopus 로고
    • Purification and characterization of two distinct NAD(P)H dehydrogenases from onion (Allium cepa L.) root plasma membrane
    • Serrano A, Cordoba F, Gonzales-Reyes JA, Navas P, Villalba JM (1994) Purification and characterization of two distinct NAD(P)H dehydrogenases from onion (Allium cepa L.) root plasma membrane. Plant Physiol 106: 87-96
    • (1994) Plant Physiol , vol.106 , pp. 87-96
    • Serrano, A.1    Cordoba, F.2    Gonzales-Reyes, J.A.3    Navas, P.4    Villalba, J.M.5
  • 27
    • 0030739681 scopus 로고    scopus 로고
    • The reduction of α-tocopherolquinone by human NAD(P)H:quinone oxidoreductase: The role of α-tocopherolhydroquinone as a cellular antioxidant
    • Siegel D, Bolton EM, Burr JA, Liebler DC, Ross D (1997) The reduction of α-tocopherolquinone by human NAD(P)H:quinone oxidoreductase: the role of α-tocopherolhydroquinone as a cellular antioxidant. Mol Pharmacol 52: 300-305
    • (1997) Mol Pharmacol , vol.52 , pp. 300-305
    • Siegel, D.1    Bolton, E.M.2    Burr, J.A.3    Liebler, D.C.4    Ross, D.5
  • 28
    • 0029914199 scopus 로고    scopus 로고
    • NAD(P)H:(quinone-acceptor) oxidoreductase of tobacco leaves is an FMN containing flavoenzyme
    • Sparla F, Tedeschi G, Trost P (1996) NAD(P)H:(quinone-acceptor) oxidoreductase of tobacco leaves is an FMN containing flavoenzyme. Plant Physiol 112: 249-258
    • (1996) Plant Physiol , vol.112 , pp. 249-258
    • Sparla, F.1    Tedeschi, G.2    Trost, P.3
  • 30
    • 0002631342 scopus 로고
    • Characterization of the plasma membrane hound nitrate reductase in Chlorella saccharophila (Krüger) Nadson
    • Stöhr C, Tischner R, Ward MR (1993) Characterization of the plasma membrane hound nitrate reductase in Chlorella saccharophila (Krüger) Nadson. Planta 191: 79-85
    • (1993) Planta , vol.191 , pp. 79-85
    • Stöhr, C.1    Tischner, R.2    Ward, M.R.3
  • 31
    • 0028834798 scopus 로고
    • Purification and properties of NAD(P)H:(quinone-acceptor) oxidoreductase of sugarbeet cells
    • Trost P, Bonora P, Scagliarini S, Pupillo P (1995) Purification and properties of NAD(P)H:(quinone-acceptor) oxidoreductase of sugarbeet cells. Eur J Biochem 234: 452-458
    • (1995) Eur J Biochem , vol.234 , pp. 452-458
    • Trost, P.1    Bonora, P.2    Scagliarini, S.3    Pupillo, P.4
  • 32
    • 0031397296 scopus 로고    scopus 로고
    • Dissecting the diphenylene iodonium-sensitive NAD(P)H:quinone oxidoreductase of Cucurbita plasma membrane
    • _ Foscarini S, Preger V, Bonora P, Vitale L, Pupillo P (1997) Dissecting the diphenylene iodonium-sensitive NAD(P)H:quinone oxidoreductase of Cucurbita plasma membrane. Plant Physiol 114: 737-746
    • (1997) Plant Physiol , vol.114 , pp. 737-746
    • Foscarini, S.1    Preger, V.2    Bonora, P.3    Vitale, L.4    Pupillo, P.5
  • 33
    • 0001943767 scopus 로고
    • NAD(P)H-duroquinone reductase in the plant plasma membrane
    • Valenti V, Guerrini F, Pupillo P (1990) NAD(P)H-duroquinone reductase in the plant plasma membrane. J Exp Bot 223: 183-192
    • (1990) J Exp Bot , vol.223 , pp. 183-192
    • Valenti, V.1    Guerrini, F.2    Pupillo, P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.