메뉴 건너뛰기




Volumn 42, Issue 7, 2003, Pages 1985-1994

Kinetic and docking studies of the interaction of quinones with the quinone reductase active site

Author keywords

[No Author keywords available]

Indexed keywords

CELLS; CORRELATION METHODS; CYTOLOGY; ELECTRONS; REACTION KINETICS; REDUCTION;

EID: 0345270443     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi026518s     Document Type: Article
Times cited : (27)

References (33)
  • 1
    • 0034724218 scopus 로고    scopus 로고
    • Structures of recombinant mouse and human Nad(P)H:Quinone Oxidoreductases: Species comparison and structural changes with substrate binding and release
    • Faig, M., Bianchet, M. A., Chen, S., Winski, S., Ross, D., Talalay, P., and Amzel, L. M. (2000) Structures of Recombinant Mouse and Human Nad(P)H:Quinone Oxidoreductases: Species Comparison and Structural Changes with Substrate Binding and Release, Proc. Natl. Acad. Sci. U.S.A. 97, 3177-3182.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 3177-3182
    • Faig, M.1    Bianchet, M.A.2    Chen, S.3    Winski, S.4    Ross, D.5    Talalay, P.6    Amzel, L.M.7
  • 2
    • 0014842505 scopus 로고
    • One electron transfer reactions in biochemical systems. V. Difference in the mechanism of quinone reductase by the NADH dehydrogenase and the NAD(P)H dehydrogenase (DT-diaphorase)
    • Iyanagi, T., and Yamazaki, I. (1970) One electron transfer reactions in biochemical systems. V. Difference in the mechanism of quinone reductase 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
    • Iyanagi, T.1    Yamazaki, I.2
  • 3
    • 0034531564 scopus 로고    scopus 로고
    • NAD(P)H:quinone oxidoreductase 1 (NQO1): Chemoprotection, bioactivation, gene regulation and genetic polymorphisms
    • Ross, D., Kepa, J. K., Winski, S. L., Beall, H. D., Anwar, A., and Siegel, D. (2000) NAD(P)H:quinone oxidoreductase 1 (NQO1): chemoprotection, bioactivation, gene regulation and genetic polymorphisms, Chem.-Biol. Interact. 129, 77-97.
    • (2000) Chem.-Biol. Interact. , vol.129 , pp. 77-97
    • Ross, D.1    Kepa, J.K.2    Winski, S.L.3    Beall, H.D.4    Anwar, A.5    Siegel, D.6
  • 4
    • 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, M. A., Talalay, P., and Amzel, L. M. (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. U.S.A. 92, 8846-8850.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 8846-8850
    • Li, R.1    Bianchet, M.A.2    Talalay, P.3    Amzel, L.M.4
  • 5
    • 0032741789 scopus 로고    scopus 로고
    • Crystal structure of human DT-diaphorase: A model for interaction with the cytotoxic drug 5-(Aziridin-1-yl)-2,4-dinitrobenzamide (CB1954)
    • Skelly, J. V., Sanderson, M. R., Suter, D. A., Baumann, U., Read, M. A., Gregory, D. S. J., Bennett, M., Hobbs, S. M., and Neidle, S. (1999) Crystal structure of human DT-diaphorase: a model for interaction with the cytotoxic drug 5-(Aziridin-1-yl)-2,4-dinitrobenzamide (CB1954), J. Med. Chem. 42, 4325-4330.
    • (1999) J. Med. Chem. , vol.42 , pp. 4325-4330
    • Skelly, J.V.1    Sanderson, M.R.2    Suter, D.A.3    Baumann, U.4    Read, M.A.5    Gregory, D.S.J.6    Bennett, M.7    Hobbs, S.M.8    Neidle, S.9
  • 6
    • 33947345493 scopus 로고
    • The reaction between quinines and sodium enolate. V. 2,3-dimethylnaphthoquinone and sodium malonic ester
    • Smith, L. I., and Webster, I. M. (1937) The reaction between quinines and sodium enolate. V. 2,3-dimethylnaphthoquinone and sodium malonic ester, J. Am. Chem. Soc. 59, 662-667.
    • (1937) J. Am. Chem. Soc. , vol.59 , pp. 662-667
    • Smith, L.I.1    Webster, I.M.2
  • 7
    • 0024207283 scopus 로고
    • Purification and crystallization of rat liver NAD(P)H:(quinone-acceptor) oxidoreductase by cibacron blue affinity chromatography: Identification of a new and potent inhibitor
    • Prochaska, H. J. (1988) Purification and crystallization of rat liver NAD(P)H:(quinone-acceptor) oxidoreductase by cibacron blue affinity chromatography: identification of a new and potent inhibitor, Biochem. Biophys. 267, 529-538.
    • (1988) Biochem. Biophys. , vol.267 , pp. 529-538
    • Prochaska, H.J.1
  • 8
    • 0016281487 scopus 로고
    • Properties and reaction mechanism of DT diaphorase from rat liver
    • Hosada, S., Nakamura, W., and Hayashi, K. (1974) Properties and Reaction mechanism of DT Diaphorase from Rat Liver, J. Biol. Chem. 249, 6416-6423.
    • (1974) J. Biol. Chem. , vol.249 , pp. 6416-6423
    • Hosada, S.1    Nakamura, W.2    Hayashi, K.3
  • 9
    • 0023930873 scopus 로고
    • Direct measurement of NAD(P)H:quinone reductase from cells cultured in microtiter wells: A screening assay for anticarcinogenic enzyme inducers
    • Prochaska, H. J., and Santamaria, A. B. (1988) Direct measurement of NAD(P)H:quinone reductase from cells cultured in microtiter wells: a screening assay for anticarcinogenic enzyme inducers, Anal. Biochem. 169, 328-336.
    • (1988) Anal. Biochem. , vol.169 , pp. 328-336
    • Prochaska, H.J.1    Santamaria, A.B.2
  • 10
    • 84962359221 scopus 로고    scopus 로고
    • Ab initio study of solvated molecules: A new implementation of the polarizable continuum model
    • Cossi, M., Barone, V., Camni, R., and Tomasi, J. (1996) Ab initio study of solvated molecules: a new implementation of the polarizable continuum model, Chem. Phys. Lett. 255, 327-335.
    • (1996) Chem. Phys. Lett. , vol.255 , pp. 327-335
    • Cossi, M.1    Barone, V.2    Camni, R.3    Tomasi, J.4
  • 11
    • 11744256643 scopus 로고
    • Molecular interactions in solution: An overview of methods based on continuous distributions of the solvent
    • Tomasi, J., and Perisco, M. (1994) Molecular interactions in solution: an overview of methods based on continuous distributions of the solvent, Chem. Rev. 94, 2027-2094.
    • (1994) Chem. Rev. , vol.94 , pp. 2027-2094
    • Tomasi, J.1    Perisco, M.2
  • 12
    • 11644261806 scopus 로고    scopus 로고
    • Automated docking using a lamarckian genetic algorithm and empirical binding free energy function
    • Morris, G. M., Goodsell, D. S., Halliday, R. S., Huey, R., Hart, W. E., Belew, R. K., and Olson, A. J. (1998) Automated Docking Using a Lamarckian Genetic Algorithm and Empirical Binding Free Energy Function, J. Comput. Chem. 19, 1639-1662.
    • (1998) J. Comput. Chem. , vol.19 , pp. 1639-1662
    • Morris, G.M.1    Goodsell, D.S.2    Halliday, R.S.3    Huey, R.4    Hart, W.E.5    Belew, R.K.6    Olson, A.J.7
  • 14
    • 0019525292 scopus 로고
    • Minimization by Random search techniques
    • Solis, F. J., and Wets, R. J. (1981) Minimization by Random search techniques, Math. Oper. Res. 6, 19-30.
    • (1981) Math. Oper. Res. , vol.6 , pp. 19-30
    • Solis, F.J.1    Wets, R.J.2
  • 15
    • 0026110673 scopus 로고
    • The inclusion of electrostatic hydration energies in molecular mechanics calculations
    • Gilson, M. K., and Honig, B. (1991) The inclusion of electrostatic hydration energies in molecular mechanics calculations, J. Comput.-Aided Mol. Des. 5, 5-20.
    • (1991) J. Comput.-Aided Mol. Des. , vol.5 , pp. 5-20
    • Gilson, M.K.1    Honig, B.2
  • 16
    • 84986439462 scopus 로고
    • Molecular dynamics simulation with a continuum electrostatic model of the solvent
    • Gilson, M. K., McCammon, J. A., and Madura, J. D. (1995) Molecular dynamics simulation with a continuum electrostatic model of the solvent, J. Comput. Chem. 16, 1081-1095.
    • (1995) J. Comput. Chem. , vol.16 , pp. 1081-1095
    • Gilson, M.K.1    McCammon, J.A.2    Madura, J.D.3
  • 17
    • 0036973992 scopus 로고    scopus 로고
    • Binding free energy of selected anticancer compounds to DNA-theoretical calculations
    • Baginski, M., Polucci, P., Antonini, I., and Martelli, S. (2002) Binding free energy of selected anticancer compounds to DNA-theoretical calculations, J. Mol. Model. 8, 24-32.
    • (2002) J. Mol. Model. , vol.8 , pp. 24-32
    • Baginski, M.1    Polucci, P.2    Antonini, I.3    Martelli, S.4
  • 19
    • 0034084991 scopus 로고    scopus 로고
    • Combined molecular mechanical and continuum solvent approach (MM-PBSA/GBSA) to predict ligand binding
    • Massova, I., and Kollman, P. A. (2000) Combined molecular mechanical and continuum solvent approach (MM-PBSA/GBSA) to predict ligand binding, Perspect. Drug Discovery Des. 18, 113-135.
    • (2000) Perspect. Drug Discovery Des. , vol.18 , pp. 113-135
    • Massova, I.1    Kollman, P.A.2
  • 20
    • 84986486656 scopus 로고
    • A rapid finite difference algorithm, utilizing successive over-relaxation to solve the Poisson-Boltzmann equation
    • Nicholls, A., and Honig, B. (1991) A rapid finite difference algorithm, utilizing successive over-relaxation to solve the Poisson-Boltzmann equation, J. Comput. Chem. 12, 435-445.
    • (1991) J. Comput. Chem. , vol.12 , pp. 435-445
    • Nicholls, A.1    Honig, B.2
  • 21
    • 32844457567 scopus 로고
    • Accurate calculation of hydration free energies using macroscopic solvent models
    • Sitkoff, D., Sharp, K. A., and Honig, B. (1994) Accurate Calculation of Hydration Free Energies Using Macroscopic Solvent Models, J. Phys. Chem. 98, 1978-1988.
    • (1994) J. Phys. Chem. , vol.98 , pp. 1978-1988
    • Sitkoff, D.1    Sharp, K.A.2    Honig, B.3
  • 22
    • 18744390749 scopus 로고    scopus 로고
    • Docking of non-nucleoside inhibitors: Neotripterifordin and its derivatives to HIV-1 reverse transcriptase
    • Zhou, Z., Madrid, M., and Madura, J. D. (2002) Docking of Non-nucleoside Inhibitors: Neotripterifordin and its Derivatives to HIV-1 Reverse Transcriptase, Proteins: Struct., Funct., Genet. 49, 529-542.
    • (2002) Proteins: Struct., Funct., Genet. , vol.49 , pp. 529-542
    • Zhou, Z.1    Madrid, M.2    Madura, J.D.3
  • 27
    • 0026762694 scopus 로고
    • Expression of rat liver NAD(P)H:quinone-acceptor oxidoreductase in Escherichia coli and mutagenesis in vitro at Arg-177
    • Chen, H. H., Ma, J. X., Forrest, G. L., Deng, P. S., Martino, P. A., Lee, T. D., and Chen, S. (1992) Expression of rat liver NAD(P)H:quinone-acceptor oxidoreductase in Escherichia coli and mutagenesis in vitro at Arg-177, Biochem. J. 284, 855-860.
    • (1992) Biochem. J. , vol.284 , pp. 855-860
    • Chen, H.H.1    Ma, J.X.2    Forrest, G.L.3    Deng, P.S.4    Martino, P.A.5    Lee, T.D.6    Chen, S.7
  • 28
    • 0030456586 scopus 로고    scopus 로고
    • The cumulative electrostatic effect of aromatic ring stacking interactions and the negative electrostatic environment of the flavin mononucleotide binding site is a major determinant of the reduction potential for the flavodoxin from Desulfovibrio vulgaris
    • Zhou, Z., and Swenson, R. P. (1996) The cumulative electrostatic effect of aromatic ring stacking interactions and the negative electrostatic environment of the flavin mononucleotide binding site is a major determinant of the reduction potential for the flavodoxin from Desulfovibrio vulgaris, Biochemistry 35, 15980-15988.
    • (1996) Biochemistry , vol.35 , pp. 15980-15988
    • Zhou, Z.1    Swenson, R.P.2
  • 29
    • 0026567982 scopus 로고
    • NAD(P)H (quinone acceptor) oxidoreductase (DT-diaphorase)-mediated two-electron reduction of anthraquinone-based antitumor agents and generation of hydroxyl radicals
    • Fisher, G. R., Gutierrez, P. L., Oldcorne, M. A., and Patterson, L. H. (1992) NAD(P)H (quinone acceptor) oxidoreductase (DT-diaphorase)-mediated two-electron reduction of anthraquinone-based antitumor agents and generation of hydroxyl radicals, Biochem. Pharmacol. 43, 575-585.
    • (1992) Biochem. Pharmacol. , vol.43 , pp. 575-585
    • Fisher, G.R.1    Gutierrez, P.L.2    Oldcorne, M.A.3    Patterson, L.H.4
  • 30
    • 0031026290 scopus 로고    scopus 로고
    • Molecular basis of the catalytic differences among DT-diaphorase of human, rat and mouse
    • Chen, S., Knox, R., Wu, K., Deng, P. S.-K., Zhou, D., Blanchet, M. A., and Amzel, L. M. (1997) Molecular Basis of the catalytic differences among DT-diaphorase of Human, Rat and Mouse, J. Biol. Chem. 272, 1437-1439.
    • (1997) J. Biol. Chem. , vol.272 , pp. 1437-1439
    • Chen, S.1    Knox, R.2    Wu, K.3    Deng, P.S.-K.4    Zhou, D.5    Blanchet, M.A.6    Amzel, L.M.7
  • 31
    • 0001227655 scopus 로고
    • The nature of π-π interactions
    • Hunter, C. A., and Sanders, K. M. (1990) The nature of π-π interactions, J. Am. Chem. Soc. 112, 5525-5534.
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 5525-5534
    • Hunter, C.A.1    Sanders, K.M.2
  • 32
    • 0037075837 scopus 로고    scopus 로고
    • A comprehensive study of the active site residues of DT-diaphorase: Rational design of benzimidazolediones as DT-diaphorase substrates
    • Suleman, A., and Skibo, E. B. (2002) A Comprehensive Study of the Active Site Residues of DT-Diaphorase: Rational Design of Benzimidazolediones as DT-Diaphorase Substrates, J. Med. Chem. 45, 1211-1220.
    • (2002) J. Med. Chem. , vol.45 , pp. 1211-1220
    • Suleman, A.1    Skibo, E.B.2
  • 33
    • 0030739681 scopus 로고    scopus 로고
    • The reduction of alpha-tocopherolquinone by human NAD(P)H:quinone oxidoreductase: The role of alpha-tocopherol-hydroquinone as a cellular antioxidant
    • Siegel, D., Bolton, E. M., Burr, J. A., Liebler, D. C., and Ross, D. (1997) The reduction of alpha-tocopherolquinone by human NAD(P)H:quinone oxidoreductase: the role of alpha-tocopherol-hydroquinone 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.