메뉴 건너뛰기




Volumn 45, Issue 9, 2006, Pages 2940-2950

Comparison of the binding and reactivity of plant and mammalian peroxidases to indole derivatives by computational docking

Author keywords

[No Author keywords available]

Indexed keywords

BIODIVERSITY; BIOSYNTHESIS; CATALYSIS; ENZYMES; OXIDATION; PROTEINS; SUBSTRATES;

EID: 33644671184     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi051510e     Document Type: Article
Times cited : (29)

References (34)
  • 2
    • 0742324902 scopus 로고    scopus 로고
    • Horseradish peroxidase: A modern view of a classic enzyme
    • Veitch, N. C. (2004) Horseradish peroxidase: A modern view of a classic enzyme, Phytochemistry 65, 249-259.
    • (2004) Phytochemistry , vol.65 , pp. 249-259
    • Veitch, N.C.1
  • 3
    • 18244390487 scopus 로고    scopus 로고
    • Myeloperoxidase: Friend and foe
    • Klebanoff, S. J. (2005) Myeloperoxidase: Friend and foe, J. Leukocyte Biol. 77, 598-625.
    • (2005) J. Leukocyte Biol. , vol.77 , pp. 598-625
    • Klebanoff, S.J.1
  • 4
    • 0034697020 scopus 로고    scopus 로고
    • X-ray crystal structure and characterization of halide-binding sites of human myeloperoxidase at 1.8 Å resolution
    • Fiedler, T. J., Davey, C. A., and Fenna, R. E. (2000) X-ray crystal structure and characterization of halide-binding sites of human myeloperoxidase at 1.8 Å resolution, J. Biol. Chem. 275, 11964-11971.
    • (2000) J. Biol. Chem. , vol.275 , pp. 11964-11971
    • Fiedler, T.J.1    Davey, C.A.2    Fenna, R.E.3
  • 6
    • 18944406318 scopus 로고    scopus 로고
    • Peroxidases: A role in the metabolism and side effects of drugs
    • Tafazoli, S., and O'Brien, P. J. (2005) Peroxidases: A role in the metabolism and side effects of drugs, Drug Discovery Today 10, 617-625.
    • (2005) Drug Discovery Today , vol.10 , pp. 617-625
    • Tafazoli, S.1    O'Brien, P.J.2
  • 9
    • 4644244154 scopus 로고    scopus 로고
    • Oxidation of melatonin and its catabolites, N1-acetyl-N2-formyl-5- methoxykynuramine and N1-acetyl-5-methoxykynuramine, by activated leukocytes
    • Silva, S. O., Rodrigues, M. R., Carvalho, S. R., Catalani, L. H., Campa, A., and Ximenes, V. F. (2004) Oxidation of melatonin and its catabolites, N1-acetyl-N2-formyl-5-methoxykynuramine and N1-acetyl-5-methoxykynuramine, by activated leukocytes, J. Pineal Res. 37, 171-175.
    • (2004) J. Pineal Res. , vol.37 , pp. 171-175
    • Silva, S.O.1    Rodrigues, M.R.2    Carvalho, S.R.3    Catalani, L.H.4    Campa, A.5    Ximenes, V.F.6
  • 10
    • 0037216933 scopus 로고    scopus 로고
    • A model of the oscillatory metabolism of activated neutrophils
    • Olsen, L. F., Kummer, U., Kindelzkii, A. L., and Petty, H. R. (2003) A Model of the Oscillatory Metabolism of Activated Neutrophils, Biophys. J. 84, 69-81.
    • (2003) Biophys. J. , vol.84 , pp. 69-81
    • Olsen, L.F.1    Kummer, U.2    Kindelzkii, A.L.3    Petty, H.R.4
  • 11
    • 0042823653 scopus 로고    scopus 로고
    • Concerted simulations reveal how peroxidase compound III formation results in cellular oscillations
    • Gabdoulline, R. R., Kummer, U., Olsen, L. F., and Wade, R. C. (2003) Concerted Simulations Reveal How Peroxidase Compound III Formation Results in Cellular Oscillations, Biophys. J. 85, 1421-1428.
    • (2003) Biophys. J. , vol.85 , pp. 1421-1428
    • Gabdoulline, R.R.1    Kummer, U.2    Olsen, L.F.3    Wade, R.C.4
  • 12
    • 0036478818 scopus 로고    scopus 로고
    • Redox intermediates of plant and mammalian peroxidases: A comparative transient-kinetic study of their reactivity toward indole derivatives
    • Jantschko, W., Furtmüller, P. G., Allegra, M., Livrea, M. A., Jakopitsch, C., Regelsberger, G., and Obinger, C. (2002) Redox Intermediates of Plant and Mammalian Peroxidases: A Comparative Transient-Kinetic Study of Their Reactivity Toward Indole Derivatives, Arch. Biochem. Biophys. 398, 12-22.
    • (2002) Arch. Biochem. Biophys. , vol.398 , pp. 12-22
    • Jantschko, W.1    Furtmüller, P.G.2    Allegra, M.3    Livrea, M.A.4    Jakopitsch, C.5    Regelsberger, G.6    Obinger, C.7
  • 13
    • 0035860288 scopus 로고    scopus 로고
    • Oxidation of melatonin and tryptophan by an HRP cycle involving compound III
    • Ximenes, V. F., Catalani, L. H., and Campa, A. (2001) Oxidation of melatonin and tryptophan by an HRP cycle involving compound III, Biochem. Biophys. Res. Commun. 287, 130-134.
    • (2001) Biochem. Biophys. Res. Commun. , vol.287 , pp. 130-134
    • Ximenes, V.F.1    Catalani, L.H.2    Campa, A.3
  • 15
    • 0037423684 scopus 로고    scopus 로고
    • Redox properties of the couples compound I/compound II and compound II/native enzyme of human myeloperoxidase
    • Furtmüller, P. G., Arnhold, J., Jantschko, W., Pichler, H., and Obinger, C. (2003) Redox properties of the couples compound I/compound II and compound II/native enzyme of human myeloperoxidase, Biochem. Biophys. Res. Commun. 301, 551-557.
    • (2003) Biochem. Biophys. Res. Commun. , vol.301 , pp. 551-557
    • Furtmüller, P.G.1    Arnhold, J.2    Jantschko, W.3    Pichler, H.4    Obinger, C.5
  • 16
    • 0028925951 scopus 로고
    • Variable temperature spectroelectrochemical study of horseradish peroxidase
    • Farhangrazi, Z. S., Fossett, M. E., Powers, L. S., and Ellis, W. R., Jr. (1995) Variable temperature spectroelectrochemical study of horseradish peroxidase, Biochemistry 34, 2866-2871.
    • (1995) Biochemistry , vol.34 , pp. 2866-2871
    • Farhangrazi, Z.S.1    Fossett, M.E.2    Powers, L.S.3    Ellis Jr., W.R.4
  • 17
    • 0033429040 scopus 로고    scopus 로고
    • Kinetics of oxidation of serotonin by myeloperoxidase compounds I and II
    • Dunford, H. B., and Hsuanyu, Y. (1999) Kinetics of oxidation of serotonin by myeloperoxidase compounds I and II, Biochem. Cell Biol. 77, 449-457.
    • (1999) Biochem. Cell Biol. , vol.77 , pp. 449-457
    • Dunford, H.B.1    Hsuanyu, Y.2
  • 18
    • 0034038196 scopus 로고    scopus 로고
    • Electrochemical oxidation of histamine and serotonin at highly boron-doped diamond electrodes
    • Sarada, B. V., Rao, T. N., Tryk, D. A., and Fujishima, A. (2000) Electrochemical oxidation of histamine and serotonin at highly boron-doped diamond electrodes, Anal. Chem. 72, 1632-1638.
    • (2000) Anal. Chem. , vol.72 , pp. 1632-1638
    • Sarada, B.V.1    Rao, T.N.2    Tryk, D.A.3    Fujishima, A.4
  • 19
    • 0033521007 scopus 로고    scopus 로고
    • The structures of the horseradish peroxidase C-ferulic acid complex and the ternary complex with cyanide suggest how peroxidases oxidize small phenolic substrates
    • Henriksen, A., Smith, A. T., and Gajhede, M. (1999) The Structures of the Horseradish Peroxidase C-Ferulic Acid Complex and the Ternary Complex with Cyanide Suggest How Peroxidases Oxidize Small Phenolic Substrates, J. Biol. Chem. 274, 35005-35011.
    • (1999) J. Biol. Chem. , vol.274 , pp. 35005-35011
    • Henriksen, A.1    Smith, A.T.2    Gajhede, M.3
  • 21
    • 0021871375 scopus 로고
    • A computational procedure for determining energetically favorable binding sites on biologically important macromolecules
    • Goodford, P. J. (1985) A computational procedure for determining energetically favorable binding sites on biologically important macromolecules, J. Med. Chem. 28, 849-857.
    • (1985) J. Med. Chem. , vol.28 , pp. 849-857
    • Goodford, P.J.1
  • 22
    • 0028020953 scopus 로고
    • Molecular dynamics studies on peroxidases: A structural model for horseradish peroxidase and a substrate adduct
    • Banci, L., Carloni, P., and Savellini, G. G. (1994) Molecular dynamics studies on peroxidases: A structural model for horseradish peroxidase and a substrate adduct, Biochemistry 33, 12356-12366.
    • (1994) Biochemistry , vol.33 , pp. 12356-12366
    • Banci, L.1    Carloni, P.2    Savellini, G.G.3
  • 23
    • 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
  • 24
    • 0025398721 scopus 로고
    • WHAT IF: A molecular modeling and drug design program
    • Vriend, G. (1990) WHAT IF: A molecular modeling and drug design program, J. Mol. Graphics 8, 52-56.
    • (1990) J. Mol. Graphics , vol.8 , pp. 52-56
    • Vriend, G.1
  • 25
    • 33751158684 scopus 로고
    • Density functional theoretical study of oxo(porphyrinato)iron(IV) complexes, models of peroxidase compounds I and II
    • Ghosh, A., Almlöf, J., and Que, L. (1994) Density Functional Theoretical Study of Oxo(porphyrinato)iron(IV) Complexes, Models of Peroxidase Compounds I and II, J. Phys. Chem. 98, 5576-5579.
    • (1994) J. Phys. Chem. , vol.98 , pp. 5576-5579
    • Ghosh, A.1    Almlöf, J.2    Que, L.3
  • 26
    • 0019321508 scopus 로고
    • The stereochemistry of peroxidase catalysis
    • Poulos, T. L., and Kraut, J. (1980) The Stereochemistry of Peroxidase Catalysis, J. Biol. Chem. 255, 8199-8205.
    • (1980) J. Biol. Chem. , vol.255 , pp. 8199-8205
    • Poulos, T.L.1    Kraut, J.2
  • 27
    • 0033520695 scopus 로고    scopus 로고
    • Reaction mechanism of compound I formation in heme peroxidases: A density functional theory
    • Wirstam, M., Blomberg, M. R. A., and Siegbahn, P. E. M. (1999) Reaction Mechanism of Compound I Formation in Heme Peroxidases: A Density Functional Theory, J. Am. Chem. Soc. 121, 10178-10185.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 10178-10185
    • Wirstam, M.1    Blomberg, M.R.A.2    Siegbahn, P.E.M.3
  • 28
    • 0032474438 scopus 로고    scopus 로고
    • Structural interactions between horseradish peroxidase C and the substrate benzhydroxamic acid determined by x-ray crystallography
    • Henriksen, A., Schuller, D. J., Meno, K., Welinder, K. G., Smith, A. T., and Gajhede, M. (1998) Structural Interactions between Horseradish Peroxidase C and the Substrate Benzhydroxamic Acid Determined by X-ray Crystallography, Biochemistry 37, 8054-8060.
    • (1998) Biochemistry , vol.37 , pp. 8054-8060
    • Henriksen, A.1    Schuller, D.J.2    Meno, K.3    Welinder, K.G.4    Smith, A.T.5    Gajhede, M.6
  • 29
    • 0025240595 scopus 로고
    • Kinetic and molecular orbital studies on the rate of oxidation of monosubstituted phenols and anilines by horseradish peroxidase compound II
    • Sakurada, J., Sekiguchi, R., Sato, K., and Hosoya, T. (1990) Kinetic and Molecular Orbital Studies on the Rate of Oxidation of Monosubstituted Phenols and Anilines by Horseradish Peroxidase Compound II, Biochemistry 29, 4093-4098.
    • (1990) Biochemistry , vol.29 , pp. 4093-4098
    • Sakurada, J.1    Sekiguchi, R.2    Sato, K.3    Hosoya, T.4
  • 30
    • 0030028437 scopus 로고    scopus 로고
    • Rates of reaction of indoleacetic acids with horseradish peroxidase compound I and Their dependence on the redox potentials
    • Candeias, L. P., Folkes, L. K., Menuchehr, P., Patrick, J., and Wardman, P. (1996) Rates of Reaction of Indoleacetic Acids with Horseradish Peroxidase Compound I and Their Dependence on the Redox Potentials, Biochemistry 35, 102-108.
    • (1996) Biochemistry , vol.35 , pp. 102-108
    • Candeias, L.P.1    Folkes, L.K.2    Menuchehr, P.3    Patrick, J.4    Wardman, P.5
  • 32
    • 0035923432 scopus 로고    scopus 로고
    • Human myeloperoxidase: Structure of a cyanide complex and its interaction with bromide and thiocyanate substrates at 1.9 Å resolution
    • Blair-Johnson, M., Fiedler, T., and Fenna, R. (2001) Human myeloperoxidase: Structure of a cyanide complex and its interaction with bromide and thiocyanate substrates at 1.9 Å resolution, Biochemistry 40, 13990-13997.
    • (2001) Biochemistry , vol.40 , pp. 13990-13997
    • Blair-Johnson, M.1    Fiedler, T.2    Fenna, R.3
  • 33
    • 0041989751 scopus 로고    scopus 로고
    • CASTp: Computed atlas of surface topography of proteins
    • Binkowski, T. A., Naghibzadeh, S., and Liang, J. (2003) CASTp: Computed Atlas of Surface Topography of proteins, Nucleic Acids Res. 31, 3352-3355.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3352-3355
    • Binkowski, T.A.1    Naghibzadeh, S.2    Liang, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.