Enzyme-Catalyzed Electron and Radical Transfer pp 317-349

Part of the Subcellular Biochemistry book series (SCBI, volume 35)

Peroxidase-Catalyzed Oxidation of Ascorbate Structural, Spectroscopic and Mechanistic Correlations in Ascorbate Peroxidase

  • Emma Lloyd Raven

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12. References

  1. Altschul, A. M., Abrams, R., and Hogness, T. R., 1940, Cytochrome c peroxidase, J. Biol. Chem. 136:777–794.Google Scholar
  2. Armstrong, F. A., and Lannon, A. M., 1987, Fast interfacial electron-transfer between cytochrome-c peroxidase and graphite-electrodes promoted by aminoglycosides-novel electroenzymic catalysis of H2O2 reduction, J. Am. Chem. Soc. 109:7211–7212.CrossRefGoogle Scholar
  3. Armstrong, F. A., Butt, J. N., and Sucheta, A., 1993, Voltammetric studies of redox-active centres in metalloproteins adsorbed on electrodes, Meth. Enzymol. 227:479–500.PubMedCrossRefGoogle Scholar
  4. Armstrong, F. A., Heering, H. A., and Hirst, J., 1997, Reactions of complex metalloproteins studied by protein-film voltammetry, Chem. Soc. Rev. 26:169–179.CrossRefGoogle Scholar
  5. Asada, K., Miyake, C., Ogawa, K., and Hossain, M. A., 1996, Microcompartmentation of ascorbate peroxidase and regeneration of ascorbate from ascorbate radical: its dual role in chloroplasts, in: Plant Peroxidases: Biochemistry and Physiology (C. Obinger, U. Burner, R. Ebermann, C. Penel, and H. Greppin, eds.), University of Geneva, pp. 163–167.Google Scholar
  6. Asada, K., Miyake, C., Sano, S., and Amako, K., 1993, Plant Peroxidases: Biochemistry and Physiology (K. Welinder, S. Ramusen, H. Penel, and H. Greppin, eds.), University of Geneva, Geneva, Switzerland, pp. 243–250.Google Scholar
  7. Bach, A. N., and Chodat, R., 1903, Untersuchungen uber die rolle der peroxyde in der chemie der lebenden zelle. IV. Uber peroxydase, Ber 36:600.CrossRefGoogle Scholar
  8. Bonagura, C. A., Sundaramoorthy, M., Bhaskar, B., and Poulos, T. L., 1999, The effects of an engineered cation site on the structure, activity and EPR properties of cytochrome c peroxidase, Biochemistry 38:5538–5545.PubMedCrossRefGoogle Scholar
  9. Bonagura, C. A., Sundaramoorthy, M., Pappa, H. S., Patterson, W. R., and Poulos, T. L., 1996, An engineered cation site in cytochrome c peroxidase alters the reactivity of the redox active tryptophan, Biochemistry 35:6107–6115.PubMedCrossRefGoogle Scholar
  10. Borraccino, G., Dipierro, S., and Arrigoni, O., 1986, Purification and properties of ascorbate free-radical reductase from potato tubers, Planta 167:521–526.PubMedCrossRefGoogle Scholar
  11. Bosshard, H. R., Anni, H., and Yonetani, T., 1991, Yeast cytochrome c peroxidase, in: Peroxidases in Chemistry and Biology, Vol. 2 (J. Everse, K. E. Everse, and M. B. Grisham, eds.), CRC Press, Boca Raton, pp. 51–84.Google Scholar
  12. Boveris, A., Sies, H., Martino, E. E., Docampo, R., Turrens, J. F., and Stoppani, A. O. M., 1980, Deficient metabolic utilisation of hydrogen peroxide in Trypanosoma cruzi, Biochem. J. 188:643–648.PubMedPubMedCentralCrossRefGoogle Scholar
  13. Bujons, J., Dikiy, A., Ferrer, J. C., Banci, L., and Mauk, A. G., 1997, Charge reversal of a critical active-site residue of cytochrome c peroxidase: characterization of the Arg48Glu variant, FEBS Lett. 243:72–84.Google Scholar
  14. Bunkelmann, J. R., and Trelease, R. N., 1996, Ascorbate peroxidase: a prominent membrane protein in oilseed glyoxysomes, Plant Physiol. 110:589–598.PubMedPubMedCentralCrossRefGoogle Scholar
  15. Bunkelmann, J. R., and Trelease, R. N., 1997, Expression of glyoxysomal ascorbate peroxidase in cotton seedlings during postgerminative growth, Plant Science 122:209–216.CrossRefGoogle Scholar
  16. Caldwell, C. R., Turano, F. J., and McMahon, M. B., 1998, Identification of two cytosolic ascorbate peroxidase cDNAs from soybean leaves and characterisation of their products by functional expression in E. coli, Planta 204:120–126.PubMedCrossRefGoogle Scholar
  17. Celik, A., Cullis, P. M., and Lloyd Raven, E., 2000, Arch. Biochem. Biophys. 373:175–181.PubMedCrossRefGoogle Scholar
  18. Chatfield, M., and Dalton, D. A., 1993, Ascorbate peroxidase from soybean root nodules, Plant Physiol. 103:661–662.PubMedPubMedCentralCrossRefGoogle Scholar
  19. Cheek, J., Mandehnan, D., Poulos, T. L., and Dawson, J. H., 1999, A study of the K+-site mutant of ascorbate peroxidase: mutations of the protein on the proximal side of the heme cause changes in iron ligation on the distal side, J. Biol. Inorg. Chem. 4:64–72.PubMedCrossRefGoogle Scholar
  20. Chen, G.-X., and Asada, K., 1989, Ascorbate peroxidase in tea leaves: occurrence of two isozymes and the differences in their enzymic and molecular properties, Plant Cell Physiol. 30:987–998.Google Scholar
  21. Chen, G.-X., Sano, S., and Asada, K., 1992, The amino acid sequence of ascorbate peroxidase from tea has a high degree of homology to that of cytochrome c peroxidase from yeast, Plant Cell Physiol. 33:109–116.Google Scholar
  22. Conroy, C. W., Tyma, P., Daum, P. H., and Erman, J. E., 1978, Oxidation-reduction potential measurements of cytochrome c peroxidase and pH dependent spectral transitions in the ferrous enzyme, Biochim. Biophys. Acta 537:62–69.PubMedCrossRefGoogle Scholar
  23. Corpas, F. J., and Trelease, R. N., 1998, Differential expression of ascorbate peroxidase and a putative molecular chaperone in the boundary membrane of differentiating cucumber seedling peroxisomes, J. Plant Physiol. 153:332–338.CrossRefGoogle Scholar
  24. Dalton, D. A., 1991, Ascorbate peroxidase, in: Peroxidases in Chemistry and Biology, Vol. 2 (J. Everse, K. E. Everse, and M. B. Grisham, eds.), CRC Press, Boca Raton, pp. 139–154.Google Scholar
  25. Dalton, D. A., Diaz del Castillo, L., Kahn, M. L., Joyner, S. L., and Chatfield, J. M., 1996, Heterologous expression and characterization of soybean cytosolic ascorbate peroxidase, Arch. Biochem. Biophys. 328:1–8.PubMedCrossRefGoogle Scholar
  26. Dalton, D. A., Hanus, F. J., Russell, S. A., and Evans, H. J., 1987, Purification, properties and distribution of ascorbate peroxidase in legume root nodules, Plant Physiol. 83:789–794.PubMedPubMedCentralCrossRefGoogle Scholar
  27. Dalton, D. A., Langeberg, L., and Robbins, M., 1992, Purification and characterisation of mondehydroascorbate reductase from soybean root nodules, Arch. Biochem. Biophys. 292:281–286.PubMedCrossRefGoogle Scholar
  28. De Gara, L., de Pinto, M. C., and Arrigoni, O., 1997, Ascorbate synthesis and ascorbate peroxidase activity during the early stage of wheat development, Physiol. Plant. 100:894–900.CrossRefGoogle Scholar
  29. De Gara, L., de Pinton, M. C., Paciolla, C., Cappetti, V., and Arrigoni, O., 1996, Is ascorbate peroxidase only a scavenger of hydrogen peroxide? in: Plant Peroxidases: Biochemistry and Physiology (C. Obinger, U. Burner, R. Ebermann, C. Penel, and H. Greppin, eds.), University of Geneva, pp. 157–162.Google Scholar
  30. DePillis, G. D., Sishta, B. P., Mauk, A. G., and Ortiz de Montellano, P. R., 1991, Small substrates and cytochrome c are oxidized at different sites of cytochrome c peroxidase, J. Biol. Chem. 266:19334–19341.PubMedGoogle Scholar
  31. Doyle, W. A., Blodig, W., Veitch, N. C., Piontek, K., and Smith, A. T., 1998, Two substrate binding sites in lignin peroxidase revealed by site-directed mutagenesis, Biochemistry 37:15097–15105.PubMedCrossRefGoogle Scholar
  32. Doyle, W. A., and Smith, A. T., 1996, Expression of lignin peroxidase H8 in Escherichia coli: folding and activation of the recombinant enzyme with Ca 2+ and haem, Biochem. J. 315:15–19.PubMedPubMedCentralCrossRefGoogle Scholar
  33. Dunford, H. B., 1982, Peroxidases, Adv. Inorg. Biochem. 4:41.Google Scholar
  34. Dunford, H. B., 1991, Horseradish peroxidase: structure and kinetic properties, in: Peroxidases in Chemistry and Biology, Vol. 2 (J. Everse, K. E. Everse, and M. B. Grisham, eds.), CRC Press, Boca Raton, pp. 1–24.Google Scholar
  35. Dunford, H. B., 1999, Heme peroxidases, John Wiley, Chichester.Google Scholar
  36. Durner, J., and Klessig, D. F., 1995, Inhibition of ascorbate peroxidase by salicylic acid and 2,6-dichloroisonicotinic acid, two inducers of plant defense responses, Proc. Natl. Acad. Sci. USA 92:11312–11316.PubMedPubMedCentralCrossRefGoogle Scholar
  37. Elia, M. R., Borracino, G., and Dipierro, S., 1992, Soluble ascorbate peroxidase from potato tubers, Plant Science 85:17–21.CrossRefGoogle Scholar
  38. Erman, J. E., 1998, Cytochrome c peroxidase: a model heme protein, J. Biochem. Mol. Biol. 31:307–327.Google Scholar
  39. Erman, J. E., Vitello, L. B., Mauro, J. M., and Kraut, J., 1989, Detection of an oxy-ferryl porphyrin π-cation radical in the reaction between hydrogen peroxide and a mutant yeast cytochrome c peroxidase. Evidence for tryptophan-191 involvement in the radical site of compound I, Biochemistry 28:7992–7995.PubMedCrossRefGoogle Scholar
  40. Farhangrazi, Z. S., Copeland, B. R., Nakayama, T., Yamazaki, I., and Powers, L. S., 1994, Oxidation-reduction properties of compounds I and II of Arthromyces ramosus peroxidase, Biochemistry 33:5647–5652.PubMedCrossRefGoogle Scholar
  41. Farhangrazi, Z. S., Fossett, M. E., Powers, L. S., and Ellis, W. R., 1995, Variable-temperature spectroelectrochemical study of horseradish peroxidase, Biochemistry 34:2866–2871.PubMedCrossRefGoogle Scholar
  42. Finzel, B. C., Poulos, T. L., and Kraut, J., 1984, Crystal structure of cytochrome c peroxidase refined at 1.7 resolution, J. Biol. Chem. 259:13027–13036.PubMedGoogle Scholar
  43. Foyer, C. H., and Mullineaux, P. M., 1998, The presence of dehydroascorbate and dehydroascorbate reductase in plant tissues, FEBS Lett. 425:528–529.PubMedCrossRefGoogle Scholar
  44. Frew, J. E., and Jones, P., 1984, Structure and functional properties of peroxidases and catalases, in: Advances in Inorganic Chemistry (A. Sykes, ed.), Academic Press, New York, pp. 175.Google Scholar
  45. Gajhede, M., Schuller, D. J., Henricksen, A., Smith, A. T., and Poulos, T. L., 1997, Crystal structure of horseradish peroxidase C at 2.15 angstrom resolution, Nature Struct. Biol. 4:1032–1038.PubMedCrossRefGoogle Scholar
  46. Gerbling, K.-P, Kelly, G. J., Fischer, K.-H., and Latzko, E., 1984, Partial purification and properties of soluble ascorbate peroxidases from pea leaves, J. Plant Physiol. 115:59–67.PubMedCrossRefGoogle Scholar
  47. Gillham, D. J., and Dodge, A. D., 1986, Hydrogen-peroxide-scavenging systems within pea chloroplasts, Planta 167:246–251.PubMedCrossRefGoogle Scholar
  48. Goodin, D. B., and McRee, D. E., 1993, The Asp-His-Fe triad of cytochrome c peroxidase controls the reduction potential, electronic-structure and coupling of the tryptophan free-radical to the heme, Biochemistry 32:3313–3324.PubMedCrossRefGoogle Scholar
  49. Groden, D., and Beck, E., 1979, H2O2 destruction by ascorbate-dependent systems from chloroplasts, Biochim. Biophys. Acta 546:426–435.PubMedCrossRefGoogle Scholar
  50. Harbury, H. A., 1957, Oxidation-reduction potentials of horseradish peroxidase, J. Biol. Chem. 225:1009–1024.PubMedGoogle Scholar
  51. Hayashi, Y., and Yamazaki, I., 1979, The oxidation-reduction potentials of compound I/II and compound II/ferric couples of horseradish peroxidase A2 and C, J. Biol. Chem. 254:9101–9106.PubMedGoogle Scholar
  52. He, B., Sinclair, R., Copeland, B. R., Makino, R., and Powers, L. S., 1996, The structure/function relationship and reduction potentials of high oxidation states of myoglobin and peroxidase, Biochemistry 35:2413–2420.PubMedCrossRefGoogle Scholar
  53. Hill, A. P., Modi, S., Sutcliffe, M. J., Turner, D. D., Gilfoyle, D. J., Smith, A. T., Tam, B. M., and Lloyd, E., 1997, Chemical, spectroscopic and structural investigation of the substrate-binding site in ascorbate peroxidase, Eur. J. Biochem. 248:347–354.PubMedCrossRefGoogle Scholar
  54. Hossain, M. A., and Asada, K., 1984, Inactivation of ascorbate peroxidase in spinach chloroplasts on dark addition of hydrogen peroxide: its protection by ascorbate, Plant Cell Physiol. 25:1285–1295.Google Scholar
  55. Hossain, M. A., Nakano, Y., and Asada, K., 1984, Monodehydroascorbate reductase in spinach chloroplasts and its participation in regeneration of ascorbate for scavenging hydrogen peroxide, Plant Cell Physiol. 25:385–395.Google Scholar
  56. Huyett, J. E., Doan, P. E., Gurbiel, R., Houseman, A. L. P., Sivaraja, M., Goodin, D. B., and Hoffman, B. M., 1995, Compound ES of cytochrome c peroxidase contains a Trp π-cation radicalócharacterisation by CW and pulsed Q-band ENDOR spectroscopy, J. Am. Chem. Soc. 117:9033–9041.CrossRefGoogle Scholar
  57. Ishikawa, T., Sakai, K., Takeda, T., and Shigeoka, S., 1995, Cloning and expression of a cDNA encoding a new type of ascorbate peroxidase from spinach, FEBS Lett. 367:28–32.PubMedCrossRefGoogle Scholar
  58. Ishikawa, T., Sakai, K., Yoshimura, K., Takeda, T., and Shigeoka, S., 1996a, cDNAs encoding spinach stromal and thylakod-bound ascorbate peroxidase, differing in the presence or absence of their 3′-coding regions, FEBS Lett. 384:289–293.PubMedCrossRefGoogle Scholar
  59. Ishikawa, T., Takeda, T., Kohno, H., and Shigeoka, S., 1996b, Molecular characterisation of Euglena ascorbate peroxidase using monoclonal antibody, Biochim. Biophys. Acta 1290:69–75.PubMedCrossRefGoogle Scholar
  60. Ishikawa, T., Takeda, T., and Shigeoka, S., 1996c, Purification and characterisation of cytosolic asorbate peroxidase from komatsuna (Brassica rapa), Plant Science 120:11–18.CrossRefGoogle Scholar
  61. Ishikawa, T., Yoshimura, K., Sakai, K., Tamoi, M., Takeda, T., and Shigeoka, S., 1998, Molecular characterisation and physiological role of a glyoxysome-bound ascorbate peroxidase from spinach, Plant Cell Physiol. 39:23–34.PubMedCrossRefGoogle Scholar
  62. Jablonski, P. P., and Anderson, J. W., 1982, Light-dependent reduction of hydrogen peroxide by ruptured pea chloroplasts, Plant Physiol. 69:1407–1413.PubMedPubMedCentralCrossRefGoogle Scholar
  63. Jensen, G. M., 1998, Energetics of cation radical formation at the proximal active site tryptophan of cytochrome c peroxidase and ascorbate peroxidase, J. Phys. Chem. 102:8221–8228.CrossRefGoogle Scholar
  64. Jespersen, H. M., Kjaersgard, I. V. H., Ostergaard, L., and Welinder, K. G., 1997, From sequence analysis of three novel ascorbate peroxidases from Arabidopsis thaliana to structure, function and evolution of seven types of ascorbate peroxidase, Eur. J. Biochem. 326:305–310.CrossRefGoogle Scholar
  65. Jimenez, A., Hernandez, J. A., del Rio, L. A., and Sevilla, F., 1997, Evidence for the presence of the ascorbate-glutathione cycle in mitochondria and peroxisomes of pea leaves, Plant Physiol. 114:275–284.PubMedPubMedCentralCrossRefGoogle Scholar
  66. Jimenez, A., Jimenez, J. A., Barcelo, A. R., Sandalio, L. M., del Rio, L. A., and Sevilla, F., 1998, Mitochondrial and peroxisomal ascorbate peroxidase of pea leaves, Physiol. Plant. 104:687–692.CrossRefGoogle Scholar
  67. Jones, D. K., Dalton, D. A., Rosell, F. I., and Lloyd Raven, E., 1998, Class I heme peroxidases: characterisation of soybean ascorbate peroxidase, Arch. Biochem. Biophys. 360:173–178.PubMedCrossRefGoogle Scholar
  68. Kelly, G. J., and Latzko, E., 1979, Soluble ascorbate peroxidase, Naturewissenschaften 66: 617–618.Google Scholar
  69. Kim, I. J., and Chung, W. I., 1998, Molecular characterisation of a cytosolic ascorbate peroxidase in strawberry fruit, Plant Science 133:69–77.CrossRefGoogle Scholar
  70. Koshiba, T., 1993, Cytosolic ascorbate peroxidase in seedlings and leaves of maize (Zea mays), Plant Cell Physiol. 34:713–721.Google Scholar
  71. Kubo, A., Saji, H., Tanaka, K., Tanaka, K., and Kondo, N., 1992, Cloning and sequencing of a cDNA encoding ascorbate peroxidase from Arabidopsis thaliana, Plant Mol. Biol. 18:691–701.PubMedCrossRefGoogle Scholar
  72. Kvaratskhelia, M., George, S. J., and Thorneley, R. N. F., 1997a, Salicylic acid is a reducing substrate and not an effective inhibitor of ascorbate peroxidase, J. Biol. Chem. 272:20998–21001.PubMedCrossRefGoogle Scholar
  73. Kvaratskhelia, M., Winkel, C., Naldrett, M. T., and Thorneley, R. N. F., 1999, A novel high activity cationic ascorbate from tea (Camellia sinensis)óa class III peroxidase with unusual substrate specificity, J. Plant Physiol. 154:273–282.CrossRefGoogle Scholar
  74. Kvaratskhelia, M., Winkel, C., and Thorneley, R. N. F., 1997b, Purification and characterisation of a novel class III peroxidase isozyme from tea leaves, Plant Physiol. 114:1237–1245.PubMedPubMedCentralCrossRefGoogle Scholar
  75. Lad, L., Basran, J., Scrutton, N. S., and Lloyd Raven, E., 1999, unpublished.Google Scholar
  76. Lim, A. R., 1989, PhD dissertation, University of British Columbia.Google Scholar
  77. Lopez, F., Vansuyt, G., CasseDelbart, F., and Fourcroy, P., 1996, Ascorbate peroxidase activity, not the mRNA level, is enhanced in salt-stressed Raphanus sativus plants, Physiol. Plant. 97:13–20.CrossRefGoogle Scholar
  78. Mandelman, D., Jamal, J., and Poulos, T. L., 1998a, Identification of two-electron transfer site in ascorbate peroxidase using chemical modification, enzyme kinetics, and crystallography, Biochemistry 37:17610–17617.PubMedCrossRefGoogle Scholar
  79. Mandelman, D., Schwarz, F. P., Li, H., and Poulos, T. L., 1998b, The role of quaternary interactions on the stability and activity of ascorbate peroxidase, Protein Science 7:2089–2098.PubMedPubMedCentralCrossRefGoogle Scholar
  80. Mano, S., Yamaguchi, K., Hayashi, M., and Nishimura, M., 1997, Stromal and thylakoid-bound ascorbate peroxidase are produced by alternative splicing in pumpkin, FEBS Lett. 413:21–26.PubMedCrossRefGoogle Scholar
  81. Maranon, M. J. R., Stillman, M. J., and van Huystee, R. B., 1993, CD analysis of co-dependency of calcium and porphyrin for the integrate molecular structure of peanut peroxidase, Biochem. Biophys. Res. Comm. 194:326–333.CrossRefGoogle Scholar
  82. Marquez, L. A., Quitoriano, M., Zilinskas, B. A., and Dunford, H. B., 1996, Kinetic and spectral properties of pea cytosolic ascorbate peroxidase, FEBS Lett. 389:153–156.PubMedCrossRefGoogle Scholar
  83. Mathews, M. C., Summers, C. B., and Felton, G. W., 1997, Ascorbate peroxidase: a novel antioxidant enzyme in insects, Arch. Insect Biochem. Physiol. 34:57–68.CrossRefGoogle Scholar
  84. Mauk, M. R., Kishi, K., Gold, M. H., and Mauk, A. G., 1998, pH-linked binding of Mn(II) to manganese peroxidase, Biochemistry 37:6767–677.PubMedCrossRefGoogle Scholar
  85. Mauro, J. M., Fishel, L. A., Hazzard, J. T., Meyer, T. E., Tollin, G., Cusanovich, M. A., and Kraut, J., 1988, Tryptophan-191-phenylalanine, a proximal-side mutation in yeast cytochrome c peroxidase that strongly affects the kinetics of ferrocytochrome c oxidation, Biochemistry 27:6243–6256.PubMedCrossRefGoogle Scholar
  86. Meneguzzo, S., Sgherm, C. L. M., Navari-Izzo, F., and Izzo, R., 1998, Stromal and thylakoid-bound ascorbate peroxidases in NaCl-treated wheat, Physiol. Plant. 104:735–740.CrossRefGoogle Scholar
  87. Menyhard, D. K., and Naray-Szabo, G., 1999, Electrostatic effect on electron transfer at the active site of heme peroxidases: a comparative molecular orbital study on cytochrome c peroxidase and ascorbate peroxidase, J. Phys. Chem. 103:227–233.CrossRefGoogle Scholar
  88. Millis, C. D., Cai, D., Stankovich, M. T., and Tien, M., 1989, Oxidation-reduction potentials and ionization states of extracellular peroxidases from the lignin-degrading fungus Phanerochaete crysoporium, Biochemistry 28:8484–8489.PubMedCrossRefGoogle Scholar
  89. Mittler, R., and Zilinskas, B. A., 1991a, Molecular cloning and nucleotide sequence analysis of a cDNA encoding pea cytosolic ascorbate peroxidase, FEBS Lett. 289:257–259.PubMedCrossRefGoogle Scholar
  90. Mittler, R., and Zilinskas, B. A., 1991b, Purification and characterisation of pea cytosolic ascorbate peroxidase, Plant Physiol. 97:962–968.PubMedPubMedCentralCrossRefGoogle Scholar
  91. Miyake, C., and Asada, K., 1996, Inactivation mechanism of ascorbate peroxidase at low concentrations of ascorbate: hydrogen peroxide decomposes Compound I of ascorbate peroxidase, Plant Cell Physiol. 37:423–430.CrossRefGoogle Scholar
  92. Miyake, C., Cao, W.-H., and Asada, K., 1993, Purification and molecular properties of the thylakoid-bound ascorbate peroxidase in spinach chloroplasts, Plant Cell Physiol. 34:3881–3889.Google Scholar
  93. Miyake, C., Michihata, F., and Asada, K., 1991, Scavenging of hydrogen peroxide in prokaryotic and eukaryotic algae: acquisition of ascorbate peroxidase during the evolution of cyanobacteria, Plant Cell Physiol. 32:33–43.Google Scholar
  94. Mondal, M. S., Goodin, D. B., and Armstrong, F. A., 1998, Simultaneous voltammetric comparisons of reduction potentials, reactivities, and stabilities of the high-potential catalytic states of wild-type and distal-pocket mutant (W51F) yeast cytochrome c peroxidase, J. Am. Chem. Soc. 120:6270–6276.CrossRefGoogle Scholar
  95. Mondal, M. S., Fuller, H. A., and Armstrong, F. A., 1996, Direct measurement of the reduction potential of catalytically active cytochrome c peroxidase compound I: voltammetric detection of a reversible, cooperative two-electron transfer reaction, J. Am. Chem. Soc. 118:263–264CrossRefGoogle Scholar
  96. Morishima, I., Kurono, M., and Shiro, Y., 1986, Presence of endogenous calcium-ion in horseradish peroxidaseóelucidation of metal-binding site by substitutions of divalent and lanthanide ions for calcium and use of metal-induced NMR H1 and Cd113 resonances, J. Biol. Chem. 261:9391–9399.PubMedGoogle Scholar
  97. Morita, S., Kaminaka, H., Yokoi, H., Masumara, T., and Tanaka, K., 1997, Differential responses of two cytosolic superoxide dismutase genes and two cytosolic ascorbate peroxidase genes in rice to environmental stresses, Plant Physiol. 114:102.Google Scholar
  98. Murthy, S. S., and Zilinskas, B. A., 1994, Molecular cloning and characterisation of a cDNA encoding pea monodehydroascorbate reductase, J. Biol. Chem. 269:31129–31133.PubMedGoogle Scholar
  99. Nakano, Y., and Asada, K., 1987, Purification of ascorbate peroxidase in spinach chloroplasts: its inactivation in ascorbate-depleted medium and reactivation by monodehydroascorbate radical, Plant Cell Physiol. 28:131–140.Google Scholar
  100. Naray-Szabo, G., 1997, Electrostatic modulation of electron transfer in the active site of heme peroxidases, J. Biol. Inorg. Chem. 2:135–138.CrossRefGoogle Scholar
  101. Newman, T., De Bruijin, F. J., Green, P., Keegstra, K., Kende, H., McIntish, L., Ohlrogge, J., Raikhel, N., Somerville, S., Thomashow, M., Retzel, E., and Somerville, C., 1996, Genes galore: a summary of methods for accessing results from large-scale partial sequencing of anonymous Arabidopsis cDNA clones, Plant Physiol. 106:1241–1255.CrossRefGoogle Scholar
  102. Nicholls, P., and Schonbaum, G. R., 1963, in: The Enzymes, Vol. 8 (P. D. Boyer, H. Lardy, and K. Myrbach, eds.), Academic Press, New York, pp. 147–225.Google Scholar
  103. Nie, G., and Aust, S. D., 1997, Effect of calcium on the reversible thermal activation of lignin peroxidase, Arch. Biochem. Biophys. 337:225–231.PubMedCrossRefGoogle Scholar
  104. Nissum, M., Neri, F., Mandelman, D., Poulos, T. L., and Smulevich, G., 1998, Spectroscopic characterisation of recombinant pea cytosolic ascorbate peroxidase: similarities and differences with cytochrome c peroxidase, Biochemistry 37:8080–8087.PubMedCrossRefGoogle Scholar
  105. Ogawa, S., Shino, Y., and Morishima, I., 1979, Calcium binding by horseradish peroxidase C and the heme environmental structure, Biochem. Biophys. Res. Comm. 90:674–678.PubMedCrossRefGoogle Scholar
  106. Ohya, T., Morimura, Y., Saji, H., Mihara, T., and Ikawa, T., 1997, Purification and characterisation of ascorbate peroxidase in roots of Japanese radish, Plant Science 125:137–145.CrossRefGoogle Scholar
  107. Ortiz de Montellano, P. R., 1987, Control of the catalytic activity of prosthetic heme by the structure of hemoproteins, Acc. Chem. Res. 20:289–294.CrossRefGoogle Scholar
  108. Orvar, B. L., and Ellis, B. E., 1995, Isolation of a cDNA encoding cytosolic ascorbate peroxidase from tobacco, Plant Physiol. 108:839–840.PubMedPubMedCentralCrossRefGoogle Scholar
  109. Pappa, H., Patterson, W. R., and Poulos, T. L., 1996, The homologous tryptophan critical for cytochrome c peroxidase function is not essential for ascorbate peroxidase activity, J. Biol. Chem. 1:61–66.Google Scholar
  110. Patterson, W. R., and Poulos, T. L., 1994, Characterization and crystallization of recombinant pea cytosolic ascorbate peroxidase, J. Biol. Chem. 269:17020–17024.PubMedGoogle Scholar
  111. Patterson, W. R., and Poulos, T. L., 1995, Crystal structure of recombinant pea cytosolic ascorbate peroxidase, Biochemistry 34:4331–4341.PubMedCrossRefGoogle Scholar
  112. Patterson, W. R., Poulos, T. L., and Goodin, D. B., 1995, Identification of a porphyrin π-Cation radical in ascorbate peroxidase Compound I, Biochemistry 34:4342–4345.PubMedCrossRefGoogle Scholar
  113. Poulos, T. L., Freer, S. T., Alden, R. A., Edwards, S. L., Skogland, U., Takio, K., Eriksson, B., Xuong, N., Yonetani, T., and Kraut, J., 1980, The crystal structure of cytochrome c peroxidase, J. Biol. Chem. 255:575–580.PubMedGoogle Scholar
  114. Poulos, T. L., and Kraut, J., 1980, The stereochemistry of peroxidase catalysis, J. Biol. Chem. 255:8199–8205.PubMedGoogle Scholar
  115. Sano, S., Miyake, C., Mikami, B., and Asada, K., 1995, Molecular characterisation of monodehydroascorbate radical reductase from cucumber highly expressed in Escherichia coli, J. Biol. Chem. 270:21354–21361.PubMedCrossRefGoogle Scholar
  116. Sano, S., Ueda, M., Kurano, N., Miyachi, S., and Yokota, A., 1996, Ascorbate peroxidase from a red alga, Galdiera partita, in: Plant Peroxidases: Biochemistry and Physiology (C. Obinger, U. Burner, R. Ebermann, C. Penel, and H. Greppin, eds.), University ofGeneva, pp. 168–172.Google Scholar
  117. Sauser, K. R., Liu, J. K., and Wong, T.-Y., 1997, Identification of a copper-sensitive ascorbate peroxidase in the unicellular green alga Selenastrum capricornutum, BioMetals 10:163–168.PubMedCrossRefGoogle Scholar
  118. Schantz, M.-L., Schreiber, H., Guillemaut, P., and Schantz, R., 1995, Changes in ascorbate peroxidase activities during fruit ripening in Capiscum annum, FEBS Lett. 358:149.PubMedCrossRefGoogle Scholar
  119. Scholes, C. P., Liu, Y., Fishel, L. A., Farnum, M. F., Mauro, J. M., and Kraut, J., 1989, Recent ENDOR and pulsed electron paramagnetic resonance studies of cytochrome c peroxidase Compound I and its site-directed mutants, Israel J. Chem. 29:85–92.CrossRefGoogle Scholar
  120. Shigeoka, S., Nakano, Y., and Kitaoka, S., 1980, Purification and some properties of L-ascorbic acid-specific peroxidase in Euglena gracilis Z, Arch. Biochem. Biophys. 201:121–127.PubMedCrossRefGoogle Scholar
  121. Shigeoka, S., Yasumoto, R., Onishi, T., Nakano, Y., and Kitaoka, S., 1987, Properties of monodehydroascorbate reductase and dehydroascorbate reductase and their participation in the regeneration of ascorbate in Euglena gracilis, J. Gen. Microbiol. 133:227–232.Google Scholar
  122. Sivaraja, M., Goodin, D. B., Smith, M., and Hoffman, B. M., 1989, Identification by ENDOR of Trp191 as the free-radical site in cytochrome c peroxidase Compound ES, Science 245:738–740.PubMedCrossRefGoogle Scholar
  123. Smith, A. T., Santama, N., Dacey, S., Edwards, M., Bray, R. C., Thorneley, R. N. F., and Burke, J. F., 1990, Expression of a synthetic gene for horseradish peroxidase C in Escherichia coli and folding and activation of the recombinant enzyme with Ca2+ and heme, J. Biol. Chem. 265:13335–13343.PubMedGoogle Scholar
  124. Smith, A. T., and Veitch, N. C., 1998, Substrate binding and catalysis in heme peroxidases, Curr. Opin. Chem. Biol. 2:269–278.PubMedCrossRefGoogle Scholar
  125. Sutherland, G. R. J., and Aust, S. D., 1997, Thermodynamics of binding of the distal calcium to manganese peroxidase, Biochemistry 36:8567–8573.PubMedCrossRefGoogle Scholar
  126. Sutherland, G. R. J., Zapanta, S., Tien, M., and Aust, S. D., 1997, Role of calcium in maintaining the heme environment of manganese peroxidase, Biochemistry 36:3654–3662.PubMedCrossRefGoogle Scholar
  127. Takeda, T., Yoshimura, K., Ishikawa, T., and Shigeoka, S., 1998, Purification and characterisation of ascorbate peroxidase in Chlorella vulgaris, Biochimie 80:295–301.PubMedCrossRefGoogle Scholar
  128. Tanaka, K., Takeuchi, E., Kubo, A., Sakaki, T., Haraguchi, K., and Kawamura, Y., 1991, Two immunologically different isozymes of ascorbate peroxidase from spinach leaves, Arch. Biochem. Biophys. 286:371–375.PubMedCrossRefGoogle Scholar
  129. Tanaka, M., Ishimori, K., and Morishima, I., 1998, Structural roles of the highly conserved Glu residue in the heme distal site of peroxidases, Biochemistry 37:2629–2638.PubMedCrossRefGoogle Scholar
  130. Tel-Or, E., Huflejt, M. E., and Packer, L., 1986, Hydroperoxide metabolism in cyanobacteria, Arch. Biochem. Biophys. 246:396–402.PubMedCrossRefGoogle Scholar
  131. Turner, D. D., Andrew, C. R., Cheesman, M. R., Thomson, A. J., and Lloyd Raven, E., 1999, submitted.Google Scholar
  132. Turner, D. D., and Lloyd Raven, E., 1999, unpublished.Google Scholar
  133. Ushimara, T., Maki, Y., Sano, S., Koshiba, K., Asada, K., and Tsuji, H., 1997, Induction of enzymes involved in the ascorbate-dependent antioxidative systems, namely ascorbate peroxidase, monodehydroascorbate reductase and dehydroascorbate reductase, after exposure to air of rice (Oryza sativa) seedlings germinated under water, Plant Cell Physiol. 38:541–549.CrossRefGoogle Scholar
  134. van Breusegem, F., Villarroel, R., van Montagu, M., and Inze, D., 1995, Ascorbate peroxidase cDNA from maize, Plant Physiol. 107:649–650.PubMedPubMedCentralCrossRefGoogle Scholar
  135. Wada, N., Kinoshita, S., Matsuo, M., Amako, K., Miyake, C., and Asada, K., 1998, Purification and molecular properties of ascorbate peroxidase from bovine eye, Biochem. Biophys. Res. Comm. 242:256–261.PubMedCrossRefGoogle Scholar
  136. Webb, R. P, and Allen, R. D., 1995, Isolation and characterisation of a cDNA for spinach cytosolic ascorbate peroxidase, Plant Physiol. 108:1325.PubMedPubMedCentralCrossRefGoogle Scholar
  137. Welinder, K. G., 1992, Superfamily of plant, fungal and bacterial peroxidases, Curr. Opin. Struct. Biol 2:388–393.CrossRefGoogle Scholar
  138. Wilcox, S. K., Jensen, G. M., Fitzgerald, M. M., McRee, D. E., and Goodin, D. B., 1996, Altering substrate specificity at the heme edge of cytochrome c peroxidase, Biochemistry 35:4858–4866.PubMedCrossRefGoogle Scholar
  139. Wilcox, S. K., Putnam, C. D., Sastry, M., Blankenship, J., Chazin, W. J., McRee, D. E., and Goodin, D. B., 1998, Rational design of a functional metalloenzyme: introduction of a site for manganese binding and oxidation into a heme peroxidase, Biochemistry 37:16853–16862.PubMedCrossRefGoogle Scholar
  140. Yamada, H., Makino, R., and Yamazaki, I., 1975, Effrects of 2,4-substituents of deuteroheme upon redox potentials of horseradish peroxidases, Arch. Biochem. Biophys. 169:344–353.PubMedCrossRefGoogle Scholar
  141. Yamaguchi, K., Hayashi, M., and Nishimura, M., 1996, cDNA cloning of thylakoid-bound ascorbate peroxidase in pumpkin and its characterisation, Plant Cell Physiol. 37:405–409.PubMedCrossRefGoogle Scholar
  142. Yamaguchi, K., Hori, H., and Nishimura, M., 1995, A novel isoenzyme of ascorbate peroxidase localized on glyoxysomal and leaf peroxisomal membranes in pumpkin, Plant Cell Physiol. 36:1157–1162.PubMedGoogle Scholar
  143. Yonetani, T., and Ray, G. S., 1965, Studies on cytochrome c peroxidase. Purification and some properties, J. Biol. Chem. 240:4503–4514.PubMedGoogle Scholar
  144. Yoshimura, K., Ishikawa, T., Nakumura, Y., Tamoi, M., Takeda, T., Tada, T., Nishimura, K., and Shigeoka, S., 1998, Comparative study on recombinant chloroplastic and cytosolic ascorbate peroxidase isozymes of spinach, Arch. Biochem. Biophys. 353:55–63.PubMedCrossRefGoogle Scholar
  145. Zhang, H., Wang, J., Nickel, U., Allen, R. D., and Goodman, H. M., 1997, Cloning and expression of an Arabidopsis gene encoding a putative peroxisomal ascorbate peroxidase, Plant Mol. Biol. 34:967–971.PubMedCrossRefGoogle Scholar

Copyright information

© Kluwer Academic/Plenum Publishers 2000

Authors and Affiliations

  • Emma Lloyd Raven
    • 1
  1. 1.Department of ChemistryUniversity of LeicesterLeicesterEngland, UK

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