메뉴 건너뛰기




Volumn 37, Issue 4, 1996, Pages 423-430

Inactivation mechanism of ascorbate peroxidase at low concentrations of ascorbate; hydrogen peroxide decomposes Compound I of ascorbate peroxidase

Author keywords

Ascorbate; Ascorbate peroxidase (EC 1.11.1.11); Compound I; Hydrogen peroxide; Inactivation; Peroxidase

Indexed keywords


EID: 0029822638     PISSN: 00320781     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.pcp.a028963     Document Type: Article
Times cited : (152)

References (35)
  • 1
    • 0028055996 scopus 로고
    • Separate assays specific for ascorbate peroxidase and guaiacol peroxidase and for chloroplastic and cytosolic isozymes of ascorbate peroxidase in plants
    • Amako, K., Chen, G-X. and Asada, K. (1994) Separate assays specific for ascorbate peroxidase and guaiacol peroxidase and for chloroplastic and cytosolic isozymes of ascorbate peroxidase in plants. Plant Cell Physiol. 35: 497-504.
    • (1994) Plant Cell Physiol. , vol.35 , pp. 497-504
    • Amako, K.1    Chen, G.-X.2    Asada, K.3
  • 3
    • 84983392009 scopus 로고
    • Ascorbate peroxidase - A hydrogen peroxide-scavenging enzyme in plants
    • Asada, K. (1992) Ascorbate peroxidase - a hydrogen peroxide-scavenging enzyme in plants. Physiol. Plant. 85: 235-241.
    • (1992) Physiol. Plant. , vol.85 , pp. 235-241
    • Asada, K.1
  • 4
    • 33745314723 scopus 로고
    • Ascorbate peroxidase in tea leaves: Occurrence of two isoenzymes and the differences in their enzymatic and molecular properties
    • Chen, G-X. and Asada, K. (1989) Ascorbate peroxidase in tea leaves: occurrence of two isoenzymes and the differences in their enzymatic and molecular properties. Plant Cell Physiol. 30: 987-998.
    • (1989) Plant Cell Physiol. , vol.30 , pp. 987-998
    • Chen, G.-X.1    Asada, K.2
  • 5
    • 0025317811 scopus 로고
    • Hydroxyurea and p-aminophenol are the suicide inhibitors of ascorbate peroxidase
    • Chen, G-X. and Asada, K. (1990) Hydroxyurea and p-aminophenol are the suicide inhibitors of ascorbate peroxidase. J. Biol. Chem. 265: 2775-2781.
    • (1990) J. Biol. Chem. , vol.265 , pp. 2775-2781
    • Chen, G.-X.1    Asada, K.2
  • 6
    • 0000205390 scopus 로고
    • Inactivation of ascorbate peroxidase by thiols requires hydrogen peroxide
    • Chen, G-X. and Asada, K. (1992a) Inactivation of ascorbate peroxidase by thiols requires hydrogen peroxide. Plant Cell Physiol. 33: 117-123.
    • (1992) Plant Cell Physiol. , vol.33 , pp. 117-123
    • Chen, G.-X.1    Asada, K.2
  • 7
    • 0013505129 scopus 로고
    • The amino acid sequence of ascorbate peroxidase from tea has a high degree of homology to that of cytochrome c peroxidase from yeast
    • Chen, G-X., Sano, S. and Asada, K. (1992b) 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.
    • (1992) Plant Cell Physiol. , vol.33 , pp. 109-116
    • Chen, G.-X.1    Sano, S.2    Asada, K.3
  • 9
    • 0002154654 scopus 로고
    • Horseradish peroxidase: Structure and kinetic properties
    • Edited by Everse, J., Everse, Ke. and Grisham, M.B. CRC Press, Inc. Florida
    • Dunford, H.B. (1991) Horseradish peroxidase: structure and kinetic properties. In Peroxidase in Chemistry and Biology, Volume II. Edited by Everse, J., Everse, Ke. and Grisham, M.B. pp. 1-23. CRC Press, Inc. Florida.
    • (1991) Peroxidase in Chemistry and Biology , vol.2 , pp. 1-23
    • Dunford, H.B.1
  • 10
    • 0000221254 scopus 로고
    • Measurement of the ascorbate content of spinach leaf protoplasts and chloroplasts during illumination
    • Foyer, C., Rowell, J. and Walker, D. (1983) Measurement of the ascorbate content of spinach leaf protoplasts and chloroplasts during illumination. Planta 157: 239-244.
    • (1983) Planta , vol.157 , pp. 239-244
    • Foyer, C.1    Rowell, J.2    Walker, D.3
  • 11
    • 0000921265 scopus 로고
    • The third intermediate compound of horseradish peroxidase and hydrogen peroxide
    • George, P. (1953) The third intermediate compound of horseradish peroxidase and hydrogen peroxide. J. Biol. Chem. 201: 427-434.
    • (1953) J. Biol. Chem. , vol.201 , pp. 427-434
    • George, P.1
  • 12
    • 10244250500 scopus 로고
    • Untersuchungen über Beziehungen zwischen Ascorbinsäure und Photosynthese
    • Gerhardt, B. (1964) Untersuchungen über Beziehungen zwischen Ascorbinsäure und Photosynthese. Planta 61: 101-129.
    • (1964) Planta , vol.61 , pp. 101-129
    • Gerhardt, B.1
  • 13
    • 0000885796 scopus 로고
    • Purification and characterization of thylakoid-bound Mn-superoxide dismutase in spinach chloroplasts
    • Hayakawa, T., Kanematsu, S. and Asada, K. (1985) Purification and characterization of thylakoid-bound Mn-superoxide dismutase in spinach chloroplasts. Planta 166: 111-116.
    • (1985) Planta , vol.166 , pp. 111-116
    • Hayakawa, T.1    Kanematsu, S.2    Asada, K.3
  • 14
    • 0000949449 scopus 로고
    • Inactivation of ascorbate peroxidase in spinach chloroplasts on dark addition of hydrogen peroxide; its protection by ascorbate
    • 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.
    • (1984) Plant Cell Physiol. , vol.25 , pp. 1285-1295
    • Hossain, M.A.1    Asada, K.2
  • 15
    • 0026812635 scopus 로고
    • Cloning and sequencing of a cDNA encoding ascorbate peroxidase from Arabidopsis thaliana
    • 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.
    • (1992) Plant Mol. Biol. , vol.18 , pp. 691-701
    • Kubo, A.1    Saji, H.2    Tanaka, K.3    Tanaka, K.4    Kondo, N.5
  • 16
    • 0000121196 scopus 로고
    • Purification and characterization of pea cytosolic ascorbate peroxidase
    • Mittler, R. and Zilinskas, B.A. (1991a) Purification and characterization of pea cytosolic ascorbate peroxidase. Plant Physiol. 97: 962-968.
    • (1991) Plant Physiol. , vol.97 , pp. 962-968
    • Mittler, R.1    Zilinskas, B.A.2
  • 17
    • 0025824122 scopus 로고
    • Molecular cloning and nucleotide sequence analysis of a cDNA encoding pea cytosolic ascorbate peroxidase
    • Mittler, R. and Zilinskas, B.A. (1991b) Molecular cloning and nucleotide sequence analysis of a cDNA encoding pea cytosolic ascorbate peroxidase. FEBS Lett. 289: 257-259.
    • (1991) FEBS Lett. , vol.289 , pp. 257-259
    • Mittler, R.1    Zilinskas, B.A.2
  • 18
    • 77957181306 scopus 로고
    • Thylakoid-bound ascorbate peroxidase in spinach chloroplasts and photoreduction of its primary oxidation product monodehydroascorbate radicals in thylakoids
    • Miyake, C. and Asada, K. (1992) Thylakoid-bound ascorbate peroxidase in spinach chloroplasts and photoreduction of its primary oxidation product monodehydroascorbate radicals in thylakoids. Plant Cell Physiol. 33: 541-553.
    • (1992) Plant Cell Physiol. , vol.33 , pp. 541-553
    • Miyake, C.1    Asada, K.2
  • 19
    • 85035177222 scopus 로고
    • Inactivation mechanism of ascorbate peroxidase in the absence of ascorbate
    • Miyake, C. and Asada, K. (1994a) Inactivation mechanism of ascorbate peroxidase in the absence of ascorbate. Plant Cell Physiol. 35: s150.
    • (1994) Plant Cell Physiol. , vol.35
    • Miyake, C.1    Asada, K.2
  • 20
    • 0028155106 scopus 로고
    • Ferredoxin-dependent photoreduction of the monodehydroascorbate radical in spinach thylakoids
    • Miyake, C. and Asada, K. (1994b) Ferredoxin-dependent photoreduction of the monodehydroascorbate radical in spinach thylakoids. Plant Cell Physiol. 35: 539-549.
    • (1994) Plant Cell Physiol. , vol.35 , pp. 539-549
    • Miyake, C.1    Asada, K.2
  • 21
    • 0001073890 scopus 로고
    • Purification and molecular properties of thylakoid-bound ascorbate peroxidase in spinach chloroplasts
    • Miyake, C., Cao, W-H. and Asada, K. (1993) Purification and molecular properties of thylakoid-bound ascorbate peroxidase in spinach chloroplasts. Plant Cell Physiol. 34: 881-889.
    • (1993) Plant Cell Physiol. , vol.34 , pp. 881-889
    • Miyake, C.1    Cao, W.-H.2    Asada, K.3
  • 22
    • 0018786142 scopus 로고
    • The mechanism of indole-3-acetic acid oxidation by horseradish peroxidase
    • Nakajima, R. and Yamazaki, I. (1979) The mechanism of indole-3-acetic acid oxidation by horseradish peroxidase. J. Biol. Chem. 254: 872-878.
    • (1979) J. Biol. Chem. , vol.254 , pp. 872-878
    • Nakajima, R.1    Yamazaki, I.2
  • 23
    • 0001330378 scopus 로고
    • Spinach chloroplasts scavenge hydrogen peroxide on illumination
    • Nakano, Y. and Asada, K. (1980) Spinach chloroplasts scavenge hydrogen peroxide on illumination. Plant Cell Physiol. 21: 1295-1307.
    • (1980) Plant Cell Physiol. , vol.21 , pp. 1295-1307
    • Nakano, Y.1    Asada, K.2
  • 24
    • 0010282460 scopus 로고
    • Hydrogen peroxide is scavenged by ascorbate peroxidase in spinach chloroplasts
    • Nakano, Y. and Asada, K. (1981) Hydrogen peroxide is scavenged by ascorbate peroxidase in spinach chloroplasts. Plant Cell Physiol. 22: 867-880.
    • (1981) Plant Cell Physiol. , vol.22 , pp. 867-880
    • Nakano, Y.1    Asada, K.2
  • 25
    • 77957183372 scopus 로고
    • Purification of ascorbate peroxidase in spinach chloroplasts; its inactivation in ascorbate-depleted medium and reactivation by monodehydroascorbate radical
    • 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.
    • (1987) Plant Cell Physiol. , vol.28 , pp. 131-140
    • Nakano, Y.1    Asada, K.2
  • 27
    • 0028801954 scopus 로고
    • Attachment of CuZn-superoxide dismutase to thylakoid membranes at the site of superoxide generation (PSI) in spinach chloroplasts: Detection by immunogold labeling after rapid freezing and substitution method
    • Ogawa, K., Kanematsu, S., Takabe, K. and Asada, K. (1995) Attachment of CuZn-superoxide dismutase to thylakoid membranes at the site of superoxide generation (PSI) in spinach chloroplasts: detection by immunogold labeling after rapid freezing and substitution method. Plant Cell Physiol. 36: 565-573.
    • (1995) Plant Cell Physiol. , vol.36 , pp. 565-573
    • Ogawa, K.1    Kanematsu, S.2    Takabe, K.3    Asada, K.4
  • 28
    • 0028913020 scopus 로고
    • Identification of porphyrin π cation radical in ascorbate peroxidase compound-I
    • Patterson, W.R., Poulos, T. and Goodin, D.B. (1995) Identification of porphyrin π cation radical in ascorbate peroxidase compound-I. Biochemistry 34: 4342-4345.
    • (1995) Biochemistry , vol.34 , pp. 4342-4345
    • Patterson, W.R.1    Poulos, T.2    Goodin, D.B.3
  • 29
    • 0029089221 scopus 로고
    • Molecular characterization of monodehydroascorbate radical reductase from cucumber highly expressed in Escherichia coli
    • Sano, S., Miyake, C., Mikami, B. and Asada, K. (1995) Molecular characterization of monodehydroascorbate radical reductase from cucumber highly expressed in Escherichia coli. J. Biol. Chem. 270: 21354-21361.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21354-21361
    • Sano, S.1    Miyake, C.2    Mikami, B.3    Asada, K.4
  • 30
    • 0020200648 scopus 로고
    • The reversibility of the vitamin C redox system: Electrochemical reasons and biological aspects
    • Sapper, H., Kang, S.O., Paul, H.H. and Lohamn, W. (1982) The reversibility of the vitamin C redox system: electrochemical reasons and biological aspects. Z. Naturforsch. 37c: 942-946.
    • (1982) Z. Naturforsch. , vol.37 C , pp. 942-946
    • Sapper, H.1    Kang, S.O.2    Paul, H.H.3    Lohamn, W.4
  • 31
    • 0020546431 scopus 로고
    • Superoxide ion as active intermediate in the autooxidation of ascorbate by molecular oxygen. Effect of superoxide dismutase
    • Scarpa, M., Steranato, R., Viglino, P. and Rigo, A. (1983) Superoxide ion as active intermediate in the autooxidation of ascorbate by molecular oxygen. Effect of superoxide dismutase. J. Biol. Chem. 258: 6695-6697.
    • (1983) J. Biol. Chem. , vol.258 , pp. 6695-6697
    • Scarpa, M.1    Steranato, R.2    Viglino, P.3    Rigo, A.4
  • 32
    • 0019325168 scopus 로고
    • Purification and some properties of L-ascorbic acid-specific peroxidase in Euglena gracilis z
    • 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.
    • (1980) Arch. Biochem. Biophys. , vol.201 , pp. 121-127
    • Shigeoka, S.1    Nakano, Y.2    Kitaoka, S.3
  • 34
    • 0013818184 scopus 로고
    • 2, and ferrocytochrome c and enzymic determination of extinction coefficients of cytochrome c
    • 2, and ferrocytochrome c and enzymic determination of extinction coefficients of cytochrome c. J. Biol. Chem. 240: 4509-4514.
    • (1965) J. Biol. Chem. , vol.240 , pp. 4509-4514
    • Yonetani, T.1
  • 35
    • 0023655398 scopus 로고
    • Yeast cytochrome c peroxidase, coordination and spin states of heme prosthetic group
    • Yonetani, T. and Anni, H. (1987) Yeast cytochrome c peroxidase, coordination and spin states of heme prosthetic group. J. Biol. Chem. 262: 9547-9554.
    • (1987) J. Biol. Chem. , vol.262 , pp. 9547-9554
    • Yonetani, T.1    Anni, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.