메뉴 건너뛰기




Volumn 69, Issue 4, 2005, Pages 762-772

Purification and cDNA cloning of chloroplastic monodehydroascorbate reductase from spinach

Author keywords

Active oxygen; Ascorbate radical; Chloroplastic isoform; Monodehydroascorbate reductase (EC 1.6.4.7); Spinach (Spinacea oleracea)

Indexed keywords

AMINO ACIDS; CELLS; CLONING; DNA; ENZYMES; ESCHERICHIA COLI; GENES; PURIFICATION;

EID: 20444416392     PISSN: 09168451     EISSN: None     Source Type: Journal    
DOI: 10.1271/bbb.69.762     Document Type: Article
Times cited : (46)

References (38)
  • 1
    • 0033513358 scopus 로고    scopus 로고
    • The water-water cycle in chloroplasts: Scavenging of active oxygens and dissipation of excess photons
    • Asada, K., The water-water cycle in chloroplasts: scavenging of active oxygens and dissipation of excess photons. Annu. Rev. Plant Physiol. Plant Mol. Biol., 50, 601-639 (1999).
    • (1999) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.50 , pp. 601-639
    • Asada, K.1
  • 2
    • 0001073890 scopus 로고
    • Purification and molecular properties of thylakoid-bound ascorbate peroxidase in spinach chloroplasts
    • Miyake, C., Cao, W.-H., and Asada, K., Purification and molecular properties of thylakoid-bound ascorbate peroxidase in spinach chloroplasts. Plant Cell Physiol., 34, 881-889 (1993).
    • (1993) Plant Cell Physiol. , vol.34 , pp. 881-889
    • Miyake, C.1    Cao, W.-H.2    Asada, K.3
  • 3
    • 77957181306 scopus 로고
    • Thylakoid-bound ascorbate peroxidase in spinach chloroplasts and photoreductioin of its primary oxidation product monodehydroascorbate radicals in thylakoids
    • Miyake, C., and Asada, K., Thylakoid-bound ascorbate peroxidase in spinach chloroplasts and photoreductioin of its primary oxidation product monodehydroascorbate radicals in thylakoids. Plant Cell Physiol., 33, 541-553 (1992).
    • (1992) Plant Cell Physiol. , vol.33 , pp. 541-553
    • Miyake, C.1    Asada, K.2
  • 4
    • 0000918942 scopus 로고
    • Monodehydroascorbate reductase in spinach chloroplasts and its participation in regeneration of ascorbate for scavenging of hydrogen peroxide
    • Hossain, M. A., Nakano, Y., and Asada, K., Monodehydroascorbate reductase in spinach chloroplasts and its participation in regeneration of ascorbate for scavenging of hydrogen peroxide. Plant Cell Physiol., 25, 385-395 (1984).
    • (1984) Plant Cell Physiol. , vol.25 , pp. 385-395
    • Hossain, M.A.1    Nakano, Y.2    Asada, K.3
  • 5
    • 0028155106 scopus 로고
    • Ferredoxin-dependent photo-reduction of the monodehydroascorbate radical in spinach thylakoids
    • Miyake, C., and Asada, K., Ferredoxin-dependent photo-reduction of the monodehydroascorbate radical in spinach thylakoids. Plant Cell Physiol., 35, 539-549 (1994).
    • (1994) Plant Cell Physiol. , vol.35 , pp. 539-549
    • Miyake, C.1    Asada, K.2
  • 6
    • 0028934243 scopus 로고
    • Formation and decay of monodehydro-ascorbate radicals in illuminated thylakoids as determined by EPR spectroscopy
    • Grace, S., Pace, R., and Wydrzynski, T., Formation and decay of monodehydro-ascorbate radicals in illuminated thylakoids as determined by EPR spectroscopy. Biochim. Biophys. Acta, 1229, 155-165 (1995).
    • (1995) Biochim. Biophys. Acta , vol.1229 , pp. 155-165
    • Grace, S.1    Pace, R.2    Wydrzynski, T.3
  • 7
    • 0001662170 scopus 로고
    • Ascorbate free radical reductase, a key enzyme of the ascorbic acid system
    • Arrigoni, O., Dipierro, S., and Borraccino, G., Ascorbate free radical reductase, a key enzyme of the ascorbic acid system. FEBS Lett., 125, 242-245 (1981).
    • (1981) FEBS Lett. , vol.125 , pp. 242-245
    • Arrigoni, O.1    Dipierro, S.2    Borraccino, G.3
  • 8
    • 0029189399 scopus 로고
    • A specific ascorbate free radical reductase isozyme participates in the regeneration of ascorbate for scavenging toxic oxygen species in potato tuber mitochondria
    • De Leonardis, S., De Lorenzo, G., Borraccino, G., and Dipierro, S., A specific ascorbate free radical reductase isozyme participates in the regeneration of ascorbate for scavenging toxic oxygen species in potato tuber mitochondria. Plant Physiol., 109, 847-851 (1995).
    • (1995) Plant Physiol. , vol.109 , pp. 847-851
    • De Leonardis, S.1    De Lorenzo, G.2    Borraccino, G.3    Dipierro, S.4
  • 9
    • 0039552192 scopus 로고    scopus 로고
    • Characterization of membrane polypeptides from pea leaf peroxisomes involved in superoxide radical generation
    • Lopez-Huertas, E., Corpas, F. J., Sandalio, L. M., and Del Rio, L. A., Characterization of membrane polypeptides from pea leaf peroxisomes involved in superoxide radical generation. Biochem. J., 337, 531-536 (1999).
    • (1999) Biochem. J. , vol.337 , pp. 531-536
    • Lopez-Huertas, E.1    Corpas, F.J.2    Sandalio, L.M.3    Del Rio, L.A.4
  • 10
    • 20444377510 scopus 로고    scopus 로고
    • Identification of a 54-kD Arabidopsis peroxisomal membrane monodehydroascorbate reductase (AtMDAR54p) that likely sorts to peroxisomes via peroxisomal endoplasmic reticulum
    • Denver
    • Lisenbee, C. S., and Trelease, R. N., Identification of a 54-kD Arabidopsis peroxisomal membrane monodehydroascorbate reductase (AtMDAR54p) that likely sorts to peroxisomes via peroxisomal endoplasmic reticulum. Plant Biology 2002, Denver, #227 (2002).
    • (2002) Plant Biology 2002 , pp. 227
    • Lisenbee, C.S.1    Trelease, R.N.2
  • 11
    • 0000796913 scopus 로고
    • Ascorbate free-radical reduction by glyoxysomal membrane
    • Bowditch, M. I., and Donaldson, R. P., Ascorbate free-radical reduction by glyoxysomal membrane. Plant Physiol., 94, 531-537 (1990).
    • (1990) Plant Physiol. , vol.94 , pp. 531-537
    • Bowditch, M.I.1    Donaldson, R.P.2
  • 12
    • 0030087896 scopus 로고    scopus 로고
    • Ascorbate peroxidase. A prominent membrane protein in oilseed glyoxysomes
    • Bunkelmann, J. R., and Trelease, R. N., Ascorbate peroxidase. A prominent membrane protein in oilseed glyoxysomes. Plant Physiol., 110, 589-598 (1996).
    • (1996) Plant Physiol. , vol.110 , pp. 589-598
    • Bunkelmann, J.R.1    Trelease, R.N.2
  • 13
    • 0542444213 scopus 로고    scopus 로고
    • NADH-monodehydroascorbate oxidoreductase is one of the redox enzymes in spinach leaf plasma membranes
    • Berczi, A., and Møller, I. M., NADH-monodehydroascorbate oxidoreductase is one of the redox enzymes in spinach leaf plasma membranes. Plant Physiol., 116, 1029-1036 (1998).
    • (1998) Plant Physiol. , vol.116 , pp. 1029-1036
    • Berczi, A.1    Møller, I.M.2
  • 14
    • 0033179358 scopus 로고    scopus 로고
    • Spectral characterization and chemical modification of FMN-containing ascorbyl free-radical reductase from Pleurotus ostreatus
    • Yu, S. W., Kim, Y. R., and Kang, S. O., Spectral characterization and chemical modification of FMN-containing ascorbyl free-radical reductase from Pleurotus ostreatus. Biochem. J., 341, 755-763 (1999).
    • (1999) Biochem. J. , vol.341 , pp. 755-763
    • Yu, S.W.1    Kim, Y.R.2    Kang, S.O.3
  • 15
    • 0028407352 scopus 로고
    • cDNA cloning of monodehydroascorbate radical reductase from cucumber: A high degree of homology in terms of amino acid sequence between this enzyme and bacterial flavoenzymes
    • Sano, S., and Asada, K., cDNA cloning of monodehydroascorbate radical reductase from cucumber: a high degree of homology in terms of amino acid sequence between this enzyme and bacterial flavoenzymes. Plant Cell Physiol., 35, 425-437 (1994).
    • (1994) Plant Cell Physiol. , vol.35 , pp. 425-437
    • Sano, S.1    Asada, K.2
  • 17
    • 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., Molecular characterization of monodehydroascorbate radical reductase from cucumber highly expressed in Escherichia coli. J. Biol. Chem., 270, 21354-21361 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 21354-21361
    • Sano, S.1    Miyake, C.2    Mikami, B.3    Asada, K.4
  • 18
    • 0028825699 scopus 로고
    • A direct demonstration of the catalytic action of monodehydroascorbate reductase by pulse radiolysis
    • Kobayashi, K., Tagawa, S., Sano, S., and Asada, K., A direct demonstration of the catalytic action of monodehydroascorbate reductase by pulse radiolysis. J. Biol. Chem., 270, 27551-27554 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 27551-27554
    • Kobayashi, K.1    Tagawa, S.2    Sano, S.3    Asada, K.4
  • 19
    • 0031694497 scopus 로고    scopus 로고
    • The FAD-enzyme monodehydroascorbate radical reductase mediates photoproduction of superoxide radicals in spinach thylakoid membranes
    • Miyake, C., Schreiber, U., Hormann, H., Sano, S., and Asada, K., The FAD-enzyme monodehydroascorbate radical reductase mediates photoproduction of superoxide radicals in spinach thylakoid membranes. Plant Cell Physiol., 39, 821-829 (1998).
    • (1998) Plant Cell Physiol. , vol.39 , pp. 821-829
    • Miyake, C.1    Schreiber, U.2    Hormann, H.3    Sano, S.4    Asada, K.5
  • 21
    • 0022372087 scopus 로고
    • Monodehydroascorbate reductase from cucumber is a flavin adenine dinucleotide enzyme
    • Hossain, M. A., and Asada, K., Monodehydroascorbate reductase from cucumber is a flavin adenine dinucleotide enzyme. J. Biol. Chem., 260, 12920-12926 (1985).
    • (1985) J. Biol. Chem. , vol.260 , pp. 12920-12926
    • Hossain, M.A.1    Asada, K.2
  • 22
    • 0000594637 scopus 로고
    • Purification and properties of ascorbate free-radical reductase from potato tubers
    • Borraccino, G., Dipierro, S., and Arrigoni, O., Purification and properties of ascorbate free-radical reductase from potato tubers. Planta, 167, 521-526 (1986).
    • (1986) Planta , vol.167 , pp. 521-526
    • Borraccino, G.1    Dipierro, S.2    Arrigoni, O.3
  • 23
    • 0026530853 scopus 로고
    • Purification and characterization of monodehydroascorbate reductase from soybean root nodules
    • Dalton, D. A., Langeberg, L., and Robbins, M., Purification and characterization of monodehydroascorbate reductase from soybean root nodules. Arch. Biochem. Biophys., 292, 281-286 (1992).
    • (1992) Arch. Biochem. Biophys. , vol.292 , pp. 281-286
    • Dalton, D.A.1    Langeberg, L.2    Robbins, M.3
  • 24
    • 0028151023 scopus 로고
    • Molecular cloning and characterization of a cDNA encoding pea monodehydroascorbate reductase
    • Murthy, S. S., and Zilinskas, B. A., Molecular cloning and characterization of a cDNA encoding pea monodehydroascorbate reductase. J. Biol. Chem., 269, 31129-31133 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 31129-31133
    • Murthy, S.S.1    Zilinskas, B.A.2
  • 25
    • 0029294106 scopus 로고
    • Ascorbate free radical reductase mRNA levels are induced by wounding
    • Grantz, A. A., Brummell, D. A., and Bennett, A. B., Ascorbate free radical reductase mRNA levels are induced by wounding. Plant Physiol., 108, 411-418 (1995).
    • (1995) Plant Physiol. , vol.108 , pp. 411-418
    • Grantz, A.A.1    Brummell, D.A.2    Bennett, A.B.3
  • 26
    • 20444383718 scopus 로고    scopus 로고
    • Dual targeting of monodehydroascorbate reductase of Arabidopsis to mitochondria and chloroplast
    • Mizota, T., Kawazu, Y., Yasuda, S., Morita, S., Sano, S., and Saito, K., Dual targeting of monodehydroascorbate reductase of Arabidopsis to mitochondria and chloroplast. Plant Cell Physiol., 43 (Suppl.), s97 (2002).
    • (2002) Plant Cell Physiol. , vol.43 , Issue.SUPPL.
    • Mizota, T.1    Kawazu, Y.2    Yasuda, S.3    Morita, S.4    Sano, S.5    Saito, K.6
  • 27
    • 0036348737 scopus 로고    scopus 로고
    • The use of multiple transcription starts causes the dual targeting of Arabidopsis putative monodehydroascorbate reductase to both mitochondria and chloroplasts
    • Obara, K., Sumi, K., and Fukuda, H., The use of multiple transcription starts causes the dual targeting of Arabidopsis putative monodehydroascorbate reductase to both mitochondria and chloroplasts. Plant Cell Physiol., 43, 697-705 (2002).
    • (2002) Plant Cell Physiol. , vol.43 , pp. 697-705
    • Obara, K.1    Sumi, K.2    Fukuda, H.3
  • 28
    • 0344875538 scopus 로고    scopus 로고
    • Molecular definition of the ascorbate-glutathione cycle in Arabidopsis mitochondria reveals dual targeting of antioxidant defenses in plants
    • Chew, O., Whelan, J., and Millar, A. H., Molecular definition of the ascorbate-glutathione cycle in Arabidopsis mitochondria reveals dual targeting of antioxidant defenses in plants. J. Biol. Chem., 278, 46869-46877 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 46869-46877
    • Chew, O.1    Whelan, J.2    Millar, A.H.3
  • 30
    • 0000389413 scopus 로고
    • Methyl viologen-dependent cyclic electron transport in spinach chloroplasts in the absence of oxygen
    • Asada, K., Neubauer, C., Heber, U., and Schreiber, U., Methyl viologen-dependent cyclic electron transport in spinach chloroplasts in the absence of oxygen. Plant Cell Physiol., 31, 557-564 (1990).
    • (1990) Plant Cell Physiol. , vol.31 , pp. 557-564
    • Asada, K.1    Neubauer, C.2    Heber, U.3    Schreiber, U.4
  • 31
    • 0014817034 scopus 로고
    • Direct and indirect transfer of ATP and ADP across the chloroplast envelope
    • Heber, U., and Santarius, K. A., Direct and indirect transfer of ATP and ADP across the chloroplast envelope. Z. Naturforsch. B, 25, 718-728 (1970).
    • (1970) Z. Naturforsch. B , vol.25 , pp. 718-728
    • Heber, U.1    Santarius, K.A.2
  • 32
    • 0017333009 scopus 로고
    • Oxidation of ascorbate anion by electron transfer to phenoxyl radicals
    • Schuler, R. H., Oxidation of ascorbate anion by electron transfer to phenoxyl radicals. Rad. Res., 69, 417-433 (1977).
    • (1977) Rad. Res. , vol.69 , pp. 417-433
    • Schuler, R.H.1
  • 33
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem., 72, 248-254 (1976).
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 34
    • 0343887396 scopus 로고
    • Comparative characterization of ferredoxins from heterocysts and vegetative cells of Anabaena variabilis
    • Böhme, H., and Schrautemeier, S., Comparative characterization of ferredoxins from heterocysts and vegetative cells of Anabaena variabilis. Biochim. Biophys. Acta, 981, 1-7 (1987).
    • (1987) Biochim. Biophys. Acta , vol.981 , pp. 1-7
    • Böhme, H.1    Schrautemeier, S.2
  • 35
    • 38249025545 scopus 로고
    • Interaction of ascorbate free radical reductase with sulphhydryl reagents
    • Borraccino, G., Dipierro, S., and Arrigoni, O., Interaction of ascorbate free radical reductase with sulphhydryl reagents. Phytochemistry, 28, 715-717 (1989).
    • (1989) Phytochemistry , vol.28 , pp. 715-717
    • Borraccino, G.1    Dipierro, S.2    Arrigoni, O.3
  • 37
    • 1042264042 scopus 로고    scopus 로고
    • Crystal structure of putidaredoxin reductase from Pseudomonas putida, the final structural component of the cytochromeP450cam monooxygenase
    • Sevrioukova, I. F., Li, H., and Poulos, T. L., Crystal structure of putidaredoxin reductase from Pseudomonas putida, the final structural component of the cytochromeP450cam monooxygenase. J. Mol. Biol., 336, 889-902 (2004).
    • (2004) J. Mol. Biol. , vol.336 , pp. 889-902
    • Sevrioukova, I.F.1    Li, H.2    Poulos, T.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.