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Volumn 52, Issue 3-4, 1997, Pages 144-152

Magnesium chelatase of Hordeum vulgare L. is not activated by light but inhibited by pheophorbide

Author keywords

Chlorophyll Synthase; Chloroplast; Etioplast Membrane Transport; Hordeum vulgare L.; Protoporphyrin

Indexed keywords

HORDEUM; HORDEUM VULGARE; HORDEUM VULGARE SUBSP. VULGARE;

EID: 1842410786     PISSN: 09395075     EISSN: None     Source Type: Journal    
DOI: 10.1515/znc-1997-3-402     Document Type: Article
Times cited : (10)

References (34)
  • 1
    • 0003128341 scopus 로고
    • Chlorophyll biosynthesis by mesophyll protoplasts and plastids from etiolated oat (Avena sativa L.) leaves
    • Benz J., Hampp R. and Rüdiger W. (1981), Chlorophyll biosynthesis by mesophyll protoplasts and plastids from etiolated oat (Avena sativa L.) leaves. Planta 152, 54-58.
    • (1981) Planta , vol.152 , pp. 54-58
    • Benz, J.1    Hampp, R.2    Rüdiger, W.3
  • 2
    • 0342360738 scopus 로고
    • Incorporation of phytol precursors into chlorophylls of tobacco cell cultures
    • Benz J., Lempert U. and Rüdiger W. (1984), Incorporation of phytol precursors into chlorophylls of tobacco cell cultures. Planta 162, 215-219.
    • (1984) Planta , vol.162 , pp. 215-219
    • Benz, J.1    Lempert, U.2    Rüdiger, W.3
  • 3
    • 0342627870 scopus 로고
    • Estimation of protochlorophyll(ide) contents in plant extracts; Re-evaluation of the molar absorption coefficient of protochlorophyll(ide)
    • Brouers M. and Michel-Wolwertz M. R. (1983), Estimation of protochlorophyll(ide) contents in plant extracts; Re-evaluation of the molar absorption coefficient of protochlorophyll(ide). Photosynth. Res. 4, 265-270.
    • (1983) Photosynth. Res. , vol.4 , pp. 265-270
    • Brouers, M.1    Michel-Wolwertz, M.R.2
  • 4
    • 0008295260 scopus 로고
    • Protoporphyrin IX and magnesium porphyrins are localized in chloroplast pigment-protein complexes
    • Russ.
    • Fradkin L. I., Titova A. E. T., Shalygo N. V. and Averina N. G. (1988), Protoporphyrin IX and magnesium porphyrins are localized in chloroplast pigment-protein complexes. Biokhimiya (Russ.) 53, 2003-2009.
    • (1988) Biokhimiya , vol.53 , pp. 2003-2009
    • Fradkin, L.I.1    Titova, A.E.T.2    Shalygo, N.V.3    Averina, N.G.4
  • 5
    • 0001314032 scopus 로고
    • Localization of Mg-chelatase and Mg-protoporphyrin IX monomethyl ester (oxidative) cyclase activities within isolated, developing cucumber chloroplasts
    • Fuesler T. P., Wong Y.-S. and Castelfranco P. A. (1984a), Localization of Mg-chelatase and Mg-protoporphyrin IX monomethyl ester (oxidative) cyclase activities within isolated, developing cucumber chloroplasts. Plant Physiol. 75, 662-664.
    • (1984) Plant Physiol. , vol.75 , pp. 662-664
    • Fuesler, T.P.1    Wong, Y.-S.2    Castelfranco, P.A.3
  • 6
    • 0000126254 scopus 로고
    • Formation of Mg-containing chlorophyll precursors from protoporphyrin XI, δ-aminolevulinic acid, and glutamate in isolated, photosynthetically competent, developing chloroplasts
    • Fuesler T. P., Castelfranco P. A. and Wong Y.-S. (1984b), Formation of Mg-containing chlorophyll precursors from protoporphyrin XI, δ-aminolevulinic acid, and glutamate in isolated, photosynthetically competent, developing chloroplasts. Plant Physiol. 74, 928-933.
    • (1984) Plant Physiol. , vol.74 , pp. 928-933
    • Fuesler, T.P.1    Castelfranco, P.A.2    Wong, Y.-S.3
  • 7
    • 0028951161 scopus 로고
    • Magnesium-protoporphyrin chelatase of Rhodobacter sphaeroides: Reconstitution of activity by combining the products of the bchH, -I, and -D genes expressed in Escherichia coli
    • Gibson L. C. D., Willows R. D., Kannangara C. G., von Wettstein D. and Hunter C. N. (1995), Magnesium-protoporphyrin chelatase of Rhodobacter sphaeroides: Reconstitution of activity by combining the products of the bchH, -I, and -D genes expressed in Escherichia coli. Proc.Natl.Acad. USA 92, 1941-1944.
    • (1995) Proc.Natl.Acad. USA , vol.92 , pp. 1941-1944
    • Gibson, L.C.D.1    Willows, R.D.2    Kannangara, C.G.3    Von Wettstein, D.4    Hunter, C.N.5
  • 8
    • 0018864205 scopus 로고
    • Substrate-specificity studies on protochlorophyllide reductase in barley (Hordeum vulgare) etioplast membranes
    • Griffiths W. T. (1980), Substrate-specificity studies on protochlorophyllide reductase in barley (Hordeum vulgare) etioplast membranes. Biochem.J. 186, 267-278.
    • (1980) Biochem.J. , vol.186 , pp. 267-278
    • Griffiths, W.T.1
  • 10
    • 0000534293 scopus 로고
    • Various metallopheophorbides as substrates for chlorophyll synthetase
    • Helfrich M. and Rüdiger W. (1992), Various metallopheophorbides as substrates for chlorophyll synthetase. Z. Naturforsch. 47c, 231-238.
    • (1992) Z. Naturforsch. , vol.47 C , pp. 231-238
    • Helfrich, M.1    Rüdiger, W.2
  • 12
    • 0001164098 scopus 로고
    • Porphyrin accumulation and export by isolated barley (Hordeum vulgare) plastids. Effect of diphenyl ether herbicides
    • Jacobs J. M. and Jacobs N. J. (1993), Porphyrin accumulation and export by isolated barley (Hordeum vulgare) plastids. Effect of diphenyl ether herbicides. Plant.Physiol. 101, 1181-1187.
    • (1993) Plant.Physiol. , vol.101 , pp. 1181-1187
    • Jacobs, J.M.1    Jacobs, N.J.2
  • 13
    • 0029895012 scopus 로고    scopus 로고
    • Expression of chlJ, chlD, and chlH genes from the cyanobacterium Synechocystis PCC6803 in Eschericha coli and demonstration that the three cognate proteins are required for magnesium-protoporphyrin chelatase activity
    • Jensen P. E., Gibson L. C. D., Henningsen K. W. and Hunter C. N. (1996a), Expression of chlJ, chlD, and chlH genes from the cyanobacterium Synechocystis PCC6803 in Eschericha coli and demonstration that the three cognate proteins are required for magnesium-protoporphyrin chelatase activity. J.Biol.Chem. 271, 16662-16667.
    • (1996) J.Biol.Chem. , vol.271 , pp. 16662-16667
    • Jensen, P.E.1    Gibson, L.C.D.2    Henningsen, K.W.3    Hunter, C.N.4
  • 15
    • 85047690585 scopus 로고
    • Possible control of transcript levels by chlorophyll precursors in Chlamydomonas
    • Johannigmeier U. (1988), Possible control of transcript levels by chlorophyll precursors in Chlamydomonas. Eur.J.Biochem. 177, 417-424.
    • (1988) Eur.J.Biochem. , vol.177 , pp. 417-424
    • Johannigmeier, U.1
  • 16
    • 0021739749 scopus 로고
    • Regulation of light-harvesting chlorophyll-binding protein mRNA accumulation in Chlamydomonas reinhardi
    • Johanningmeier U. and Howell S. H. (1984), Regulation of light-harvesting chlorophyll-binding protein mRNA accumulation in Chlamydomonas reinhardi. J.Biol.Chem. 21, 13541-13549.
    • (1984) J.Biol.Chem. , vol.21 , pp. 13541-13549
    • Johanningmeier, U.1    Howell, S.H.2
  • 17
    • 0027133813 scopus 로고
    • Chlorophyll breakdown in senescent leaves: Demonstration of Mg-chelatase activity
    • Langmeier M., Ginsburg S. and Matile P. (1993), Chlorophyll breakdown in senescent leaves: demonstration of Mg-chelatase activity. Physiol.Plant. 89, 347-353.
    • (1993) Physiol.Plant. , vol.89 , pp. 347-353
    • Langmeier, M.1    Ginsburg, S.2    Matile, P.3
  • 18
    • 0002767497 scopus 로고
    • Esterification of chlorophyllide in prolamellar body (PLB) and prothylakoid (PT) fractions from Avena sativa etioplasts
    • Lütz C., Benz J. and Rüdiger W. (1981) Esterification of chlorophyllide in prolamellar body (PLB) and prothylakoid (PT) fractions from Avena sativa etioplasts. Z.Naturforsch. 36c, 58-61.
    • (1981) Z.Naturforsch. , vol.36 C , pp. 58-61
    • Lütz, C.1    Benz, J.2    Rüdiger, W.3
  • 19
    • 1842406860 scopus 로고
    • The greening process in cress seedlings. V. Possible interference of chlorophyll precursors, accumulated after thujaplicin treatment, with light-regulated expression of Lhc genes
    • in press
    • Oster U., Brunner H. and Rüdiger W. (1977), The greening process in cress seedlings. V. Possible interference of chlorophyll precursors, accumulated after thujaplicin treatment, with light-regulated expression of Lhc genes J.Photochem.Photobiol. in press.
    • (1977) J.Photochem.Photobiol.
    • Oster, U.1    Brunner, H.2    Rüdiger, W.3
  • 20
    • 84989762261 scopus 로고
    • The localization of magnesium-protoporphyrin and protochlorophylide in separated prolamellar bodies and protylalkoids of wheat treated with 8-hydroxyquinoline and δ-aminolevulinic acid
    • Ryberg M. (1983), The localization of magnesium-protoporphyrin and protochlorophylide in separated prolamellar bodies and protylalkoids of wheat treated with 8-hydroxyquinoline and δ-aminolevulinic acid. Physiol.Plant. 59, 617-622.
    • (1983) Physiol.Plant. , vol.59 , pp. 617-622
    • Ryberg, M.1
  • 21
    • 11344295054 scopus 로고    scopus 로고
    • Reduction of the formyl group of zinc pheophorbide b in vitro and in vivo: A model for the chlorophyll b to a transformation
    • Scheumann V., Helfrich M., Schoch S. and Rüdiger W. (1996), Reduction of the formyl group of zinc pheophorbide b in vitro and in vivo: a model for the chlorophyll b to a transformation. Z.Naturtorsch. 51c, 185-194.
    • (1996) Z.Naturtorsch. , vol.51 C , pp. 185-194
    • Scheumann, V.1    Helfrich, M.2    Schoch, S.3    Rüdiger, W.4
  • 22
    • 0028912995 scopus 로고
    • Photoreduction of zinc protopheophorbide b with NADPH-protochlorophyllide oxidoreductase from etiolated wheat (Triticum aestivum L.)
    • Schoch S., Helfrich M., Wiktorsson B., Sundqvist C., Rüdiger W. and Ryberg M. (1995), Photoreduction of zinc protopheophorbide b with NADPH-protochlorophyllide oxidoreductase from etiolated wheat (Triticum aestivum L.). Eur.J.Biochem. 229, 291-298.
    • (1995) Eur.J.Biochem. , vol.229 , pp. 291-298
    • Schoch, S.1    Helfrich, M.2    Wiktorsson, B.3    Sundqvist, C.4    Rüdiger, W.5    Ryberg, M.6
  • 23
    • 0027213464 scopus 로고
    • Investigation of the subcellular location of the tetrapyrrole biosynthesis enzyme coproporphyrinogen oxidase in higher plants
    • Smith A. G., Marsh O. and Elder G. H. (1993), Investigation of the subcellular location of the tetrapyrrole biosynthesis enzyme coproporphyrinogen oxidase in higher plants. Biochem.J. 292, 503-508.
    • (1993) Biochem.J. , vol.292 , pp. 503-508
    • Smith, A.G.1    Marsh, O.2    Elder, G.H.3
  • 24
    • 0001743752 scopus 로고
    • Hydrogenation of geranylgeraniol: Two pathways exist in spinach chloroplasts
    • Soll J., Schultz G., Rüdiger W. and Benz J. (1983), Hydrogenation of geranylgeraniol: Two pathways exist in spinach chloroplasts. Plant.Physiol. 71, 849-854.
    • (1983) Plant.Physiol. , vol.71 , pp. 849-854
    • Soll, J.1    Schultz, G.2    Rüdiger, W.3    Benz, J.4
  • 25
    • 0025788026 scopus 로고
    • Holophytochrome assembly. Coupled assay for phytochromobilin synthase in organello
    • Terry M. J. and Lagarias J. C. (1991) Holophytochrome assembly. Coupled assay for phytochromobilin synthase in organello. J.Biol.Chem. 266, 22215-22221.
    • (1991) J.Biol.Chem. , vol.266 , pp. 22215-22221
    • Terry, M.J.1    Lagarias, J.C.2
  • 27
    • 0029139320 scopus 로고
    • Development of an assay for Mg-dechelatase of oilseed rape cotyledons, using chlorophyllin as the substrate
    • Vicentini F., Iten F. and Matile P. (1995), Development of an assay for Mg-dechelatase of oilseed rape cotyledons, using chlorophyllin as the substrate. Physiol.-Plant. 94, 57-63.
    • (1995) Physiol.-Plant. , vol.94 , pp. 57-63
    • Vicentini, F.1    Iten, F.2    Matile, P.3
  • 28
    • 0000641448 scopus 로고
    • Further characterization of the magnesium chelatase in isolated developing cucumber chloroplasts
    • Walker C. J. and Weinstein J. D. (1991a), Further characterization of the magnesium chelatase in isolated developing cucumber chloroplasts. Plant Physiol. 95, 1189-1196.
    • (1991) Plant Physiol. , vol.95 , pp. 1189-1196
    • Walker, C.J.1    Weinstein, J.D.2
  • 29
    • 0026077563 scopus 로고
    • In vitro assay of the chlorophyll biosynthetic enzyme Mg-chelatase: Resolution of the activity into soluble and membrane-bound fractions
    • Walker C. J. and Weinstein J. D. (1991b), In vitro assay of the chlorophyll biosynthetic enzyme Mg-chelatase: Resolution of the activity into soluble and membrane-bound fractions. Proc.Nat.Acad.Sci.USA 88, 5789-5793.
    • (1991) Proc.Nat.Acad.Sci.USA , vol.88 , pp. 5789-5793
    • Walker, C.J.1    Weinstein, J.D.2
  • 30
    • 0028316179 scopus 로고
    • The magnesium-insertion step of chlorophyll biosynthesis is a two-stage reaction
    • Walker C. J. and Weinstein J. D. (1994), The magnesium-insertion step of chlorophyll biosynthesis is a two-stage reaction. Biochem. J. 299, 277-284.
    • (1994) Biochem. J. , vol.299 , pp. 277-284
    • Walker, C.J.1    Weinstein, J.D.2
  • 31
    • 0028796972 scopus 로고
    • Reexamination of the localization of Mg-chelatase within the chloroplast
    • Walker C. J. and Weinstein J. D. (1995), Reexamination of the localization of Mg-chelatase within the chloroplast. Physiol.Plant. 94, 419-424.
    • (1995) Physiol.Plant. , vol.94 , pp. 419-424
    • Walker, C.J.1    Weinstein, J.D.2
  • 32
    • 0021099519 scopus 로고
    • Separate physiological roles and subcellular compartments for two tetrapyrrole biosynthetic pathways in Euglena gracilis
    • Weinstein J. D. and Beale S. I. (1983), Separate physiological roles and subcellular compartments for two tetrapyrrole biosynthetic pathways in Euglena gracilis. J.Biol.Chem. 258, 6799-6807.
    • (1983) J.Biol.Chem. , vol.258 , pp. 6799-6807
    • Weinstein, J.D.1    Beale, S.I.2
  • 34
    • 0029840277 scopus 로고    scopus 로고
    • Subcellular location of the tetrapyrrole synthesis enzyme porphobilinogen deaminase in higher plants: An immunological investigation
    • Witty M., Jones R. M., Robb M. S., Shoolingin-Jordan P. M. and Smith A. G. (1996), Subcellular location of the tetrapyrrole synthesis enzyme porphobilinogen deaminase in higher plants: an immunological investigation. Planta 199, 557-564.
    • (1996) Planta , vol.199 , pp. 557-564
    • Witty, M.1    Jones, R.M.2    Robb, M.S.3    Shoolingin-Jordan, P.M.4    Smith, A.G.5


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