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Volumn 7, Issue 7, 1995, Pages 1039-1057

Chlorophyll biosynthesis

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EID: 0028833696     PISSN: 10404651     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (473)

References (18)
  • 1
    • 0028694655 scopus 로고
    • The modification of acetate and propionate side chains during the biosynthesis of haem and chlorophylls: Mechanistic and stereochemical studies
    • The Biosynthesis of the Tetrapyrrole Pigments, D.J. Chadwick and K. Ackrill, eds (Chichester, England: John Wiley and Sons)
    • Akhtar, M. (1994). The modification of acetate and propionate side chains during the biosynthesis of haem and chlorophylls: Mechanistic and stereochemical studies. In The Biosynthesis of the Tetrapyrrole Pigments, Ciba Foundation Symposium 180, D.J. Chadwick and K. Ackrill, eds (Chichester, England: John Wiley and Sons), pp. 131-151.
    • (1994) Ciba Foundation Symposium , vol.180 , pp. 131-151
    • Akhtar, M.1
  • 2
    • 1842413441 scopus 로고
    • Characterization of a barley tRNA synthetase involved in chlorophyll biosynthesis
    • N. Murata, ed (The Hague: Kluwer)
    • Andersen, R.V. (1992). Characterization of a barley tRNA synthetase involved in chlorophyll biosynthesis. In Research in Photosynthesis, Vol. 3, N. Murata, ed (The Hague: Kluwer), pp. 27-30.
    • (1992) Research in Photosynthesis , vol.3 , pp. 27-30
    • Andersen, R.V.1
  • 3
    • 0029328503 scopus 로고
    • Plant carotenoids: Pigments for photoprotection, visual attraction, and human health
    • Bartley, G.E., and Scolnik, P.A. (1995). Plant carotenoids: Pigments for photoprotection, visual attraction, and human health. Plant Cell 7, 1027-1038.
    • (1995) Plant Cell , vol.7 , pp. 1027-1038
    • Bartley, G.E.1    Scolnik, P.A.2
  • 4
    • 0003066310 scopus 로고
    • The role of the light harvesting complex and photosystem II in thylakoid stacking in the chlorina-f2 barley mutant
    • Bassi, R., Hinz, U., and Barbato, R. (1985). The role of the light harvesting complex and photosystem II in thylakoid stacking in the chlorina-f2 barley mutant. Carlsberg Res. Commun. 50, 347-367.
    • (1985) Carlsberg Res. Commun. , vol.50 , pp. 347-367
    • Bassi, R.1    Hinz, U.2    Barbato, R.3
  • 5
    • 0023040607 scopus 로고
    • The implication of a plastid-derived factor in the transcriptional control of nuclear genes encoding the light-harvesting chlorophyll a/b protein
    • Batschauer, A., Mösinger, E., Kreuz, K., Dörr, I., and Apel, K. (1986). The implication of a plastid-derived factor in the transcriptional control of nuclear genes encoding the light-harvesting chlorophyll a/b protein. Eur. J. Biochem. 154, 625-634.
    • (1986) Eur. J. Biochem. , vol.154 , pp. 625-634
    • Batschauer, A.1    Mösinger, E.2    Kreuz, K.3    Dörr, I.4    Apel, K.5
  • 6
    • 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 E. coli
    • Gibson, L.C., 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 E. coli. Proc. Natl. Acad. Sci. USA 92, 1941-1944.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 1941-1944
    • Gibson, L.C.1    Willows, R.D.2    Kannangara, C.G.3    Von Wettstein, D.4    Hunter, C.N.5
  • 7
    • 0026676696 scopus 로고
    • Cloning and characterization of the Bacillus subtilis hemEHY gene cluster, which encodes protoheme IX biosynthetic enzymes
    • Hansson, M., and Hederstedt, L. (1992). Cloning and characterization of the Bacillus subtilis hemEHY gene cluster, which encodes protoheme IX biosynthetic enzymes. J. Bacteriol. 174, 8081-8093.
    • (1992) J. Bacteriol. , vol.174 , pp. 8081-8093
    • Hansson, M.1    Hederstedt, L.2
  • 8
    • 85115039665 scopus 로고
    • The biosynthesis of uroporphyrinogen III: Mechanism of action of porphobilinogen deaminase
    • The Biosynthesis of the Tetrapyrrole Pigments, D.J. Chadwick and K. Ackrill, eds (Chichester, England: John Wiley and Sons)
    • Jordan, P.M. (1994). The biosynthesis of uroporphyrinogen III: Mechanism of action of porphobilinogen deaminase. In The Biosynthesis of the Tetrapyrrole Pigments, Ciba Foundation Symposium 180, D.J. Chadwick and K. Ackrill, eds (Chichester, England: John Wiley and Sons), pp. 50-64.
    • (1994) Ciba Foundation Symposium , vol.180 , pp. 50-64
    • Jordan, P.M.1
  • 9
    • 0002943854 scopus 로고
    • Genetic regulation of chlorophyll synthesis analyzed with double mutants in barley
    • T. Bücher, W. Neupert, W. Sebald, and S. Werner, eds (Amsterdam: North Holland)
    • Kahn, A., Avivi-Bleiser, N., and von Wettstein, D. (1976). Genetic regulation of chlorophyll synthesis analyzed with double mutants in barley. In Genetics and Biogenesis of Chloroplasts and Mitochondria T. Bücher, W. Neupert, W. Sebald, and S. Werner, eds (Amsterdam: North Holland), pp. 119-131.
    • (1976) Genetics and Biogenesis of Chloroplasts and Mitochondria , pp. 119-131
    • Kahn, A.1    Avivi-Bleiser, N.2    Von Wettstein, D.3
  • 11
    • 0027673660 scopus 로고
    • A soybean coproporphyrinogen oxidase gene is highly expressed in root nodules
    • Madsen, O., Sandal, L., Sandal, N.N., and Marcker, K.A. (1993). A soybean coproporphyrinogen oxidase gene is highly expressed in root nodules. Plant Mol. Biol. 23, 35-43.
    • (1993) Plant Mol. Biol. , vol.23 , pp. 35-43
    • Madsen, O.1    Sandal, L.2    Sandal, N.N.3    Marcker, K.A.4
  • 12
    • 0015767767 scopus 로고
    • Mutations affecting porphyrin biosynthesis in Escherichia coli
    • Powell, K.A., Cox, R., McConville, M., and Charles, H.P. (1973). Mutations affecting porphyrin biosynthesis in Escherichia coli. Enzyme 16, 65-73
    • (1973) Enzyme , vol.16 , pp. 65-73
    • Powell, K.A.1    Cox, R.2    McConville, M.3    Charles, H.P.4
  • 13
    • 0028342739 scopus 로고
    • Chloroplastic genomes of Gingko biloba and Chlamydomonas moewusii contain a chIB gene encoding one subunit of light-independent protochiorophyllide reductase
    • Richard, M., Tremblay, C., and Bellemare, G. (1994). Chloroplastic genomes of Gingko biloba and Chlamydomonas moewusii contain a chIB gene encoding one subunit of light-independent protochiorophyllide reductase. Curr. Genet. 26, 159-165.
    • (1994) Curr. Genet. , vol.26 , pp. 159-165
    • Richard, M.1    Tremblay, C.2    Bellemare, G.3
  • 14
    • 0029065496 scopus 로고
    • A prokaryotic origin of light-dependent chlorophyll biosynthesis of plants
    • in press
    • Suzuki. J.Y., and Bauer, C.E. (1995). A prokaryotic origin of light-dependent chlorophyll biosynthesis of plants. Proc. Natl. Acad. Sci. USA. in press.
    • (1995) Proc. Natl. Acad. Sci. USA.
    • Suzuki, J.Y.1    Bauer, C.E.2
  • 15
    • 0001410510 scopus 로고
    • The formation of plastid structure
    • The Photochemical Apparatus, Its Structure and Function. (Upton, NY: Brookhaven National Laboratory)
    • von Wettstein, D. (1958). The formation of plastid structure. In The Photochemical Apparatus, Its Structure and Function. Brookhaven Symposium Biology 11 (Upton, NY: Brookhaven National Laboratory), pp. 138-159.
    • (1958) Brookhaven Symposium Biology , vol.11 , pp. 138-159
    • Von Wettstein, D.1
  • 16
    • 0029021234 scopus 로고
    • Glu involved in recognition by barley chloroplast glutamyl-tRNA synthetase and glutamyMRNA reductase
    • in press
    • Glu involved in recognition by barley chloroplast glutamyl-tRNA synthetase and glutamyMRNA reductase. Biochim. Biophys. Acta, in press.
    • (1995) Biochim. Biophys. Acta
    • Willows, R.1    Kannangara, C.G.2    Pontoppidan, B.3
  • 17
    • 0027667070 scopus 로고
    • Structure and expression of chloroplast-localized porphobilinogen deaminase from pea (Pisum sativum L.) isolated by redundant polymerase chain reaction
    • Witty, M., Wallace-Cook, A.D.M., Albrecht, H., Spano, A.J., Michel, H., Shabanowitz, J., Hunt, D.F., Timko, M.P., and Smith, A.G. (1993). Structure and expression of chloroplast-localized porphobilinogen deaminase from pea (Pisum sativum L.) isolated by redundant polymerase chain reaction. Plant Physiol. 103, 139-147.
    • (1993) Plant Physiol. , vol.103 , pp. 139-147
    • Witty, M.1    Wallace-Cook, A.D.M.2    Albrecht, H.3    Spano, A.J.4    Michel, H.5    Shabanowitz, J.6    Hunt, D.F.7    Timko, M.P.8    Smith, A.G.9
  • 18
    • 0028302959 scopus 로고
    • Evidence for participation of aspartate-84 as a catalytic group at the active site of porphobilinogen deaminase obtained by site-directed mutagenesis of the hemC gene from Escherichia coli
    • Woodcock, S.C., and Jordan, P.M. (1994). Evidence for participation of aspartate-84 as a catalytic group at the active site of porphobilinogen deaminase obtained by site-directed mutagenesis of the hemC gene from Escherichia coli. Biochemistry 33, 2688-2695.
    • (1994) Biochemistry , vol.33 , pp. 2688-2695
    • Woodcock, S.C.1    Jordan, P.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.