메뉴 건너뛰기




Volumn 8, Issue 5, 1996, Pages 763-769

PORA and PORB, two light-dependent protochlorophyllide-reducing enzymes of angiosperm chlorophyll biosynthesis

Author keywords

[No Author keywords available]

Indexed keywords

MAGNOLIOPHYTA;

EID: 0000448607     PISSN: 10404651     EISSN: None     Source Type: Journal    
DOI: 10.2307/3870279     Document Type: Review
Times cited : (107)

References (63)
  • 1
    • 0019638624 scopus 로고
    • The protochlorophyllide holochrome of barley (Hordeum vulgare L). Phytochrome-induced decrease of translatable mRNA coding for the NADPH:protochlorophyllide oxidoreductase
    • Apel, K. (1981). The protochlorophyllide holochrome of barley (Hordeum vulgare L). Phytochrome-induced decrease of translatable mRNA coding for the NADPH:protochlorophyllide oxidoreductase. Eur. J. Biochem. 120, 89-93.
    • (1981) Eur. J. Biochem. , vol.120 , pp. 89-93
    • Apel, K.1
  • 2
    • 0000528190 scopus 로고
    • The effect of light on the biosynthesis of the light-harvesting chlorophyll a/b protein. Evidence for the requirement of chlorophyll a for the stabilization of the apoprotein
    • Apel, K., and Kloppstech, K. (1980). The effect of light on the biosynthesis of the light-harvesting chlorophyll a/b protein. Evidence for the requirement of chlorophyll a for the stabilization of the apoprotein. Planta 150, 426-430.
    • (1980) Planta , vol.150 , pp. 426-430
    • Apel, K.1    Kloppstech, K.2
  • 3
    • 0019073797 scopus 로고
    • The protochlorophyllide holochrome of barley. Isolation and characterization of the NADPH:protochlorophyllide oxidoreductase
    • Apel, K., Santel, H.-J., Redlinger, T.E., and Falk, H. (1980). The protochlorophyllide holochrome of barley. Isolation and characterization of the NADPH:protochlorophyllide oxidoreductase. Eur. J. Biochem. 111, 251-258.
    • (1980) Eur. J. Biochem. , vol.111 , pp. 251-258
    • Apel, K.1    Santel, H.-J.2    Redlinger, T.E.3    Falk, H.4
  • 4
    • 0029346958 scopus 로고
    • Identification of protochlorophyllide oxidoreductases A and B: A branched pathway for light-dependent chlorophyll biosynthesis in Arabidopsis thaliana
    • Armstrong, G.A., Runge, S., Frick, G., Sperling, U., and Apel, K. (1995). Identification of protochlorophyllide oxidoreductases A and B: A branched pathway for light-dependent chlorophyll biosynthesis in Arabidopsis thaliana. Plant Physiol. 108, 1505-1517.
    • (1995) Plant Physiol. , vol.108 , pp. 1505-1517
    • Armstrong, G.A.1    Runge, S.2    Frick, G.3    Sperling, U.4    Apel, K.5
  • 5
    • 0028226211 scopus 로고
    • Protochlorophyllide oxidoreductase is homologous to human carbonyl reductase and pig 20β-hydroxysteroid dehydrogenase
    • Baker, M.E. (1994). Protochlorophyllide oxidoreductase is homologous to human carbonyl reductase and pig 20β-hydroxysteroid dehydrogenase. Biochem. J. 300, 605-607.
    • (1994) Biochem. J. , vol.300 , pp. 605-607
    • Baker, M.E.1
  • 6
    • 0021766006 scopus 로고
    • An inverse control by phytochrome of the expression of two nuclear genes in barley
    • Batschauer, A., and Apel, K. (1984). An inverse control by phytochrome of the expression of two nuclear genes in barley. Eur. J. Biochem. 143, 593-597.
    • (1984) Eur. J. Biochem. , vol.143 , pp. 593-597
    • Batschauer, A.1    Apel, K.2
  • 7
    • 0000501058 scopus 로고
    • Protochlorophyllide reductase. 1. Determination of the regiochemistry and the stereochemistry of the reduction of protochlorophyllide to chlorophyllide
    • Begley, T., and Young, H. (1989). Protochlorophyllide reductase. 1. Determination of the regiochemistry and the stereochemistry of the reduction of protochlorophyllide to chlorophyllide. J. Am. Chem. Soc. 111, 3095-3096.
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 3095-3096
    • Begley, T.1    Young, H.2
  • 8
    • 0026149940 scopus 로고
    • Effect of light on the NADPH-protochlorophyllide oxidoreductase of Arabidopsis thaliana
    • Benli, M., Schulz, R., and Apel, K. (1991). Effect of light on the NADPH-protochlorophyllide oxidoreductase of Arabidopsis thaliana. Plant Mol. Biol. 16, 615-625.
    • (1991) Plant Mol. Biol. , vol.16 , pp. 615-625
    • Benli, M.1    Schulz, R.2    Apel, K.3
  • 9
    • 0019597638 scopus 로고
    • Biosynthesis of the light-harvesting chlorophyll a/b-protein. Polypeptide turnover in darkness
    • Bennett, J. (1981). Biosynthesis of the light-harvesting chlorophyll a/b-protein. Polypeptide turnover in darkness. Eur. J. Biochem. 118, 61-70.
    • (1981) Eur. J. Biochem. , vol.118 , pp. 61-70
    • Bennett, J.1
  • 10
    • 6944234779 scopus 로고
    • Biochemistry of chloroplasts
    • T.W. Goodwin, ed (New York: Academic Press)
    • Bogorad, L. (1967). Biochemistry of chloroplasts. In Biosynthesis and Morphogenesis in Plants, T.W. Goodwin, ed (New York: Academic Press), pp. 615-631.
    • (1967) Biosynthesis and Morphogenesis in Plants , pp. 615-631
    • Bogorad, L.1
  • 11
    • 0024965016 scopus 로고
    • Arabidopsis thaliana mutant that develops as a light-grown plant in the absence of light
    • Chory, J., Peto, C., Feinbaum, R., Pratt, L., and Ausubel, F. (1989). Arabidopsis thaliana mutant that develops as a light-grown plant in the absence of light. Cell 58, 991-999.
    • (1989) Cell , vol.58 , pp. 991-999
    • Chory, J.1    Peto, C.2    Feinbaum, R.3    Pratt, L.4    Ausubel, F.5
  • 12
    • 0025129263 scopus 로고
    • Cloning and sequencing of protochlorophyllide reductase
    • Darrah, P.M., Kay, S.A., Teakle, J.R., and Griffiths, W.T. (1990). Cloning and sequencing of protochlorophyllide reductase. Biochem. J. 265, 789-798.
    • (1990) Biochem. J. , vol.265 , pp. 789-798
    • Darrah, P.M.1    Kay, S.A.2    Teakle, J.R.3    Griffiths, W.T.4
  • 13
    • 0012305224 scopus 로고
    • The NADPH-protochlorophyllide oxidoreductase is the major protein constituent of prolamellar bodies in wheat (Triticum aestivum L.)
    • Dehesh, K., and Ryberg, M. (1985). The NADPH-protochlorophyllide oxidoreductase is the major protein constituent of prolamellar bodies in wheat (Triticum aestivum L.). Planta 164, 396-399.
    • (1985) Planta , vol.164 , pp. 396-399
    • Dehesh, K.1    Ryberg, M.2
  • 14
    • 34250130280 scopus 로고
    • Light-induced changes in the distribution of the 36000-Mr polypeptide of NADPH-protochlorophyllide oxidoreductase within different cellular compartments of barley (Hordeum vulgare L.). I. Localisation by immunoblotting in isolated plastids and total leaf extracts
    • Dehesh, K., Klaas, M., Häuser, I., and Apel, K. (1986). Light-induced changes in the distribution of the 36000-Mr polypeptide of NADPH-protochlorophyllide oxidoreductase within different cellular compartments of barley (Hordeum vulgare L.). I. Localisation by immunoblotting in isolated plastids and total leaf extracts. Planta 169, 162-171.
    • (1986) Planta , vol.169 , pp. 162-171
    • Dehesh, K.1    Klaas, M.2    Häuser, I.3    Apel, K.4
  • 15
    • 0027291060 scopus 로고
    • Acceptor side mechanism of photoinduced proteolysis of the D1 protein in photosystem II reaction centers
    • De Las Rivas, J.D.L., Shipton, C., Ponticos, M., and Barber, J. (1993). Acceptor side mechanism of photoinduced proteolysis of the D1 protein in photosystem II reaction centers. Biochemistry 32, 6944-6950.
    • (1993) Biochemistry , vol.32 , pp. 6944-6950
    • De Las Rivas, J.D.L.1    Shipton, C.2    Ponticos, M.3    Barber, J.4
  • 16
    • 0027422649 scopus 로고
    • Light-independent and light-dependent protochlorophyllide-reducing activities and two distinct NADPH-protochlorophyllide oxidoreductase polypeptides in mountain pine (Pinus mugo)
    • Forreiter, C., and Apel, K. (1993). Light-independent and light-dependent protochlorophyllide-reducing activities and two distinct NADPH-protochlorophyllide oxidoreductase polypeptides in mountain pine (Pinus mugo). Planta 190, 536-545.
    • (1993) Planta , vol.190 , pp. 536-545
    • Forreiter, C.1    Apel, K.2
  • 17
    • 0001005946 scopus 로고
    • Evidence for a general light-dependent negative control of NADPH-protochlorophyllide oxidoreductase in angiosperms
    • Forreiter, C., van Cleve, B., Schmidt, A., and Apel, K. (1990). Evidence for a general light-dependent negative control of NADPH-protochlorophyllide oxidoreductase in angiosperms. Planta 183, 126-132.
    • (1990) Planta , vol.183 , pp. 126-132
    • Forreiter, C.1    Van Cleve, B.2    Schmidt, A.3    Apel, K.4
  • 18
    • 0026668652 scopus 로고
    • Detection of the photoactive protochlorophyllide complex in the light during the greening of barley
    • Franck, F., and Strzalka, K. (1992). Detection of the photoactive protochlorophyllide complex in the light during the greening of barley. FEBS Lett. 309, 73-77.
    • (1992) FEBS Lett. , vol.309 , pp. 73-77
    • Franck, F.1    Strzalka, K.2
  • 19
    • 0038531356 scopus 로고
    • The structural and functional relationship between heme and chlorophyll
    • Granick, S. (1950). The structural and functional relationship between heme and chlorophyll. Harvey Lectures 44, 220-245.
    • (1950) Harvey Lectures , vol.44 , pp. 220-245
    • Granick, S.1
  • 20
    • 0018076305 scopus 로고
    • Reconstitution of chlorophyll formation by isolated etioplast membranes
    • Griffiths, W.T. (1978). Reconstitution of chlorophyll formation by isolated etioplast membranes. Biochem. J. 174, 681-692.
    • (1978) Biochem. J. , vol.174 , pp. 681-692
    • Griffiths, W.T.1
  • 21
    • 0021382276 scopus 로고
    • The proteolytic degradation in vitro of the NADPH-protochlorophyllide oxidoreductase of barley (Hordeum vulgare L.)
    • Häuser, I., Dehesh, K., and Apel, K. (1984). The proteolytic degradation in vitro of the NADPH-protochlorophyllide oxidoreductase of barley (Hordeum vulgare L.). Arch. Biochem. Biophys. 228, 577-586.
    • (1984) Arch. Biochem. Biophys. , vol.228 , pp. 577-586
    • Häuser, I.1    Dehesh, K.2    Apel, K.3
  • 22
    • 0014876110 scopus 로고
    • Macromolecular physiology of plastids. IV. Changes in membrane structure associated with shifts in the absorption maxima of chlorophyllous pigments
    • Henningsen, K.W. (1970). Macromolecular physiology of plastids. IV. Changes in membrane structure associated with shifts in the absorption maxima of chlorophyllous pigments. J. Cell Sci. 7, 587-621.
    • (1970) J. Cell Sci. , vol.7 , pp. 587-621
    • Henningsen, K.W.1
  • 23
    • 0002183889 scopus 로고
    • Mutants at xantha and albina loci in relation to chloroplast biogenesis in barley (Hordeum vulgare L.)
    • Henningsen, K.W., Boynton, J.E., and von Wettstein, D. (1993). Mutants at xantha and albina loci in relation to chloroplast biogenesis in barley (Hordeum vulgare L.). R. Dan. Acad. Sci. Lett. Biol. Skrifter 42, 1-349.
    • (1993) R. Dan. Acad. Sci. Lett. Biol. Skrifter , vol.42 , pp. 1-349
    • Henningsen, K.W.1    Boynton, J.E.2    Von Wettstein, D.3
  • 24
    • 0028961554 scopus 로고
    • Two routes of chlorophyllide synthesis that are differentially regulated by light in barley
    • Holtorf, H., Reinbothe, S., Reinbothe, C., Bereza, B., and Apel, K. (1995). Two routes of chlorophyllide synthesis that are differentially regulated by light in barley. Proc. Natl. Acad. Sci. USA 92, 3254-3258.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 3254-3258
    • Holtorf, H.1    Reinbothe, S.2    Reinbothe, C.3    Bereza, B.4    Apel, K.5
  • 25
    • 5844333607 scopus 로고
    • Changes in the polypeptide composition of internal membranes of barley plastids during greening
    • Høyer-Hansen, G., and Simpson, D.J. (1977). Changes in the polypeptide composition of internal membranes of barley plastids during greening. Carlsberg Res. Commun. 42, 379-389.
    • (1977) Carlsberg Res. Commun. , vol.42 , pp. 379-389
    • Høyer-Hansen, G.1    Simpson, D.J.2
  • 26
    • 77957180294 scopus 로고
    • Separation and characterization of prolamellar bodies and prothylakoids from squash etioplasts
    • Ikeuchi, M., and Murakami, S. (1983). Separation and characterization of prolamellar bodies and prothylakoids from squash etioplasts. Plant Cell Physiol. 24, 71-80.
    • (1983) Plant Cell Physiol. , vol.24 , pp. 71-80
    • Ikeuchi, M.1    Murakami, S.2
  • 27
    • 0006260961 scopus 로고
    • Developmental physiology of bean leaf plastids. III. Tube transformation and protochlorophyll(ide) photoconversion by a flash irradiation
    • Kahn, A. (1968). Developmental physiology of bean leaf plastids. III. Tube transformation and protochlorophyll(ide) photoconversion by a flash irradiation. Plant Physiol. 43, 1781-1785.
    • (1968) Plant Physiol. , vol.43 , pp. 1781-1785
    • Kahn, A.1
  • 28
    • 0000668045 scopus 로고
    • Light-induced breakdown of NADPH:protochlorophyllide oxidoreductase in vitro
    • Kay, S.A., and Griffiths, W.T. (1983). Light-induced breakdown of NADPH:protochlorophyllide oxidoreductase in vitro. Plant Physiol. 72, 229-236.
    • (1983) Plant Physiol. , vol.72 , pp. 229-236
    • Kay, S.A.1    Griffiths, W.T.2
  • 29
    • 0028388549 scopus 로고
    • Chlorophyll regulates accumulation of the plastid-encoded chlorophyll proteins P700 and D1 by increasing apoprotein stability
    • Kim, J., Eichacker, L., Rüdiger, W., and Mullet, J.E. (1994). Chlorophyll regulates accumulation of the plastid-encoded chlorophyll proteins P700 and D1 by increasing apoprotein stability. Plant Physiol. 104, 907-916.
    • (1994) Plant Physiol. , vol.104 , pp. 907-916
    • Kim, J.1    Eichacker, L.2    Rüdiger, W.3    Mullet, J.E.4
  • 31
    • 0029198416 scopus 로고
    • Chlorophyll synthesis in a deetiolated (det340) mutant of Arabidopsis without NADPH-protochlorophyllide (PChlide) oxidoreductase (POR) A and photoactive PChlide-F655
    • Lebedev, N., van Cleve, B., Armstrong, G., and Apel, K. (1995). Chlorophyll synthesis in a deetiolated (det340) mutant of Arabidopsis without NADPH-protochlorophyllide (PChlide) oxidoreductase (POR) A and photoactive PChlide-F655. Plant Cell 7, 2081-2090.
    • (1995) Plant Cell , vol.7 , pp. 2081-2090
    • Lebedev, N.1    Van Cleve, B.2    Armstrong, G.3    Apel, K.4
  • 32
    • 0019041296 scopus 로고
    • Light modulation of the activity of the protochlorophyllide oxidoreductase
    • Mapleston, E.R., and Griffiths, W.T. (1980). Light modulation of the activity of the protochlorophyllide oxidoreductase. Biochem. J. 189, 125-133.
    • (1980) Biochem. J. , vol.189 , pp. 125-133
    • Mapleston, E.R.1    Griffiths, W.T.2
  • 33
    • 0022425589 scopus 로고
    • Phytochrome control of in vitro transcription of specific genes in isolated nuclei from barley (Hordeum vulgare)
    • Mösinger, E., Batschauer, A., Schäfer, E., and Apel, K. (1985). Phytochrome control of in vitro transcription of specific genes in isolated nuclei from barley (Hordeum vulgare). Eur. J. Biochem. 147, 137-142.
    • (1985) Eur. J. Biochem. , vol.147 , pp. 137-142
    • Mösinger, E.1    Batschauer, A.2    Schäfer, E.3    Apel, K.4
  • 35
    • 0015952532 scopus 로고
    • Photoconversion and regeneration of active protochlorophyll(ide) in mutants defective in the regulation of chlorophyll synthesis
    • Nielsen, O.F. (1974). Photoconversion and regeneration of active protochlorophyll(ide) in mutants defective in the regulation of chlorophyll synthesis. Arch. Biochem. Biophys. 160, 430-439.
    • (1974) Arch. Biochem. Biophys. , vol.160 , pp. 430-439
    • Nielsen, O.F.1
  • 36
    • 0006933849 scopus 로고
    • Macromolecular physiology of plastids. XIII. The effect of photoinactive protochlorophyllide on the function of protochlorophyllide holochrome
    • Nielsen, O.F. (1975). Macromolecular physiology of plastids. XIII. The effect of photoinactive protochlorophyllide on the function of protochlorophyllide holochrome. Biochem. Physiol. Pflanz. 167, 195-206.
    • (1975) Biochem. Physiol. Pflanz. , vol.167 , pp. 195-206
    • Nielsen, O.F.1
  • 38
    • 0001633977 scopus 로고
    • Pigment-protein complexes of illuminated etiolated leaves
    • Oliver, R.P., and Griffiths, W.T. (1982). Pigment-protein complexes of illuminated etiolated leaves. Plant Physiol. 70, 1019-1025.
    • (1982) Plant Physiol. , vol.70 , pp. 1019-1025
    • Oliver, R.P.1    Griffiths, W.T.2
  • 39
    • 0023033271 scopus 로고
    • Fluorescence properties of the envelope membranes from spinach chloroplasts
    • Pineau, B., Dubertret, G., Joyard, J., and Douce, R. (1986). Fluorescence properties of the envelope membranes from spinach chloroplasts. J. Biol. Chem. 261, 9210-9215.
    • (1986) J. Biol. Chem. , vol.261 , pp. 9210-9215
    • Pineau, B.1    Dubertret, G.2    Joyard, J.3    Douce, R.4
  • 40
    • 0000069321 scopus 로고
    • Identification of the main species of tetrapyrrolic pigments in envelope membranes from spinach chloroplasts
    • Pineau, B., Gerard-Hirne, C., Douce, R., and Joyard, J. (1993). Identification of the main species of tetrapyrrolic pigments in envelope membranes from spinach chloroplasts. Plant Physiol. 102, 821-828.
    • (1993) Plant Physiol. , vol.102 , pp. 821-828
    • Pineau, B.1    Gerard-Hirne, C.2    Douce, R.3    Joyard, J.4
  • 41
    • 0028784796 scopus 로고
    • A light-induced protease from barley plastids degrades NADPH:protochlorophyllide oxidoreductase complexed with chlorophyllide
    • Reinbothe, C., Apel, K., and Reinbothe, S. (1995). A light-induced protease from barley plastids degrades NADPH:protochlorophyllide oxidoreductase complexed with chlorophyllide. Mol. Cell. Biol. 15, 6206-6212.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6206-6212
    • Reinbothe, C.1    Apel, K.2    Reinbothe, S.3
  • 42
    • 0029240288 scopus 로고
    • Substrate-dependent transport of the NADPH:protochlorophyllide oxidoreductase into isolated plastids
    • Reinbothe, S., Runge, S., Reinbothe, C., van Cleve, B., and Apel, K. (1995a). Substrate-dependent transport of the NADPH:protochlorophyllide oxidoreductase into isolated plastids. Plant Cell 7, 161-172.
    • (1995) Plant Cell , vol.7 , pp. 161-172
    • Reinbothe, S.1    Runge, S.2    Reinbothe, C.3    Van Cleve, B.4    Apel, K.5
  • 43
    • 0028907432 scopus 로고
    • Enzymatic product formation impairs both the chloroplast receptor binding function as well as translocation competence of the NADPH:protochlorophyllide oxidoreductase, a nuclear-encoded plastid protein
    • Reinbothe, S., Reinbothe, C., Runge, S., and Apel, K. (1995b) Enzymatic product formation impairs both the chloroplast receptor binding function as well as translocation competence of the NADPH:protochlorophyllide oxidoreductase, a nuclear-encoded plastid protein. J. Cell Biol. 129, 299-308.
    • (1995) J. Cell Biol. , vol.129 , pp. 299-308
    • Reinbothe, S.1    Reinbothe, C.2    Runge, S.3    Apel, K.4
  • 44
    • 0029201048 scopus 로고
    • Two NADPH:protochlorophyllide oxidoreductases in barley: Evidence for the selective disappearance of PORA during the light-induced greening of etiolated seedlings
    • Reinbothe, S., Reinbothe, C., Holtorf, H., and Apel, K. (1995c) Two NADPH:protochlorophyllide oxidoreductases in barley: Evidence for the selective disappearance of PORA during the light-induced greening of etiolated seedlings. Plant Cell 7, 1933-1940.
    • (1995) Plant Cell , vol.7 , pp. 1933-1940
    • Reinbothe, S.1    Reinbothe, C.2    Holtorf, H.3    Apel, K.4
  • 45
    • 0002119280 scopus 로고
    • Structural and functional significance of pigment-protein complexes of chlorophyll precursors
    • H. Scheer, ed (Boca Raton, FL: CRC Press)
    • Ryberg, M., and Sundqvist, C. (1991). Structural and functional significance of pigment-protein complexes of chlorophyll precursors. In Chlorophylls, H. Scheer, ed (Boca Raton, FL: CRC Press), pp. 587-612.
    • (1991) Chlorophylls , pp. 587-612
    • Ryberg, M.1    Sundqvist, C.2
  • 46
    • 0019638822 scopus 로고
    • The protochlorophyllide holochrome of barley. The effect of light on the NADPH-protochlorophyllide oxidoreductase
    • Santel, H.J., and Apel, K. (1981). The protochlorophyllide holochrome of barley. The effect of light on the NADPH-protochlorophyllide oxidoreductase. Eur. J. Biochem. 120, 95-103.
    • (1981) Eur. J. Biochem. , vol.120 , pp. 95-103
    • Santel, H.J.1    Apel, K.2
  • 47
    • 0028912995 scopus 로고
    • Photoreduction of protopheophorbide with NADPH-protochlorophyllide oxidoreductase from etiolated wheat (Triticum aestivum)
    • Schoch, S., Helfrich, M., Wiktorsson, B., Sundqvist, C., Rüdiger, W., and Ryberg, M. (1995). Photoreduction of protopheophorbide with NADPH-protochlorophyllide oxidoreductase from etiolated wheat (Triticum aestivum). 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
  • 48
    • 0001687615 scopus 로고
    • Protochlorophyllide reductase: A key enzyme in the greening process
    • M. Ryberg and C. Sundqvist, eds (New York: Academic Press)
    • Schulz, R., and Senger, H. (1993). Protochlorophyllide reductase: A key enzyme in the greening process. In Pigment-Protein Complexes in Plastids: Synthesis and Assembly, M. Ryberg and C. Sundqvist, eds (New York: Academic Press), pp. 179-218.
    • (1993) Pigment-Protein Complexes in Plastids: Synthesis and Assembly , pp. 179-218
    • Schulz, R.1    Senger, H.2
  • 49
    • 0024676061 scopus 로고
    • Nucleotide sequence of a cDNA coding for the NADPH-protochlorophyllide oxidoreductase (PCR) of barley (Hordeum vulgare L.) and expression in Escherichia coli
    • Schulz, R., Steinmüller, K., Klaas, M., Forreiter, C., Rasmussen, S., Hiller, C., and Apel, K. (1989). Nucleotide sequence of a cDNA coding for the NADPH-protochlorophyllide oxidoreductase (PCR) of barley (Hordeum vulgare L.) and expression in Escherichia coli. Mol. Gen. Genet. 217, 355-361.
    • (1989) Mol. Gen. Genet. , vol.217 , pp. 355-361
    • Schulz, R.1    Steinmüller, K.2    Klaas, M.3    Forreiter, C.4    Rasmussen, S.5    Hiller, C.6    Apel, K.7
  • 50
    • 77957246491 scopus 로고
    • Spectroscopic studies on chlorophyll formation in intact leaves
    • Shibata, A. (1957). Spectroscopic studies on chlorophyll formation in intact leaves. J. Biochem. 44, 147-173.
    • (1957) J. Biochem. , vol.44 , pp. 147-173
    • Shibata, A.1
  • 51
    • 0026824270 scopus 로고
    • Molecular cloning, nuclear gene structure, and developmental expression of NADPH-protochlorophyllide oxidoreductase in pea (Pisum sativum L.)
    • Spano, A.J., He, Z., Michel, H., Hunt, D.F., and Timko, M.P. (1992a). Molecular cloning, nuclear gene structure, and developmental expression of NADPH-protochlorophyllide oxidoreductase in pea (Pisum sativum L.). Plant Mol. Biol. 18, 967-972.
    • (1992) Plant Mol. Biol. , vol.18 , pp. 967-972
    • Spano, A.J.1    He, Z.2    Michel, H.3    Hunt, D.F.4    Timko, M.P.5
  • 52
    • 0026679884 scopus 로고
    • NADPH:protochlorophyllide oxidoreductases in white pine (Pinus strobus) and loblolly pine (P. taeda). Evidence for light and developmental regulation of expression and conservation in gene organization and protein structure between angiosperms and gymnosperms
    • Spano, A.J., He, Z., and Timko, M.P. (1992b). NADPH:protochlorophyllide oxidoreductases in white pine (Pinus strobus) and loblolly pine (P. taeda). Evidence for light and developmental regulation of expression and conservation in gene organization and protein structure between angiosperms and gymnosperms. Mol. Gen. Genet. 236, 86-95.
    • (1992) Mol. Gen. Genet. , vol.236 , pp. 86-95
    • Spano, A.J.1    He, Z.2    Timko, M.P.3
  • 53
    • 84981566338 scopus 로고
    • The pool size of protochlorophyllide during different stages of greening of dark-grown wheat leaves
    • Sundqvist, C. (1974). The pool size of protochlorophyllide during different stages of greening of dark-grown wheat leaves. Physiol. Plant. 30, 143-147.
    • (1974) Physiol. Plant. , vol.30 , pp. 143-147
    • Sundqvist, C.1
  • 54
    • 0029065496 scopus 로고
    • A prokaryotic origin for light-dependent chlorophyll biosynthesis of plants
    • Suzuki, J.Y., and Bauer, C.E. (1995). A prokaryotic origin for light-dependent chlorophyll biosynthesis of plants. Proc. Natl. Acad. Sci. USA 92, 3749-3753.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 3749-3753
    • Suzuki, J.Y.1    Bauer, C.E.2
  • 55
    • 0027360306 scopus 로고
    • Cloning, characterization and import studies on protochlorophyllide reductase from wheat (Triticum aestivum)
    • Teakle, J.R., and Griffiths, W.T. (1993). Cloning, characterization and import studies on protochlorophyllide reductase from wheat (Triticum aestivum). Biochem. J. 296, 225-230.
    • (1993) Biochem. J. , vol.296 , pp. 225-230
    • Teakle, J.R.1    Griffiths, W.T.2
  • 56
    • 0000492532 scopus 로고
    • Physiological and molecular studies of light-regulated nuclear genes in higher plants
    • Thompson, W.F., and White, M.J. (1991). Physiological and molecular studies of light-regulated nuclear genes in higher plants. Annu. Rev. Plant Physiol. Plant Mol. Biol. 42, 423-466.
    • (1991) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.42 , pp. 423-466
    • Thompson, W.F.1    White, M.J.2
  • 57
    • 0015220496 scopus 로고
    • The greening of etiolated bean leaves. I. The initial photoconversion process
    • Thorne, S. (1971). The greening of etiolated bean leaves. I. The initial photoconversion process. Biochim. Biophys. Acta 226, 113-127.
    • (1971) Biochim. Biophys. Acta , vol.226 , pp. 113-127
    • Thorne, S.1
  • 58
    • 51249172694 scopus 로고
    • Plastid gene regulation during development: An intriguing complexity of mechanisms
    • van Grinsven, M.Q.J.M., and Kool, A.J. (1988). Plastid gene regulation during development: An intriguing complexity of mechanisms. Plant Mol. Biol. Rep. 6, 213-239.
    • (1988) Plant Mol. Biol. Rep. , vol.6 , pp. 213-239
    • Van Grinsven, M.Q.J.M.1    Kool, A.J.2
  • 59
    • 0002304892 scopus 로고
    • The physiology of chlorophyll formation in relation to structural changes in chloroplasts
    • Virgin, H.I., Kahn, A., and von Wettstein, D. (1963). The physiology of chlorophyll formation in relation to structural changes in chloroplasts. Photochem. Photobiol. 2, 83-91.
    • (1963) Photochem. Photobiol. , vol.2 , pp. 83-91
    • Virgin, H.I.1    Kahn, A.2    Von Wettstein, D.3
  • 62
    • 0027022309 scopus 로고
    • COP9: A new genetic locus involved in light-regulated development and gene expression in Arabidopsis
    • Wei, N., and Deng, X.-W. (1992). COP9: A new genetic locus involved in light-regulated development and gene expression in Arabidopsis. Plant Cell 4, 1507-1518.
    • (1992) Plant Cell , vol.4 , pp. 1507-1518
    • Wei, N.1    Deng, X.-W.2
  • 63
    • 0028895568 scopus 로고
    • A light-dependent complementation system for analysis of NADPH:protochlorophyllide oxidoreductase: Identification and mutagenesis of two conserved residues that are essential for enzyme activity
    • Wilks, H.M., and Timko, M.P. (1995). A light-dependent complementation system for analysis of NADPH:protochlorophyllide oxidoreductase: Identification and mutagenesis of two conserved residues that are essential for enzyme activity. Proc. Natl. Acad. Sci. USA 92, 724-728.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 724-728
    • Wilks, H.M.1    Timko, M.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.