메뉴 건너뛰기




Volumn 33, Issue 3-4, 1997, Pages 331-345

The Calvin cycle - A historical perspective

Author keywords

C4 plants; CAM plants; Enzyme regulation; Glycolate pathway; Molecular cloning; Photosynthetically active radiation; Phylogeny; Ribulose 1,5 bisphosphate carboxylase oxygenase

Indexed keywords


EID: 0013310022     PISSN: 03003604     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (6)

References (111)
  • 1
    • 0000249948 scopus 로고
    • Chloroplast and cytoplasmic enzymes. Three distinct isoenzymes associated with the reductive pentose phosphate cycle
    • Anderson, L.E., Advani, V.R.: Chloroplast and cytoplasmic enzymes. Three distinct isoenzymes associated with the reductive pentose phosphate cycle. - Plant Physiol. 45: 583-585, 1970.
    • (1970) Plant Physiol. , vol.45 , pp. 583-585
    • Anderson, L.E.1    Advani, V.R.2
  • 2
    • 0001182939 scopus 로고
    • Light modulation of enzyme activity in chloroplasts. Generation of membrane-bound vincinal-dithiol groups by photosynthetic electron transport
    • Anderson, L.E., Avron, M.: Light modulation of enzyme activity in chloroplasts. Generation of membrane-bound vincinal-dithiol groups by photosynthetic electron transport. - Plant Physiol. 57: 209-213, 1976.
    • (1976) Plant Physiol. , vol.57 , pp. 209-213
    • Anderson, L.E.1    Avron, M.2
  • 3
    • 0015911742 scopus 로고
    • Ribulose diphosphate oxygenase. I. Synthesis of phosphoglycolate by fraction-1 protein of leaves
    • Andrews, T.J., Lorimer, G.H., Tolbert, N.E.: Ribulose diphosphate oxygenase. I. Synthesis of phosphoglycolate by fraction-1 protein of leaves. - Biochemistry 12: 11-18, 1973.
    • (1973) Biochemistry , vol.12 , pp. 11-18
    • Andrews, T.J.1    Lorimer, G.H.2    Tolbert, N.E.3
  • 4
    • 0001357053 scopus 로고
    • Photosynthesis by isolated chloroplasts
    • Arnon, D.I., Allen, M.B., Whatley, F.R.: Photosynthesis by isolated chloroplasts. - Nature 174: 394-396, 1954.
    • (1954) Nature , vol.174 , pp. 394-396
    • Arnon, D.I.1    Allen, M.B.2    Whatley, F.R.3
  • 5
    • 0005462288 scopus 로고
    • Triphosphopyridine nucleotide as a catalyst in photosynthetic phosphorylation
    • Amon, D.I., Whatley, F.R., Allen, M.B.: Triphosphopyridine nucleotide as a catalyst in photosynthetic phosphorylation. - Nature 180: 182-186, 1957.
    • (1957) Nature , vol.180 , pp. 182-186
    • Amon, D.I.1    Whatley, F.R.2    Allen, M.B.3
  • 6
    • 84980084918 scopus 로고
    • Über die Wasserentziehung und ihre Bedeutung für das Pflanzenleben und die Gärung
    • Baeyer, A.: Über die Wasserentziehung und ihre Bedeutung für das Pflanzenleben und die Gärung. - Ber. chem. Ges. 3: 63-75, 1870.
    • (1870) Ber. Chem. Ges. , vol.3 , pp. 63-75
    • Baeyer, A.1
  • 8
    • 0016680803 scopus 로고
    • Properties and regulation of C-1-fructose-1,6-diphosphatase from spinach chloroplasts
    • Baier, D., Latzko, E.: Properties and regulation of C-1-fructose-1,6-diphosphatase from spinach chloroplasts. - Biochim. biophys. Acta 396: 141-147, 1975.
    • (1975) Biochim. Biophys. Acta , vol.396 , pp. 141-147
    • Baier, D.1    Latzko, E.2
  • 10
    • 0019182515 scopus 로고
    • Molecular cloning and sequencing of cDNA encoding the precursor of small subunit of chloroplast ribulose-1,5-bisphosphate carboxylase
    • Bedbrook, J., Smith, S.M., Ellis, R.J.: Molecular cloning and sequencing of cDNA encoding the precursor of small subunit of chloroplast ribulose-1,5-bisphosphate carboxylase. - Nature 287: 692-697, 1980.
    • (1980) Nature , vol.287 , pp. 692-697
    • Bedbrook, J.1    Smith, S.M.2    Ellis, R.J.3
  • 11
    • 0000417407 scopus 로고
    • Isolation, identification and synthesis of 2-carboxyarabinitol 1-phosphate, a diurnal regulator of ribulose-bisphosphate carboxylase activity
    • Berry, J.A., Lorimer, G.H., Pierce, J., Seemann, J.R., Meek, J., Freas, S.: Isolation, identification and synthesis of 2-carboxyarabinitol 1-phosphate, a diurnal regulator of ribulose-bisphosphate carboxylase activity. - Proc. nat. Acad. Sci. USA 84: 734-738, 1987.
    • (1987) Proc. Nat. Acad. Sci. USA , vol.84 , pp. 734-738
    • Berry, J.A.1    Lorimer, G.H.2    Pierce, J.3    Seemann, J.R.4    Meek, J.5    Freas, S.6
  • 14
    • 0015212072 scopus 로고
    • Phosphoglycolate production catalyzed by ribulose diphosphate carboxylase
    • Bowes, G., Ogren, W.L., Hageman, R.H.: Phosphoglycolate production catalyzed by ribulose diphosphate carboxylase. - Biochem. biophys. Res. Commun. 45: 716-722, 1971.
    • (1971) Biochem. Biophys. Res. Commun. , vol.45 , pp. 716-722
    • Bowes, G.1    Ogren, W.L.2    Hageman, R.H.3
  • 16
    • 0030037573 scopus 로고    scopus 로고
    • Higher plant chloroplast and cytosolic 3-phosphoglycerate kinases: A case of endosymbiotic gene replacement
    • Brinkmann, H., Martin, W.: Higher plant chloroplast and cytosolic 3-phosphoglycerate kinases: A case of endosymbiotic gene replacement. - Plant mol. Biol. 30: 65-75, 1996.
    • (1996) Plant Mol. Biol. , vol.30 , pp. 65-75
    • Brinkmann, H.1    Martin, W.2
  • 17
    • 0000765807 scopus 로고
    • Role of light in the regulation of chloroplast enzymes
    • Buchanan, B.B.: Role of light in the regulation of chloroplast enzymes. - Annu. Rev. Plant Physiol. 31: 341-374, 1980.
    • (1980) Annu. Rev. Plant Physiol. , vol.31 , pp. 341-374
    • Buchanan, B.B.1
  • 18
    • 0015218774 scopus 로고
    • Ferredoxin-activated fructose diphosphatase of spinach chloroplasts. Resolution of the system, properties of the alkaline fructose diphosphatase component, and physiological significance of the ferredoxin-linked activation
    • Buchanan, B.B., Schumann, P., Kalberer, P.P.: Ferredoxin-activated fructose diphosphatase of spinach chloroplasts. Resolution of the system, properties of the alkaline fructose diphosphatase component, and physiological significance of the ferredoxin-linked activation. - J. biol. Chem. 246: 5952-5929, 1971.
    • (1971) J. Biol. Chem. , vol.246 , pp. 5952-15929
    • Buchanan, B.B.1    Schumann, P.2    Kalberer, P.P.3
  • 19
    • 0002340038 scopus 로고
    • The photosynthetic carbon cycle
    • Calvin, M.: The photosynthetic carbon cycle. - J. chem. Soc. 78: 1895-1915, 1956.
    • (1956) J. Chem. Soc. , vol.78 , pp. 1895-1915
    • Calvin, M.1
  • 20
    • 0015506187 scopus 로고
    • Chloroplast DNA codes for the primary structure of the large subunit of Fraction I protein
    • Chan, P.-H., Wildman, S.G.: Chloroplast DNA codes for the primary structure of the large subunit of Fraction I protein. - Biochim. biophys. Acta 277: 677-680, 1972.
    • (1972) Biochim. Biophys. Acta , vol.277 , pp. 677-680
    • Chan, P.-H.1    Wildman, S.G.2
  • 22
    • 27544486404 scopus 로고
    • Proteins of green leaves. VIII. The distribution of fraction I protein in the plant kingdom as detected by precipitin and ultracentrifugal analyses
    • Dorner, R.W., Kahn, A., Wildman, S.G.: Proteins of green leaves. VIII. The distribution of fraction I protein in the plant kingdom as detected by precipitin and ultracentrifugal analyses. - Biochim. biophys. Acta 29: 240-245, 1958.
    • (1958) Biochim. Biophys. Acta , vol.29 , pp. 240-245
    • Dorner, R.W.1    Kahn, A.2    Wildman, S.G.3
  • 23
    • 0028928609 scopus 로고
    • Redox equilibria between the regulatory thiols of light/dark-modulated chloroplast enzymes and dithiothreitol: Fine-tuning by metabolites
    • Faske, M., Holtgrefe, S., Ocheretina, O., Meister, M., Backhausen, J.E., Scheibe, R.: Redox equilibria between the regulatory thiols of light/dark-modulated chloroplast enzymes and dithiothreitol: fine-tuning by metabolites. - Biochim. biophys. Acta 1247: 135-142, 1995.
    • (1995) Biochim. Biophys. Acta , vol.1247 , pp. 135-142
    • Faske, M.1    Holtgrefe, S.2    Ocheretina, O.3    Meister, M.4    Backhausen, J.E.5    Scheibe, R.6
  • 24
    • 0030294746 scopus 로고    scopus 로고
    • Molecular characterization of transketolase (EC 2.2.1.1) active in the Calvin cycle of spinach chloroplasts
    • Flechner, A., Dreßen, U., Westhoff, P., Henze, K., Schnarrenberger, C., Martin, W.: Molecular characterization of transketolase (EC 2.2.1.1) active in the Calvin cycle of spinach chloroplasts. - Plant mol. Biol. 32: 475-484, 1996.
    • (1996) Plant Mol. Biol. , vol.32 , pp. 475-484
    • Flechner, A.1    Dreßen, U.2    Westhoff, P.3    Henze, K.4    Schnarrenberger, C.5    Martin, W.6
  • 25
    • 0024820705 scopus 로고
    • Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg-ATP
    • Goloubinoff, P., Christeller, J.T., Gatenby, A.A., Lorimer, G.H.: Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg-ATP. - Nature 342: 884-889, 1989.
    • (1989) Nature , vol.342 , pp. 884-889
    • Goloubinoff, P.1    Christeller, J.T.2    Gatenby, A.A.3    Lorimer, G.H.4
  • 26
    • 0027951015 scopus 로고
    • Two distinct aldolases of class II type in the cyanoplasts and in the cytosol of the alga Cyanophora paradoxa
    • Gross, W., Bayer, M.G., Schnarrenberger, C., Gebhart, U.B., Maier, T.L., Schenk, H.E.A.: Two distinct aldolases of class II type in the cyanoplasts and in the cytosol of the alga Cyanophora paradoxa. - Plant Physiol. 105: 1393-1398, 1994.
    • (1994) Plant Physiol. , vol.105 , pp. 1393-1398
    • Gross, W.1    Bayer, M.G.2    Schnarrenberger, C.3    Gebhart, U.B.4    Maier, T.L.5    Schenk, H.E.A.6
  • 28
    • 0006396908 scopus 로고
    • Vergleichende Anatomie des assimilatorischen Gewebesystems der Pflanzen
    • Haberlandt, G.: Vergleichende Anatomie des assimilatorischen Gewebesystems der Pflanzen. - Jahrb. wiss. Bot. 13: 74-188, 1881.
    • (1881) Jahrb. Wiss. Bot. , vol.13 , pp. 74-188
    • Haberlandt, G.1
  • 29
    • 0013954204 scopus 로고
    • Photosynthesis by sugar-cane leaves. A new carboxylation reaction and the pathway of sugar formation
    • Hatch, M.D., Slack, C.R.: Photosynthesis by sugar-cane leaves. A new carboxylation reaction and the pathway of sugar formation. - Biochem. J. 101: 103-111, 1966.
    • (1966) Biochem. J. , vol.101 , pp. 103-111
    • Hatch, M.D.1    Slack, C.R.2
  • 30
    • 84941394843 scopus 로고
    • Untersuchungen zur intrazellulären Verteilung von Enzymen und Substraten in der Blattzelle. II. Localisation von Enzymen des reduktiven und dem oxidativen Pentosephosphat-Zyklus in den Chloroplasten und Permeabilität der Chloroplasten-Membran gegenüber Metaboliten
    • Heber, U., Hallier, U.W., Hudson, M.A.: Untersuchungen zur intrazellulären Verteilung von Enzymen und Substraten in der Blattzelle. II. Localisation von Enzymen des reduktiven und dem oxidativen Pentosephosphat-Zyklus in den Chloroplasten und Permeabilität der Chloroplasten-Membran gegenüber Metaboliten. - Z. Naturforsch. 22b: 1200-1215, 1967.
    • (1967) Z. Naturforsch. , vol.22 B , pp. 1200-1215
    • Heber, U.1    Hallier, U.W.2    Hudson, M.A.3
  • 31
    • 0000301399 scopus 로고
    • Localization of carboxydismutase and triosephosphate dehydrogenases in chloroplasts
    • Heber, U., Pon, N.G., Heber, M.: Localization of carboxydismutase and triosephosphate dehydrogenases in chloroplasts. - Plant Physiol. 38: 355-360, 1963.
    • (1963) Plant Physiol. , vol.38 , pp. 355-360
    • Heber, U.1    Pon, N.G.2    Heber, M.3
  • 32
    • 0029047354 scopus 로고
    • A nuclear gene of eubacterial origin in Euglena gracilis reflects cryptic endosymbiosis during protist evolution
    • Henze, K., Badr, A., Wettern, M., Cerff, R., Martin, W.: A nuclear gene of eubacterial origin in Euglena gracilis reflects cryptic endosymbiosis during protist evolution. - Proc. nat. Acad. Sci. USA 92: 9122-9126, 1995.
    • (1995) Proc. Nat. Acad. Sci. USA , vol.92 , pp. 9122-9126
    • Henze, K.1    Badr, A.2    Wettern, M.3    Cerff, R.4    Martin, W.5
  • 33
    • 0028675654 scopus 로고
    • Chloroplast and cytosolic triosephosphate isomerases from spinach: Purification, microsequencing and cDNA cloning of the chloroplast enzyme
    • Henze, K., Schnarrenberger, C., Kellermann, J., Martin, W.: Chloroplast and cytosolic triosephosphate isomerases from spinach: Purification, microsequencing and cDNA cloning of the chloroplast enzyme. - Plant mol. Biol. 26: 1961-1973, 1994.
    • (1994) Plant Mol. Biol. , vol.26 , pp. 1961-1973
    • Henze, K.1    Schnarrenberger, C.2    Kellermann, J.3    Martin, W.4
  • 34
    • 0012428534 scopus 로고
    • Oxygen produced by isolated chloroplasts
    • Hill, R.: Oxygen produced by isolated chloroplasts. - Proc. roy. Soc. B 127: 192-210, 1939.
    • (1939) Proc. Roy. Soc. B , vol.127 , pp. 192-210
    • Hill, R.1
  • 36
  • 37
    • 0015520411 scopus 로고
    • Studies on fraction I protein. IV. Mode of inhereditance of primary structure in relation to whether chloroplast or nuclear DNA contains the code for a chloroplast protein
    • Kawashima, N., Wildman, N.G.: Studies on fraction I protein. IV. Mode of inhereditance of primary structure in relation to whether chloroplast or nuclear DNA contains the code for a chloroplast protein. - Biochim. biophys. Acta 262: 42-49, 1972.
    • (1972) Biochim. Biophys. Acta , vol.262 , pp. 42-49
    • Kawashima, N.1    Wildman, N.G.2
  • 38
    • 0007658874 scopus 로고
    • Chloroplast phosphofructokinase. I. Proof of phosphofructokinase activity in chloroplasts
    • Kelly, G. J., Latzko, E.: Chloroplast phosphofructokinase. I. Proof of phosphofructokinase activity in chloroplasts. - Plant Physiol. 60: 290-294, 1977.
    • (1977) Plant Physiol. , vol.60 , pp. 290-294
    • Kelly, G.J.1    Latzko, E.2
  • 39
    • 0025160560 scopus 로고
    • Crystallographic analysis of ribulose 1,5-bisphosphate carboxylase of spinach at 2.4 Å resolution. Subunit interactions and active site
    • Knight, S., Andersson, I., Brändén, C.-I.: Crystallographic analysis of ribulose 1,5-bisphosphate carboxylase of spinach at 2.4 Å resolution. Subunit interactions and active site. - J. mol. Biol. 215: 113-160, 1990.
    • (1990) J. Mol. Biol. , vol.215 , pp. 113-160
    • Knight, S.1    Andersson, I.2    Brändén, C.-I.3
  • 40
    • 0001272527 scopus 로고
    • Carbon dioxide fixation in sugar cane leaves
    • Kortschak, H.P., Hartt, C.E., Burr, G.O.: Carbon dioxide fixation in sugar cane leaves. - Plant Physiol. 40: 209-213, 1965.
    • (1965) Plant Physiol. , vol.40 , pp. 209-213
    • Kortschak, H.P.1    Hartt, C.E.2    Burr, G.O.3
  • 41
    • 0014917942 scopus 로고
    • Effect of photosynthesis, photosynthetic inhibitors and oxygen on the activity of ribulose 5-phosphate kinase
    • Latzko, E., Garnier, R.v., Gibbs, M.: Effect of photosynthesis, photosynthetic inhibitors and oxygen on the activity of ribulose 5-phosphate kinase. - Biochem. biophys. Res. Commun. 39: 1140-1144, 1970.
    • (1970) Biochem. Biophys. Res. Commun. , vol.39 , pp. 1140-1144
    • Latzko, E.1    Garnier, R.V.2    Gibbs, M.3
  • 42
    • 0016152220 scopus 로고
    • Evidence for a hexosediphosphatase from the cytoplasm of spinach leaves
    • Latzko, E., Zimmermann, G., Feller, U.: Evidence for a hexosediphosphatase from the cytoplasm of spinach leaves. - Hoppe-Seyler's Z. physiol. Chem. 355: 321-326, 1974.
    • (1974) Hoppe-Seyler's Z. Physiol. Chem. , vol.355 , pp. 321-326
    • Latzko, E.1    Zimmermann, G.2    Feller, U.3
  • 43
    • 0024978453 scopus 로고
    • Wheat phosphoglycerate kinase: Evidence for recombination between genes for the chloroplastic and cytosolic enzymes
    • Longstaff, M., Raines, C.A., McMorrow, E.M., Bradbeer, J.W., Dyer, T.A.: Wheat phosphoglycerate kinase: Evidence for recombination between genes for the chloroplastic and cytosolic enzymes. - Nucl. Acids Res. 17: 6569-6580, 1989.
    • (1989) Nucl. Acids Res. , vol.17 , pp. 6569-6580
    • Longstaff, M.1    Raines, C.A.2    McMorrow, E.M.3    Bradbeer, J.W.4    Dyer, T.A.5
  • 44
    • 0015911743 scopus 로고
    • Ribulose diphosphate oxygenase. II. Further proof for reaction products and mechanism of action
    • Lorimer, G.H., Andrews, T.J., Tolbert, N.B.: Ribulose diphosphate oxygenase. II. Further proof for reaction products and mechanism of action. - Biochemistry 12: 19-23, 1973.
    • (1973) Biochemistry , vol.12 , pp. 19-23
    • Lorimer, G.H.1    Andrews, T.J.2    Tolbert, N.B.3
  • 45
    • 0017253134 scopus 로고
    • The activation of ribulose-1,5-bisphosphate carboxylase by carbon dioxide and magnesium ions. Equilibria, kinetics, a suggested mechanism, and physiological implications
    • Lorimer, G.H., Badger, M.R., Andrews, T.J.: The activation of ribulose-1,5-bisphosphate carboxylase by carbon dioxide and magnesium ions. Equilibria, kinetics, a suggested mechanism, and physiological implications. - Biochemistry 15: 529-536, 1976.
    • (1976) Biochemistry , vol.15 , pp. 529-536
    • Lorimer, G.H.1    Badger, M.R.2    Andrews, T.J.3
  • 46
    • 27544512021 scopus 로고
    • Proteins from pasture plants. Cytoplasmic proteins of white clover and Italian ryegrass
    • Lyttleton, J.W.: Proteins from pasture plants. Cytoplasmic proteins of white clover and Italian ryegrass. - Biochem. J. 64: 70-80, 1956.
    • (1956) Biochem. J. , vol.64 , pp. 70-80
    • Lyttleton, J.W.1
  • 47
    • 0029740284 scopus 로고    scopus 로고
    • Is something wrong with the tree of life?
    • Martin, W.: Is something wrong with the tree of life? - BioEssays 18: 523-527, 1996.
    • (1996) BioEssays , vol.18 , pp. 523-527
    • Martin, W.1
  • 48
    • 0027169132 scopus 로고
    • Evidence for a chimaeric nature of nuclear genomes: Eubacterial origin of eukaryotic glyceraldehyde-3-phosphate dehydrogenase genes
    • Martin, W., Brinkmann, H. Savona, C., Cerff, R.: Evidence for a chimaeric nature of nuclear genomes: Eubacterial origin of eukaryotic glyceraldehyde-3-phosphate dehydrogenase genes. - Proc. nat. Acad. Sci. USA 90: 8692-8696, 1993.
    • (1993) Proc. Nat. Acad. Sci. USA , vol.90 , pp. 8692-8696
    • Martin, W.1    Brinkmann, H.2    Savona, C.3    Cerff, R.4
  • 49
    • 0022780595 scopus 로고
    • Prokaryotic features of a nucleus encoded enzyme. cDNA sequences for chloroplast and cytosolic glyceraldehyde-3-phosphate dehydrogenase from mustard (Sinapis alba)
    • Martin, W., Cerff, R.: Prokaryotic features of a nucleus encoded enzyme. cDNA sequences for chloroplast and cytosolic glyceraldehyde-3-phosphate dehydrogenase from mustard (Sinapis alba). - Eur. J. Biochem. 159: 323-331, 1986.
    • (1986) Eur. J. Biochem. , vol.159 , pp. 323-331
    • Martin, W.1    Cerff, R.2
  • 50
    • 0030088125 scopus 로고    scopus 로고
    • Microsequencing and cDNA cloning of the Calvin cycle/OPPP enzyme ribose-5-phosphate isomerase (EC 5.3.1.6) from spinach chloroplasts
    • Martin, W., Henze, K., Kellermann, J., Flechner, A., Schnarrenberger, C.: Microsequencing and cDNA cloning of the Calvin cycle/OPPP enzyme ribose-5-phosphate isomerase (EC 5.3.1.6) from spinach chloroplasts. - Plant mol. Biol. 30: 795-805, 1996b.
    • (1996) Plant Mol. Biol. , vol.30 , pp. 795-805
    • Martin, W.1    Henze, K.2    Kellermann, J.3    Flechner, A.4    Schnarrenberger, C.5
  • 51
    • 0030293672 scopus 로고    scopus 로고
    • Higher plant chloroplast and cytosolic fructose-1,6-bisphophosphatase isoenzymes: Origins via duplication rather than prokaryote-eukaryote divergence
    • Martin, W., Mustafa, A.-Z., Henze, K., Schnarrenberger, C.: Higher plant chloroplast and cytosolic fructose-1,6-bisphophosphatase isoenzymes: Origins via duplication rather than prokaryote-eukaryote divergence. - Plant mol. Biol. 32: 485-491, 1996a.
    • (1996) Plant Mol. Biol. , vol.32 , pp. 485-491
    • Martin, W.1    Mustafa, A.-Z.2    Henze, K.3    Schnarrenberger, C.4
  • 52
    • 0019192754 scopus 로고
    • Chloroplast gene sequence for the large subunit of ribulose bisphosphatecarboxylase of maize
    • McIntosh, L., Poulsen, C., Bogorad, L.: Chloroplast gene sequence for the large subunit of ribulose bisphosphatecarboxylase of maize. - Nature 288: 556-560, 1980.
    • (1980) Nature , vol.288 , pp. 556-560
    • McIntosh, L.1    Poulsen, C.2    Bogorad, L.3
  • 53
    • 0028534791 scopus 로고
    • +-dependent glyceraldehyde-3-phosphate dehydrogenase in plastids of the gymnosperm Pinus sylvestris L
    • +-dependent glyceraldehyde-3-phosphate dehydrogenase in plastids of the gymnosperm Pinus sylvestris L. - Plant mol. Biol. 26: 1155-1166, 1994.
    • (1994) Plant Mol. Biol. , vol.26 , pp. 1155-1166
    • Meyer-Gauen, G.1    Schnarrenberger, C.2    Cerff, R.3    Martin, W.4
  • 54
    • 0024287911 scopus 로고
    • Cloning and sequencing of cDNA encoding the mature form of phosphoribulokinase from spinach
    • Milanez, S., Mural, R.J.: Cloning and sequencing of cDNA encoding the mature form of phosphoribulokinase from spinach. - Gene 66: 55-63, 1988.
    • (1988) Gene , vol.66 , pp. 55-63
    • Milanez, S.1    Mural, R.J.2
  • 55
    • 0028977898 scopus 로고
    • A nuclear-encoded form II Rubisco in dinoflagellates
    • Morse, D., Salois, P., Markovic, P., Hastings, J.W.: A nuclear-encoded form II Rubisco in dinoflagellates. - Science 268: 1622-1624, 1995.
    • (1995) Science , vol.268 , pp. 1622-1624
    • Morse, D.1    Salois, P.2    Markovic, P.3    Hastings, J.W.4
  • 56
    • 0014515279 scopus 로고
    • Lichtinduzierte, reversible Aktivitätssteigerung der NADP-abhängigen Glycerinaldehyd-3-phosphat-Dehydrogenase in Chloroplasten. Zum Mechanismus der Reaktion
    • Müller, B., Ziegler, I., Ziegler, H.: Lichtinduzierte, reversible Aktivitätssteigerung der NADP-abhängigen Glycerinaldehyd-3-phosphat-Dehydrogenase in Chloroplasten. Zum Mechanismus der Reaktion. - Eur. J. Biochem. 9: 101-106, 1969.
    • (1969) Eur. J. Biochem. , vol.9 , pp. 101-106
    • Müller, B.1    Ziegler, I.2    Ziegler, H.3
  • 57
    • 0019888195 scopus 로고
    • 4 photosynthesis. Purification and properties of thioredoxin-linked fructose bisphosphatase and sedoheptulose bisphosphatase from corn leaves
    • 4 photosynthesis. Purification and properties of thioredoxin-linked fructose bisphosphatase and sedoheptulose bisphosphatase from corn leaves. - J. biol. Chem. 256: 6119-6126, 1981.
    • (1981) J. Biol. Chem. , vol.256 , pp. 6119-6126
    • Nishizawa, A.N.1    Buchanan, B.B.2
  • 58
    • 0029556742 scopus 로고
    • Cloning of the amphibolic Calvin cycle/OPPP enzyme D-ribulose-5-phosphate 3-epimerase (EC 5.1.3.1) from spinach chloroplasts: Functional and evolutionary aspects
    • Nowitzki, U., Westhoff, P., Henze, K., Schnarrenberger, C., Martin W.: Cloning of the amphibolic Calvin cycle/OPPP enzyme D-ribulose-5-phosphate 3-epimerase (EC 5.1.3.1) from spinach chloroplasts: Functional and evolutionary aspects. - Plant mol. Biol. 29: 1279-1291, 1995.
    • (1995) Plant Mol. Biol. , vol.29 , pp. 1279-1291
    • Nowitzki, U.1    Westhoff, P.2    Henze, K.3    Schnarrenberger, C.4    Martin, W.5
  • 59
    • 0015246690 scopus 로고
    • Ribulose diphosphate carboxylase regulates soybean photorespiration
    • Ogren, W.L., Bowes, G.: Ribulose diphosphate carboxylase regulates soybean photorespiration. - Nature - new Biol. 230: 159-160, 1971.
    • (1971) Nature - New Biol. , vol.230 , pp. 159-160
    • Ogren, W.L.1    Bowes, G.2
  • 60
    • 0027354591 scopus 로고
    • Plant aldolase: CDNA and deduced amino-acid sequences of the chloroplast and cytosol enzyme from spinach
    • Pelzer-Reith, B., Penger, A., Schnarrenberger, C.: Plant aldolase: cDNA and deduced amino-acid sequences of the chloroplast and cytosol enzyme from spinach. - Plant mol. Biol. 21: 331-340, 1993.
    • (1993) Plant Mol. Biol. , vol.21 , pp. 331-340
    • Pelzer-Reith, B.1    Penger, A.2    Schnarrenberger, C.3
  • 61
    • 27544510430 scopus 로고
    • Mitteilung einer botanischen Preisfrage
    • Pringsheim, N.: Mitteilung einer botanischen Preisfrage. - Ber. deutsch, bot. Ges. 2: LXVIII-LXIX, 1884.
    • (1884) Ber. Deutsch, Bot. Ges. , vol.2
    • Pringsheim, N.1
  • 63
    • 0001282803 scopus 로고
    • The reductive pentose phosphate cycle. I. Phosphoribulokinase and ribulose diphosphate carboxylase
    • Racker, E.: The reductive pentose phosphate cycle. I. Phosphoribulokinase and ribulose diphosphate carboxylase. - Arch. Biochem. Biophys. 69: 300-310, 1957.
    • (1957) Arch. Biochem. Biophys. , vol.69 , pp. 300-310
    • Racker, E.1
  • 64
    • 0024297099 scopus 로고
    • Chloroplast fructose-1,6-bisphosphatase: The product of a mosaic gene
    • Raines, C.A., Lloyd, J.C., Longstaff, M., Bradley, D., Dyer, T.: Chloroplast fructose-1,6-bisphosphatase: the product of a mosaic gene. - Nucl. Acids Res. 16: 7931-7942, 1988.
    • (1988) Nucl. Acids Res. , vol.16 , pp. 7931-7942
    • Raines, C.A.1    Lloyd, J.C.2    Longstaff, M.3    Bradley, D.4    Dyer, T.5
  • 65
    • 0026557817 scopus 로고
    • cDNA and gene sequences of wheat chloroplast sedoheptulose-1,7-bisphosphatase reveal homology with fructose-1,6-bisphosphates
    • Raines, C.A., Lloyd, J.C, Willingham, N.M., Potts, S., Dyer, T.A.: cDNA and gene sequences of wheat chloroplast sedoheptulose-1,7-bisphosphatase reveal homology with fructose-1,6-bisphosphates. - Eur. J. Biochem. 205: 1053-1059, 1992.
    • (1992) Eur. J. Biochem. , vol.205 , pp. 1053-1059
    • Raines, C.A.1    Lloyd, J.C.2    Willingham, N.M.3    Potts, S.4    Dyer, T.A.5
  • 66
    • 0026630489 scopus 로고
    • Chloroplast and cytoplasmic enzymes: Isolation and sequencing of cDNAs coding for two distinct pea chloroplast aldolases
    • Razdan, K.K., Heinrikson, R.L., Zurcher-Neely, H.A., Morris, P., Anderson, L.E.: Chloroplast and cytoplasmic enzymes: isolation and sequencing of cDNAs coding for two distinct pea chloroplast aldolases. - Arch. Biochem. Biophys. 298: 192-197, 1993.
    • (1993) Arch. Biochem. Biophys. , vol.298 , pp. 192-197
    • Razdan, K.K.1    Heinrikson, R.L.2    Zurcher-Neely, H.A.3    Morris, P.4    Anderson, L.E.5
  • 67
    • 0012145678 scopus 로고
    • Photosynthesis with radioactive carbon. II. Chemical properties of the intermediates
    • Ruben, S., Kamen, M.D., Hassid, W.Z.: Photosynthesis with radioactive carbon. II. Chemical properties of the intermediates. - J. amer. chem. Soc. 62: 3443-3450, 1940.
    • (1940) J. Amer. Chem. Soc. , vol.62 , pp. 3443-3450
    • Ruben, S.1    Kamen, M.D.2    Hassid, W.Z.3
  • 69
    • 0014214772 scopus 로고
    • Nonidentical subunits of ribulose diphosphate carboxylase
    • Rutner, A., Lane, M.D.: Nonidentical subunits of ribulose diphosphate carboxylase. - Biochem. biophys. Res. Commun. 28: 531-537, 1967.
    • (1967) Biochem. Biophys. Res. Commun. , vol.28 , pp. 531-537
    • Rutner, A.1    Lane, M.D.2
  • 70
    • 27544491467 scopus 로고
    • Obersicht der Ergebnisse der neueren Untersuchungen über das Chlorophyll
    • Sachs, J.: Obersicht der Ergebnisse der neueren Untersuchungen über das Chlorophyll. - Flora 45: 129-221, 1862a.
    • (1862) Flora , vol.45 , pp. 129-221
    • Sachs, J.1
  • 71
    • 0037981907 scopus 로고
    • Ueber den Einfluss des Lichtes auf die Bildung des Amylum in den Chlorophyllkörnern
    • Sachs, J.: Ueber den Einfluss des Lichtes auf die Bildung des Amylum in den Chlorophyllkörnern. - Bot. Z. 20: 365-373, 1862b.
    • (1862) Bot. Z. , vol.20 , pp. 365-373
    • Sachs, J.1
  • 72
    • 3042773071 scopus 로고
    • Photosynthetic pyridine nucleotide reductase. I. Partial purification and properties of the enzyme from spinach
    • San Pietro, A., Lang, H.M.: Photosynthetic pyridine nucleotide reductase. I. Partial purification and properties of the enzyme from spinach. - J. biol. Chem. 231: 211-229, 1958.
    • (1958) J. Biol. Chem. , vol.231 , pp. 211-229
    • San Pietro, A.1    Lang, H.M.2
  • 73
    • 84995036286 scopus 로고
    • Light/dark modulation: Regulation of chloroplast metabolism in new light
    • Scheibe, R.: Light/dark modulation: regulation of chloroplast metabolism in new light. - Bot. Acta 103: 327-334, 1990.
    • (1990) Bot. Acta , vol.103 , pp. 327-334
    • Scheibe, R.1
  • 74
    • 0019878627 scopus 로고
    • Dark modulation of NADP-dependent malate dehydrogenase and glucose-6-phosphate dehydrogenase in the chloroplast
    • Scheibe, R., Anderson, L.E.: Dark modulation of NADP-dependent malate dehydrogenase and glucose-6-phosphate dehydrogenase in the chloroplast. - Biochim. biophys. Acta 636: 58-64, 1981.
    • (1981) Biochim. Biophys. Acta , vol.636 , pp. 58-64
    • Scheibe, R.1    Anderson, L.E.2
  • 75
    • 0020478953 scopus 로고
    • The stereochemical course of ribulosebisphosphate carboxylase. Reductive trapping of the C6-carbon reaction intermediate
    • Schloss, J.V., Lorimer, G.H.: The stereochemical course of ribulosebisphosphate carboxylase. Reductive trapping of the C6-carbon reaction intermediate. - J. mol. Biol. 257: 4691-4694, 1982.
    • (1982) J. Mol. Biol. , vol.257 , pp. 4691-4694
    • Schloss, J.V.1    Lorimer, G.H.2
  • 76
    • 0028917458 scopus 로고
    • Analysis of the primary structure of the chloroplast isozyme of triosephosphate isomerase from rye leaves by protein and cDNA sequencing indicates a eukaryotic origin of its gene
    • Schmidt, M., Svendsen, I., Feierabend, J.: Analysis of the primary structure of the chloroplast isozyme of triosephosphate isomerase from rye leaves by protein and cDNA sequencing indicates a eukaryotic origin of its gene. - Biochim. biophys. Acta 1261: 257-264, 1995.
    • (1995) Biochim. Biophys. Acta , vol.1261 , pp. 257-264
    • Schmidt, M.1    Svendsen, I.2    Feierabend, J.3
  • 77
    • 0028814117 scopus 로고
    • Enzymatic evidence for a complete oxidative pentose phosphate pathway in chloroplasts and an incomplete pathway in the cytosol of spinach leaves
    • Schnarrenberger, C., Flechner, A., Martin, W.: Enzymatic evidence for a complete oxidative pentose phosphate pathway in chloroplasts and an incomplete pathway in the cytosol of spinach leaves. - Plant Physiol. 108: 609-614, 1995.
    • (1995) Plant Physiol. , vol.108 , pp. 609-614
    • Schnarrenberger, C.1    Flechner, A.2    Martin, W.3
  • 78
    • 0015548474 scopus 로고
    • Two isoenzymes each of glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase in spinach leaves
    • Schnarrenberger, C., Oeser, A., Tolbert, N.E.: Two isoenzymes each of glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase in spinach leaves. - Arch. Biochem. Biophys. 154: 438-448, 1973.
    • (1973) Arch. Biochem. Biophys. , vol.154 , pp. 438-448
    • Schnarrenberger, C.1    Oeser, A.2    Tolbert, N.E.3
  • 81
    • 0023046216 scopus 로고
    • Evidence in favor of the symbiotic origin of chloroplasts: Primary structure and evolution of tobacco glyceraldehyde-3-phosphate dehydrogenase
    • Shin, M.-C., Lazar, G., Goodman, H.M.: Evidence in favor of the symbiotic origin of chloroplasts: primary structure and evolution of tobacco glyceraldehyde-3-phosphate dehydrogenase. - Cell 47: 73-80, 1986.
    • (1986) Cell , vol.47 , pp. 73-80
    • Shin, M.-C.1    Lazar, G.2    Goodman, H.M.3
  • 82
    • 0011209293 scopus 로고
    • The proteins of green leaves. IV. A high molecular weight protein comprising a large part of the cytoplasmic proteins
    • Singer, S.J., Eggman, L., Campbell, J.M., Wildman, S.G.: The proteins of green leaves. IV. A high molecular weight protein comprising a large part of the cytoplasmic proteins. - J. biol. Chem. 197: 233, 1952.
    • (1952) J. Biol. Chem. , vol.197 , pp. 233
    • Singer, S.J.1    Eggman, L.2    Campbell, J.M.3    Wildman, S.G.4
  • 83
    • 0014572985 scopus 로고
    • Distribution of enzymes in mesophyll and parenchymasheath chloroplasts of maize leaves in relation to the C4-dicarboxylic acid pathway of photosynthesis
    • Slack, C.R., Hatch, M.D., Goodchild, D.J.: Distribution of enzymes in mesophyll and parenchymasheath chloroplasts of maize leaves in relation to the C4-dicarboxylic acid pathway of photosynthesis. - Biochem. J. 114: 489-498, 1969.
    • (1969) Biochem. J. , vol.114 , pp. 489-498
    • Slack, C.R.1    Hatch, M.D.2    Goodchild, D.J.3
  • 84
    • 1842318308 scopus 로고
    • Glycolysis in CAM plants
    • Sutton, B.G.: Glycolysis in CAM plants. - Aust. J. Plant Physiol. 2: 389-402, 1975.
    • (1975) Aust. J. Plant Physiol. , vol.2 , pp. 389-402
    • Sutton, B.G.1
  • 86
    • 0016165638 scopus 로고
    • D-Ribulose 1,5-diphosphate carboxylase from Rhodospirillum rubrum. II. Quaternary structure, composition, catalytic, and immunological properties
    • Tabita, F.R., McFadden, B.A.: D-Ribulose 1,5-diphosphate carboxylase from Rhodospirillum rubrum. II. Quaternary structure, composition, catalytic, and immunological properties. - J. biol. Chem. 249: 3459-3464, 1974.
    • (1974) J. Biol. Chem. , vol.249 , pp. 3459-3464
    • Tabita, F.R.1    McFadden, B.A.2
  • 87
    • 0347737041 scopus 로고
    • Glycolate pathway
    • Nat. Acad. Sci. - Nat. Res. Council, Publ. 1145
    • Tolbert, N.B.: Glycolate pathway. - In: Photosynthetic Mechanisms in Green Plants. Pp. 648-662. Nat. Acad. Sci. - Nat. Res. Council, Publ. 1145, 1963.
    • (1963) Photosynthetic Mechanisms in Green Plants , pp. 648-662
    • Tolbert, N.B.1
  • 88
    • 0000478533 scopus 로고
    • Microbodies - Peroxisomes and glyoxysomes
    • Tolbert, N.B.: Microbodies - peroxisomes and glyoxysomes. - Annu. Rev. Plant Physiol. 22: 45-74, 1971.
    • (1971) Annu. Rev. Plant Physiol. , vol.22 , pp. 45-74
    • Tolbert, N.B.1
  • 89
    • 0014409902 scopus 로고
    • Peroxisomes in spinach leaves containing enzymes related to glycolate metabolism
    • Tolbert, N.E., Oeser, A., Kisaki, T., Hageman, R.H., Yamazaki, R.K.: Peroxisomes in spinach leaves containing enzymes related to glycolate metabolism. - J. biol. Chem. 243: 5179-5184, 1968.
    • (1968) J. Biol. Chem. , vol.243 , pp. 5179-5184
    • Tolbert, N.E.1    Oeser, A.2    Kisaki, T.3    Hageman, R.H.4    Yamazaki, R.K.5
  • 91
    • 27544445516 scopus 로고
    • Activation of spinach chloroplast glyceraldehyde-3 - Phosphate dehydrogenase. Effect of glycerate 1,3-bisphosphate
    • Trost, P., Scaliarini, S., Valenti, V., Pupillo, P.: Activation of spinach chloroplast glyceraldehyde-3 - phosphate dehydrogenase. Effect of glycerate 1,3-bisphosphate. - Planta 185: 337-343, 1993.
    • (1993) Planta , vol.185 , pp. 337-343
    • Trost, P.1    Scaliarini, S.2    Valenti, V.3    Pupillo, P.4
  • 93
    • 3042821667 scopus 로고
    • Proteins of green leaves. IX. Enzymatic properties of fraction-I protein isolated by a specific antibody
    • van Groot, G., Wildman, S.G.: Proteins of green leaves. IX. Enzymatic properties of fraction-I protein isolated by a specific antibody. - Biochim. biophys. Acta 90: 309-317, 1964.
    • (1964) Biochim. Biophys. Acta , vol.90 , pp. 309-317
    • Van Groot, G.1    Wildman, S.G.2
  • 94
    • 34250940918 scopus 로고
    • On the morphology and physiology of the purple bacteria
    • van Niel, C.B.: On the morphology and physiology of the purple bacteria. - Arch. Mikrobiol. 3: 1-112, 1931.
    • (1931) Arch. Mikrobiol. , vol.3 , pp. 1-112
    • Van Niel, C.B.1
  • 97
    • 0007860633 scopus 로고
    • Über die Geschwindigkeit der photochemischen Kohlensäurezersetzung in lebenden Zellen
    • Warburg, O.: Über die Geschwindigkeit der photochemischen Kohlensäurezersetzung in lebenden Zellen. - Biochem. Z. 100: 230-270, 1919.
    • (1919) Biochem. Z. , vol.100 , pp. 230-270
    • Warburg, O.1
  • 98
    • 0009164379 scopus 로고
    • Über die Geschwindigkeit der photochemischen Kohlensäurezersetzung in lebenden Zellen
    • Warburg, O.: Über die Geschwindigkeit der photochemischen Kohlensäurezersetzung in lebenden Zellen. - Biochem. Z. 103: 188-217, 1920.
    • (1920) Biochem. Z. , vol.103 , pp. 188-217
    • Warburg, O.1
  • 99
    • 3042818733 scopus 로고
    • Über den Energieumsatz bei der Kohlensäureassimilation
    • Warburg, O., Negelein, E.: Über den Energieumsatz bei der Kohlensäureassimilation. - Z. physik. Chem. 102: 235-266, 1922.
    • (1922) Z. Physik. Chem. , vol.102 , pp. 235-266
    • Warburg, O.1    Negelein, E.2
  • 100
    • 0011209261 scopus 로고
    • Über den Einfluß der Wellenlänge und den Energieumsatz bei Kohlensäureassimilation
    • Warburg, O., Negelein, E.: Über den Einfluß der Wellenlänge und den Energieumsatz bei Kohlensäureassimilation. - Z. physik. Chem. 106: 191-218, 1923.
    • (1923) Z. Physik. Chem. , vol.106 , pp. 191-218
    • Warburg, O.1    Negelein, E.2
  • 101
    • 0019343489 scopus 로고
    • Genetic and biochemical implications of the endosymbiotic origin of the chloroplast
    • Weeden, N.F.: Genetic and biochemical implications of the endosymbiotic origin of the chloroplast. - J. mol. Evol. 17: 133-139, 1981.
    • (1981) J. Mol. Evol. , vol.17 , pp. 133-139
    • Weeden, N.F.1
  • 102
    • 0001329772 scopus 로고
    • The enzymatic formation of phosphoglyceric acid from ribulose diphosphate and carbon dioxide
    • Weissbach, A., Horecker, B.L., Hurwitz, J.: The enzymatic formation of phosphoglyceric acid from ribulose diphosphate and carbon dioxide. - J. biol. Chem. 218: 795-810, 1956.
    • (1956) J. Biol. Chem. , vol.218 , pp. 795-810
    • Weissbach, A.1    Horecker, B.L.2    Hurwitz, J.3
  • 106
    • 84872625210 scopus 로고
    • The proteins of green leaves. I. Isolation, enzymatic properties and auxin content of spinach cytoplasmic proteins
    • Wildman, S.G., Bonner, J.: The proteins of green leaves. I. Isolation, enzymatic properties and auxin content of spinach cytoplasmic proteins. - Arch. Biochem. 14: 381-413, 1947.
    • (1947) Arch. Biochem. , vol.14 , pp. 381-413
    • Wildman, S.G.1    Bonner, J.2
  • 109
    • 0017336797 scopus 로고
    • Thioredoxin and glutathione regulate photosynthesis in chloroplasts
    • Wolosiuk, R.A., Buchanan, B.B.: Thioredoxin and glutathione regulate photosynthesis in chloroplasts. - Nature 266: 565-567, 1977.
    • (1977) Nature , vol.266 , pp. 565-567
    • Wolosiuk, R.A.1    Buchanan, B.B.2
  • 110
    • 0000474564 scopus 로고
    • +-abhängige Glycerinaldehyd-3-phosphat-Dehydrogenase
    • +-abhängige Glycerinaldehyd-3-phosphat-Dehydrogenase. - Planta 65: 369-380, 1965.
    • (1965) Planta , vol.65 , pp. 369-380
    • Ziegler, H.1    Ziegler, I.2
  • 111
    • 0017308249 scopus 로고
    • Efficient purification and molecular properties of spinach chloroplast fructose 1,6-bisphosphatase
    • Zimmermann, G., Kelly, G.J., Latzko, E.: Efficient purification and molecular properties of spinach chloroplast fructose 1,6-bisphosphatase. - Eur. J. Biochem. 70: 361-367, 1976.
    • (1976) Eur. J. Biochem. , vol.70 , pp. 361-367
    • Zimmermann, G.1    Kelly, G.J.2    Latzko, E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.