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Volumn 94, Issue 1, 2007, Pages 121-143

Discoveries in Rubisco (Ribulose 1,5-bisphosphate carboxylase/oxygenase): A historical perspective

Author keywords

Carbamylation; Carbon fixation; History; Inhibitors; Light regulation; Photorespiration; Rubisco; Rubisco activase

Indexed keywords

PENTOSE; RIBULOSE; RIBULOSEBISPHOSPHATE CARBOXYLASE; UNCLASSIFIED DRUG;

EID: 34548177803     PISSN: 01668595     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11120-007-9225-6     Document Type: Review
Times cited : (130)

References (313)
  • 1
    • 34548149989 scopus 로고
    • Mechanism of the carboxydismutase reaction. II. Carboxylation of the enzyme
    • Akoyunoglou G, Calvin M (1963) Mechanism of the carboxydismutase reaction. II. Carboxylation of the enzyme. Biochem Zeits 338:20-30
    • (1963) Biochem Zeits , vol.338 , pp. 20-30
    • Akoyunoglou, G.1    Calvin, M.2
  • 2
    • 0014401022 scopus 로고
    • Molecular diversity of the ribulose-1,5-diphosphate carboxylase from photosynthetic microorganisms
    • Anderson LE, Price GB, Fuller RC (1968) Molecular diversity of the ribulose-1,5-diphosphate carboxylase from photosynthetic microorganisms. Science 161:482-484
    • (1968) Science , vol.161 , pp. 482-484
    • Anderson, L.E.1    Price, G.B.2    Fuller, R.C.3
  • 3
    • 0014750754 scopus 로고
    • Ribulose diphosphate carboxylase: III. Altered forms of ribulose diphosphate carboxylase from mutant tomato plants
    • Andersen WR, Wildner GF, Criddle RS (1970) Ribulose diphosphate carboxylase: III. Altered forms of ribulose diphosphate carboxylase from mutant tomato plants. Arch Biochem Biophys 137:84-90
    • (1970) Arch Biochem Biophys , vol.137 , pp. 84-90
    • Andersen, W.R.1    Wildner, G.F.2    Criddle, R.S.3
  • 4
    • 10244252723 scopus 로고    scopus 로고
    • Conversion of d-hamamelose into 2-carboxy-d-arabinitol and 2-carboxy-d-arabinitol 1-phosphate in leaves of Phaseolus vulgaris L
    • Andralojc PJ, Keys AJ, Martindale W, Dawson GW, Parry MAJ (1996) Conversion of d-hamamelose into 2-carboxy-d-arabinitol and 2-carboxy-d- arabinitol 1-phosphate in leaves of Phaseolus vulgaris L. J Biol Chem 271:26803-26809
    • (1996) J Biol Chem , vol.271 , pp. 26803-26809
    • Andralojc, P.J.1    Keys, A.J.2    Martindale, W.3    Dawson, G.W.4    Parry, M.A.J.5
  • 6
    • 0025819595 scopus 로고
    • Pyruvate is a by-product of catalysis by ribulosebisphosphate carboxylase/oxygenase
    • Andrews TJ, Kane HJ (1991) Pyruvate is a by-product of catalysis by ribulosebisphosphate carboxylase/oxygenase. J Biol Chem 266:9447-9452
    • (1991) J Biol Chem , vol.266 , pp. 9447-9452
    • Andrews, T.J.1    Kane, H.J.2
  • 7
    • 0000691060 scopus 로고
    • Rubisco: Structure, mechanisms, and prospects for improvement
    • Academic Press New York
    • Andrews TJ, Lorimer GH (1987) Rubisco: structure, mechanisms, and prospects for improvement. In: Hatch MD, Boardman NK (eds) The biochemistry of plants, vol 10. Academic Press, New York, pp 131-218
    • (1987) The Biochemistry of Plants , vol.10 , pp. 131-218
    • Andrews, T.J.1    Lorimer, G.H.2    Hatch, M.D.3    Boardman, N.K.4
  • 8
    • 0015911742 scopus 로고
    • Ribulose diphosphate oxygenase. I. Synthesis of phosphoglycolate by fraction 1 protein of leaves
    • Andrews TJ, Lorimer GH, Tolbert NE (1973) Ribulose diphosphate oxygenase. I. Synthesis of phosphoglycolate by fraction 1 protein of leaves. Biochemistry 12:1-18
    • (1973) Biochemistry , vol.12 , pp. 1-18
    • Andrews, T.J.1    Lorimer, G.H.2    Tolbert, N.E.3
  • 9
    • 0030591422 scopus 로고    scopus 로고
    • Different location in dark-adapted leaves of Phaseolus vulgaris of ribulose-1,5-bisphosphate carboxylase/oxygenase and 2-carboxyarabinitol 1-phosphate
    • Anwaruzzaman, Nakano Y, Yokota A (1996) Different location in dark-adapted leaves of Phaseolus vulgaris of ribulose-1,5-bisphosphate carboxylase/oxygenase and 2-carboxyarabinitol 1-phosphate. FEBS Lett 388:223-227
    • (1996) FEBS Lett , vol.388 , pp. 223-227
    • Anwaruzzaman1    Nakano, Y.2    Yokota, A.3
  • 10
    • 0141993683 scopus 로고    scopus 로고
    • A functional link between RuBisCO-like protein of Bacillus and photosynthetic RuBisCO
    • Ashida H, Saito Y, Kojima C, Kobayashi K, Ogasawara N, Yokota A (2003) A functional link between RuBisCO-like protein of Bacillus and photosynthetic RuBisCO. Science 302:286-290
    • (2003) Science , vol.302 , pp. 286-290
    • Ashida, H.1    Saito, Y.2    Kojima, C.3    Kobayashi, K.4    Ogasawara, N.5    Yokota, A.6
  • 11
    • 0019879667 scopus 로고
    • Interaction of sugar phosphates with the catalytic site of ribulose-1,5-bisphosphate carboxylase
    • Badger MR, Lorimer GH (1981) Interaction of sugar phosphates with the catalytic site of ribulose-1,5-bisphosphate carboxylase. Biochemistry 20:2219-2225
    • (1981) Biochemistry , vol.20 , pp. 2219-2225
    • Badger, M.R.1    Lorimer, G.H.2
  • 14
    • 0016612256 scopus 로고
    • The structure of form I crystals of d-ribulose-1,5-diphosphate carboxylase
    • Baker TS, Eisenberg D, Eiserling FA, Weissman L (1975) The structure of form I crystals of d-ribulose-1,5-diphosphate carboxylase. J Mol Biol 91:391-398
    • (1975) J Mol Biol , vol.91 , pp. 391-398
    • Baker, T.S.1    Eisenberg, D.2    Eiserling, F.A.3    Weissman, L.4
  • 15
    • 0019333950 scopus 로고
    • Protein synthesis in chloroplasts. XI. Assembly of newly-synthesized large subunits into ribulose bisphosphate carboxylase in isolated pea chloroplasts
    • Barraclough R, Ellis RJ (1980) Protein synthesis in chloroplasts. XI. Assembly of newly-synthesized large subunits into ribulose bisphosphate carboxylase in isolated pea chloroplasts. Biochim Biophys Acta 608:19-31
    • (1980) Biochim Biophys Acta , vol.608 , pp. 19-31
    • Barraclough, R.1    Ellis, R.J.2
  • 16
    • 0001137784 scopus 로고
    • Abscisic acid control of rbcS and cab transcription in tomato leaves
    • Bartholomew DM, Bartley GE, Scolnik P (1991) Abscisic acid control of rbcS and cab transcription in tomato leaves. Plant Physiol 96:291-296
    • (1991) Plant Physiol , vol.96 , pp. 291-296
    • Bartholomew, D.M.1    Bartley, G.E.2    Scolnik, P.3
  • 17
    • 0041859263 scopus 로고    scopus 로고
    • Mapping the carbon reduction cycle: A personal retrospective
    • Bassham JA (2003) Mapping the carbon reduction cycle: a personal retrospective. Photosynth Res 76:35-52
    • (2003) Photosynth Res , vol.76 , pp. 35-52
    • Bassham, J.A.1
  • 18
    • 0041344682 scopus 로고
    • 2 to glycolic acid and other products during photosynthesis by Chlorella
    • 2 to glycolic acid and other products during photosynthesis by Chlorella. Biochem Biophys Res Commun 9:376-380
    • (1962) Biochem Biophys Res Commun , vol.9 , pp. 376-380
    • Bassham, J.A.1    Kirk, M.2
  • 19
    • 0001148367 scopus 로고
    • The path of carbon in photosynthesis. XXI. the cyclic regeneration of carbon dioxide acceptor
    • Bassham JA, Benson AA, Kay LD, Harris AZ, Wilson AT, Calvin M (1954) The path of carbon in photosynthesis. XXI. The cyclic regeneration of carbon dioxide acceptor. J Am Chem Soc 76:1760-1770
    • (1954) J Am Chem Soc , vol.76 , pp. 1760-1770
    • Bassham, J.A.1    Benson, A.A.2    Kay, L.D.3    Harris, A.Z.4    Wilson, A.T.5    Calvin, M.6
  • 20
    • 0019182515 scopus 로고
    • Molecular cloning and sequencing of cDNA encoding the precursor to the small subunit of chloroplast ribulose-1,5-bisphosphate carboxylase
    • Bedbrook JR, Smith SM, Ellis RJ (1980) Molecular cloning and sequencing of cDNA encoding the precursor to the small subunit of chloroplast ribulose-1,5-bisphosphate carboxylase. Nature 287:692-697
    • (1980) Nature , vol.287 , pp. 692-697
    • Bedbrook, J.R.1    Smith, S.M.2    Ellis, R.J.3
  • 21
    • 0001341186 scopus 로고
    • Mass spectrophotometric studies of carbon-13 variation in corn and other grasses
    • Bender MM (1968) Mass spectrophotometric studies of carbon-13 variation in corn and other grasses. Radiocarbon 10:468-472
    • (1968) Radiocarbon , vol.10 , pp. 468-472
    • Bender, M.M.1
  • 22
    • 49649157486 scopus 로고
    • 12C ratios of plants in relation to the pathway of photosynthetic carbon dioxide fixation
    • 12C ratios of plants in relation to the pathway of photosynthetic carbon dioxide fixation. Phytochemistry 10:1239-1244
    • (1971) Phytochemistry , vol.10 , pp. 1239-1244
    • Bender, M.M.1
  • 23
    • 0000862360 scopus 로고
    • 2 photosynthesis products
    • 2 photosynthesis products. J Am Chem Soc 73:2971-2972
    • (1951) J Am Chem Soc , vol.73 , pp. 2971-2972
    • Benson, A.A.1
  • 24
    • 0036409693 scopus 로고    scopus 로고
    • Following the path of carbon in photosynthesis: A personal story
    • Benson AA (2002) Following the path of carbon in photosynthesis: a personal story. Photosynth Res 73:29-49
    • (2002) Photosynth Res , vol.73 , pp. 29-49
    • Benson, A.A.1
  • 25
    • 0001814998 scopus 로고
    • The path of carbon in photosynthesis. VII. Respiration and photosynthesis
    • Benson AA, Calvin M (1950) The path of carbon in photosynthesis. VII. Respiration and photosynthesis. J Exp Bot 1:63-68
    • (1950) J Exp Bot , vol.1 , pp. 63-68
    • Benson, A.A.1    Calvin, M.2
  • 26
    • 0001676790 scopus 로고
    • The path of carbon in photosynthesis. V. Paper chromatography and radioautography of the products
    • Benson AA, Bassham JA, Calvin M, Goodale TC, Hass VA, Stepka W (1950) The path of carbon in photosynthesis. V. Paper chromatography and radioautography of the products. J Am Chem Soc 72:1710-1718
    • (1950) J Am Chem Soc , vol.72 , pp. 1710-1718
    • Benson, A.A.1    Bassham, J.A.2    Calvin, M.3    Goodale, T.C.4    Hass, V.A.5    Stepka, W.6
  • 28
    • 0000417407 scopus 로고
    • Isolation, identification, and synthesis of 2-carboxyarabinitol 1-phosphate, a diurnal regulator of ribulose-bisphosphate carboxylase activity
    • Berry JA, Lorimer GH, Pierce J, Seemann JR, Meek J, Freas S (1987) Isolation, identification, and synthesis of 2-carboxyarabinitol 1-phosphate, a diurnal regulator of ribulose-bisphosphate carboxylase activity. Proc Natl Acad Sci USA 84:734-738
    • (1987) Proc Natl 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
  • 29
    • 0021849973 scopus 로고
    • Transcriptional and post-transcriptional regulation of ribulose 1,5-bisphosphate carboxylase gene expression in light- and dark-grown amaranth cotyledons
    • Berry JO, Nikolau BJ, Carr JP, Klessig DF (1985) Transcriptional and post-transcriptional regulation of ribulose 1,5-bisphosphate carboxylase gene expression in light- and dark-grown amaranth cotyledons. Mol Cell Biol 5:2238-2246
    • (1985) Mol Cell Biol , vol.5 , pp. 2238-2246
    • Berry, J.O.1    Nikolau, B.J.2    Carr, J.P.3    Klessig, D.F.4
  • 30
    • 0025465479 scopus 로고
    • Light-mediated control of translational initiation of ribulose-1,5-bisphosphate carboxylase in amaranth cotyledons
    • Berry JO, Breiding DE, Klessig DF (1990) Light-mediated control of translational initiation of Ribulose-1,5-bisphosphate carboxylase in Amaranth Cotyledons. Plant Cell 2:795-803
    • (1990) Plant Cell , vol.2 , pp. 795-803
    • Berry, J.O.1    Breiding, D.E.2    Klessig, D.F.3
  • 31
    • 0020440905 scopus 로고
    • The nucleotide sequence, expression and evolution of one member of a multigene family encoding the small subunit of ribulose-1,5-bisphosphate carboxylase in soybean
    • Berry-Lowe SL, McKnight TD, Meagher RB (1982) The nucleotide sequence, expression and evolution of one member of a multigene family encoding the small subunit of ribulose-1,5-bisphosphate carboxylase in soybean. J Mol Appl Genet 1:483-498
    • (1982) J Mol Appl Genet , vol.1 , pp. 483-498
    • Berry-Lowe, S.L.1    McKnight, T.D.2    Meagher, R.B.3
  • 32
    • 0018172551 scopus 로고
    • Evidence for the involvement of superoxide anions in the oxygenase reaction of ribulose-1,5-diphosphate carboxylase
    • Bhagwat AJ, Sane PV (1978) Evidence for the involvement of superoxide anions in the oxygenase reaction of ribulose-1,5-diphosphate carboxylase. Biochem Biophys Res Commun 84:865
    • (1978) Biochem Biophys Res Commun , vol.84 , pp. 865
    • Bhagwat, A.J.1    Sane, P.V.2
  • 33
    • 0018171103 scopus 로고
    • Specific inhibition of oxygenase activity of ribulose-1,5-diphosphate carboxylase by hydroxylamine
    • Bhagwat AJ, Ramakrishna J, Sane PV (1978) Specific inhibition of oxygenase activity of ribulose-1,5-diphosphate carboxylase by hydroxylamine. Biochem Biophys Res Commun 83:954-962
    • (1978) Biochem Biophys Res Commun , vol.83 , pp. 954-962
    • Bhagwat, A.J.1    Ramakrishna, J.2    Sane, P.V.3
  • 34
    • 84980184829 scopus 로고
    • Carboxydismutase activity in shade-adapted and sun-adapted species of higher plants
    • Björkman O (1968a) Carboxydismutase activity in shade-adapted and sun-adapted species of higher plants. Physiol Plant 21:1-10
    • (1968) Physiol Plant , vol.21 , pp. 1-10
    • Björkman, O.1
  • 35
    • 0001979338 scopus 로고
    • Further studies of photosynthetic properties in sun and shade ecotypes of Solidago virgaurea
    • Björkman O (1968b) Further studies of photosynthetic properties in sun and shade ecotypes of Solidago virgaurea. Physiol Plant 21:84-99
    • (1968) Physiol Plant , vol.21 , pp. 84-99
    • Björkman, O.1
  • 36
    • 0015867189 scopus 로고
    • Protein synthesis in chloroplasts. I. Light-driven synthesis of the large subunit of Fraction I protein by isolated pea chloroplasts
    • Blair GE, Ellis RJ (1973) Protein synthesis in chloroplasts. I. Light-driven synthesis of the large subunit of Fraction I protein by isolated pea chloroplasts. Biochim Biophys Acta 319:223-224
    • (1973) Biochim Biophys Acta , vol.319 , pp. 223-224
    • Blair, G.E.1    Ellis, R.J.2
  • 37
    • 0042178263 scopus 로고    scopus 로고
    • Photosynthesis research: Advances through molecular biology-the beginnings, 1975-1980s and on
    • Bogorad L (2003) Photosynthesis research: advances through molecular biology-the beginnings, 1975-1980s and on. Photosynth Res 76:13-33
    • (2003) Photosynth Res , vol.76 , pp. 13-33
    • Bogorad, L.1
  • 38
    • 0001317710 scopus 로고
    • 2: Photosynthetic responses mediated through Rubisco
    • 2: photosynthetic responses mediated through Rubisco. Plant Cell Environ 14:795-806
    • (1991) Plant Cell Environ , vol.14 , pp. 795-806
    • Bowes, G.1
  • 39
    • 0015212072 scopus 로고
    • Phosphoglycolate production catalyzed by ribulose 1,5-diphosphate carboxylase
    • Bowes G, Ogren WL, Hageman RH (1971) Phosphoglycolate production catalyzed by ribulose 1,5-diphosphate carboxylase. Biochem Biophys Res Commun 45:716-722
    • (1971) Biochem Biophys Res Commun , vol.45 , pp. 716-722
    • Bowes, G.1    Ogren, W.L.2    Hageman, R.H.3
  • 41
    • 0017897469 scopus 로고
    • Ribulose-1,5-bisphosphate carboxylase and oxygenase from green plants are two different enzymes
    • Brändén R (1978) Ribulose-1,5-bisphosphate carboxylase and oxygenase from green plants are two different enzymes. Biochem Biophys Res Commun 81:539-546
    • (1978) Biochem Biophys Res Commun , vol.81 , pp. 539-546
    • Brändén, R.1
  • 42
    • 0019333811 scopus 로고
    • The formation of l-3-phosphoglyceric acid by ribulose-1,5-bisphosphate carboxylase
    • Brändén R, Nilsson T, Styring S (1980a) The formation of l-3-phosphoglyceric acid by ribulose-1,5-bisphosphate carboxylase. Biochem Biophys Res Commun 92:1297-1305
    • (1980) Biochem Biophys Res Commun , vol.92 , pp. 1297-1305
    • Brändén, R.1    Nilsson, T.2    Styring, S.3
  • 43
    • 0019333813 scopus 로고
    • L-3-phosphoglyceric acid, formed by ribulose-1,5-bisphosphate carboxylase, is the primary substrate for photorespiration
    • Brändén R, Nilsson T, Styring S, Ångström J (1980b) l-3-phosphoglyceric acid, formed by ribulose-1,5-bisphosphate carboxylase, is the primary substrate for photorespiration. Biochem Biophys Res Commun 92:1306-1312
    • (1980) Biochem Biophys Res Commun , vol.92 , pp. 1306-1312
    • Brändén, R.1    Nilsson, T.2    Styring, S.3    Ångström, J.4
  • 45
    • 0000164847 scopus 로고
    • 2 specificity of ribulose 1,5-bisphosphate carboxylase/oxygenase and the rate of respiration in the light. Estimates from gas-exchange measurements on spinach
    • 2 specificity of ribulose 1,5-bisphosphate carboxylase/oxygenase and the rate of respiration in the light. Estimates from gas-exchange measurements on spinach. Planta 165:397-406
    • (1985) Planta , vol.165 , pp. 397-406
    • Brooks, A.1    Farquhar, G.D.2
  • 46
    • 0001276970 scopus 로고
    • Protein-bound ribulose bisphosphate correlates with deactivation of ribulose bisphosphate carboxylase in leaves
    • Brooks A, Portis AR Jr (1988) Protein-bound ribulose bisphosphate correlates with deactivation of ribulose bisphosphate carboxylase in leaves. Plant Physiol 87:244-249
    • (1988) Plant Physiol , vol.87 , pp. 244-249
    • Brooks, A.1    Portis Jr., A.R.2
  • 48
    • 0001222591 scopus 로고
    • Chemical and photochemical reactions of thioctic acid and related disulfides
    • Calvin M (1954) Chemical and photochemical reactions of thioctic acid and related disulfides. Fed Proc 13:697-711
    • (1954) Fed Proc , vol.13 , pp. 697-711
    • Calvin, M.1
  • 49
    • 34249966346 scopus 로고
    • Forty years of photosynthesis and related activities
    • Calvin M (1989) Forty years of photosynthesis and related activities. Photosynth Res 21:3-16
    • (1989) Photosynth Res , vol.21 , pp. 3-16
    • Calvin, M.1
  • 50
    • 0000528430 scopus 로고
    • The path of carbon in photosynthesis
    • Calvin M, Benson AA (1948) The path of carbon in photosynthesis. Science 107:476-480
    • (1948) Science , vol.107 , pp. 476-480
    • Calvin, M.1    Benson, A.A.2
  • 51
    • 0011855905 scopus 로고
    • The path of carbon in photosynthesis IV: The identity and sequence of the intermediates in sucrose synthesis
    • Calvin M, Benson AA (1949) The path of carbon in photosynthesis IV: the identity and sequence of the intermediates in sucrose synthesis. Science 109:140-142
    • (1949) Science , vol.109 , pp. 140-142
    • Calvin, M.1    Benson, A.A.2
  • 53
    • 0015506187 scopus 로고
    • Chloroplast DNA codes for the primary structure of the large subunit of Fraction I protein
    • Chan P-K, Wildman SG (1972) Chloroplast DNA codes for the primary structure of the large subunit of Fraction I protein. Biochim Biophys Acta 277:677-680
    • (1972) Biochim Biophys Acta , vol.277 , pp. 677-680
    • Chan, P.-K.1    Wildman, S.G.2
  • 54
    • 0023663713 scopus 로고
    • Sliding-layer conformational change limited by the quaternary structure of plant Rubisco
    • Chapman M, Suh SW, Cascio D, Smith WW, Eisenberg D (1987) Sliding-layer conformational change limited by the quaternary structure of plant Rubisco. Nature 329:354-356
    • (1987) Nature , vol.329 , pp. 354-356
    • Chapman, M.1    Suh, S.W.2    Cascio, D.3    Smith, W.W.4    Eisenberg, D.5
  • 56
    • 0027398292 scopus 로고
    • Chloroplast gene sequences and the study of plant evolution
    • Clegg MT (1993) Chloroplast gene sequences and the study of plant evolution. Proc Natl Acad Sci USA 90:363-367
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 363-367
    • Clegg, M.T.1
  • 59
    • 0021473404 scopus 로고
    • Tissue-specific and light-regulated expression of a pea nuclear gene encoding the small subunit of ribulose-1,5-bisphosphate carboxylase
    • Coruzzi G, Broglie R, Edwards C, Chua N-H (1984) Tissue-specific and light-regulated expression of a pea nuclear gene encoding the small subunit of ribulose-1,5-bisphosphate carboxylase. EMBO J 3:1671-1679
    • (1984) EMBO J , vol.3 , pp. 1671-1679
    • Coruzzi, G.1    Broglie, R.2    Edwards, C.3    Chua, N.-H.4
  • 62
    • 0001017356 scopus 로고
    • Differential expression of the eight genes of the petunia ribulose bisphosphate carboxylase small subunit multi-gene family
    • Dean C, van den Elzen P, Tamaki S, Dunsmuir P, Bedbrook J (1985) Differential expression of the eight genes of the petunia ribulose bisphosphate carboxylase small subunit multi-gene family. EMBO J 4:3055-3061
    • (1985) EMBO J , vol.4 , pp. 3055-3061
    • Dean, C.1    Van Den Elzen, P.2    Tamaki, S.3    Dunsmuir, P.4    Bedbrook, J.5
  • 63
    • 0029897169 scopus 로고    scopus 로고
    • Rampant horizontal transfer and duplication of rubisco genes in eubacteria and plastids
    • Delwiche CF, Palmer JD (1996) Rampant horizontal transfer and duplication of rubisco genes in eubacteria and plastids. Mol Biol Evol 13:873-882
    • (1996) Mol Biol Evol , vol.13 , pp. 873-882
    • Delwiche, C.F.1    Palmer, J.D.2
  • 64
    • 0001165153 scopus 로고    scopus 로고
    • Oxidative stress induces partial degradation of the large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase in isolated chloroplasts of barley
    • Desimone M, Henke A, Wagner E (1996) Oxidative stress induces partial degradation of the large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase in isolated chloroplasts of barley. Plant Physiol 111:789-796
    • (1996) Plant Physiol , vol.111 , pp. 789-796
    • Desimone, M.1    Henke, A.2    Wagner, E.3
  • 65
    • 0012244040 scopus 로고
    • In vitro synthesis and processing of a putative precursor for the small subunit of ribulose-1,5-bisphosphate carboxylase of Chlamydomonas reinhardtii
    • Dobberstein B, Blobel G, Chua N-H (1977) In vitro synthesis and processing of a putative precursor for the small subunit of ribulose-1,5- bisphosphate carboxylase of Chlamydomonas reinhardtii. Proc Natl Acad Sci USA 74:1082-1085
    • (1977) Proc Natl Acad Sci USA , vol.74 , pp. 1082-1085
    • Dobberstein, B.1    Blobel, G.2    Chua, N.-H.3
  • 66
    • 0000024737 scopus 로고
    • The proteins of green leaves. VII. Synthesis and decay of the cytoplasmic proteins during the life of the tobacco leaf
    • Dorner RW, Kahn A, Wildman SG (1957) The proteins of green leaves. VII. Synthesis and decay of the cytoplasmic proteins during the life of the tobacco leaf. J Biol Chem 229:945-952
    • (1957) J Biol Chem , vol.229 , pp. 945-952
    • Dorner, R.W.1    Kahn, A.2    Wildman, S.G.3
  • 67
    • 0034685616 scopus 로고    scopus 로고
    • The transition between the open and closed states of rubisco is triggered by the inter-phosphate distance of the bound bisphosphate
    • Duff AP, Andrews TJ, Curmi PMG (2000) The transition between the open and closed states of rubisco is triggered by the inter-phosphate distance of the bound bisphosphate. J Mol Biol 298:903-916
    • (2000) J Mol Biol , vol.298 , pp. 903-916
    • Duff, A.P.1    Andrews, T.J.2    Curmi, P.M.G.3
  • 68
    • 11944267330 scopus 로고
    • A kinetic characterization of slow inactivation of ribulosebisphosphate carboxylase during catalysis
    • Edmondson DL, Badger MR, Andrews TJ (1990a) A kinetic characterization of slow inactivation of ribulosebisphosphate carboxylase during catalysis. Plant Physiol 93:1376-1382
    • (1990) Plant Physiol , vol.93 , pp. 1376-1382
    • Edmondson, D.L.1    Badger, M.R.2    Andrews, T.J.3
  • 69
    • 0012535188 scopus 로고
    • Slow inactivation ribulosebisphosphate carboxylase during catalysis is not due to decarbamylation of the catalytic site
    • Edmondson DL, Badger MR, Andrews TJ (1990b) Slow inactivation ribulosebisphosphate carboxylase during catalysis is not due to decarbamylation of the catalytic site. Plant Physiol 93:1383-1389
    • (1990) Plant Physiol , vol.93 , pp. 1383-1389
    • Edmondson, D.L.1    Badger, M.R.2    Andrews, T.J.3
  • 70
    • 0001041057 scopus 로고
    • Slow inactivation ribulosebisphosphate carboxylase during catalysis is caused by accumulation of a slow, tight-binding inhibitor at the catalytic site
    • Edmondson DL, Badger MR, Andrews TJ (1990c) Slow inactivation ribulosebisphosphate carboxylase during catalysis is caused by accumulation of a slow, tight-binding inhibitor at the catalytic site. Plant Physiol 93:1390-1397
    • (1990) Plant Physiol , vol.93 , pp. 1390-1397
    • Edmondson, D.L.1    Badger, M.R.2    Andrews, T.J.3
  • 71
    • 0025021677 scopus 로고
    • Substrate isomerization inhibits ribulosebisphosphate carboxylase during catalysis
    • Edmondson DL, Kane HJ, Andrews TJ (1990d) Substrate isomerization inhibits ribulosebisphosphate carboxylase during catalysis. FEBS Lett 260:62-66
    • (1990) FEBS Lett , vol.260 , pp. 62-66
    • Edmondson, D.L.1    Kane, H.J.2    Andrews, T.J.3
  • 72
    • 49249144575 scopus 로고
    • The most abundant protein in the world
    • Ellis RJ (1979) The most abundant protein in the world. Trends Biochem Sci 4:241-244
    • (1979) Trends Biochem Sci , vol.4 , pp. 241-244
    • Ellis, R.J.1
  • 73
    • 3042725094 scopus 로고    scopus 로고
    • Chloroplasts to chaperones: How one thing led to another
    • Ellis RJ (2004) Chloroplasts to chaperones: how one thing led to another. Photosynth Res 80:333-343
    • (2004) Photosynth Res , vol.80 , pp. 333-343
    • Ellis, R.J.1
  • 75
    • 0033582465 scopus 로고    scopus 로고
    • Presence of a structurally novel type ribulose-bisphosphate carboxylase/oxygenase in the hyperthermophilic archaeon, Pyrococcus kodakaraensis KOD1
    • Ezaki S, Maeda N, Kishimoto T, Atomi H, Imanaka T (1999) Presence of a structurally novel type ribulose-bisphosphate carboxylase/oxygenase in the hyperthermophilic archaeon, Pyrococcus kodakaraensis KOD1. J Biol Chem 274:5078-5082
    • (1999) J Biol Chem , vol.274 , pp. 5078-5082
    • Ezaki, S.1    Maeda, N.2    Kishimoto, T.3    Atomi, H.4    Imanaka, T.5
  • 78
    • 0001569341 scopus 로고    scopus 로고
    • Moderately high temperatures inhibit ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) activase-mediated activation of Rubisco
    • Feller U, Crafts-Brandner SJ, Salvucci ME (1998) Moderately high temperatures inhibit ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) activase-mediated activation of Rubisco. Plant Physiol 116:539-546
    • (1998) Plant Physiol , vol.116 , pp. 539-546
    • Feller, U.1    Crafts-Brandner, S.J.2    Salvucci, M.E.3
  • 79
    • 0014101803 scopus 로고
    • Mechanism of ribulose-diphosphate carboxydismutase reaction
    • Fiedler F, Müllhofer G, Trebst A, Rose IA (1967) Mechanism of ribulose-diphosphate carboxydismutase reaction. Eur J Biochem 1:395-399
    • (1967) Eur J Biochem , vol.1 , pp. 395-399
    • Fiedler, F.1    Müllhofer, G.2    Trebst, A.3    Rose, I.A.4
  • 80
    • 4544272017 scopus 로고    scopus 로고
    • Modified pathway to synthesize ribulose 1,5-bisphosphate in methanogenic archaea
    • Finn MW, Tabita FR (2004) Modified pathway to synthesize ribulose 1,5-bisphosphate in methanogenic archaea. J Bacteriol 186:6360-6366
    • (2004) J Bacteriol , vol.186 , pp. 6360-6366
    • Finn, M.W.1    Tabita, F.R.2
  • 81
    • 0000479187 scopus 로고
    • Developmental regulation of two genes encoding ribulose-bisphosphate carboxylase small subunit in pea and transgenic petunia plants: Phytochrome response and blue-light induction
    • Fluhr R, Chua N-H (1986) Developmental regulation of two genes encoding ribulose-bisphosphate carboxylase small subunit in pea and transgenic petunia plants: phytochrome response and blue-light induction. Proc Natl Acad Sci USA 83:2358-2362
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 2358-2362
    • Fluhr, R.1    Chua, N.-H.2
  • 82
    • 0024286551 scopus 로고
    • Non-cyclic photoreductive carbon fixation in photosynthesis. Light and dark transients of the glycerate-3-P special pair
    • Fong FK, Butcher KA (1988) Non-cyclic photoreductive carbon fixation in photosynthesis. Light and dark transients of the glycerate-3-P special pair. Biochem Biophys Res Commun 150:399-404
    • (1988) Biochem Biophys Res Commun , vol.150 , pp. 399-404
    • Fong, F.K.1    Butcher, K.A.2
  • 83
    • 0004561190 scopus 로고
    • Effect of oxygen on photosynthesis, photorespiration, and respiration in detached leaves. I
    • Forrester ML, Krotkov G, Nelson CD (1966) Effect of oxygen on photosynthesis, photorespiration, and respiration in detached leaves. I. Soybean Plant Physiol 41:422-427
    • (1966) Soybean Plant Physiol , vol.41 , pp. 422-427
    • Forrester, M.L.1    Krotkov, G.2    Nelson, C.D.3
  • 85
    • 0000850438 scopus 로고
    • Photosynthesis, leaf resistances, and ribulose-1,5-bisphosphate carboxylase degradation in senescing barley leaves
    • Friedrich JW, Huffaker RC (1980) Photosynthesis, leaf resistances, and ribulose-1,5-bisphosphate carboxylase degradation in senescing barley leaves. Plant Physiol 65:1103-1107
    • (1980) Plant Physiol , vol.65 , pp. 1103-1107
    • Friedrich, J.W.1    Huffaker, R.C.2
  • 87
    • 0041121558 scopus 로고
    • Energy storage: Photosynthesis
    • Academic Press New York
    • Gaffron H (1960) Energy storage: photosynthesis. In: Steward FC (ed) Plant physiology. Academic Press, New York, pp 136-160
    • (1960) Plant Physiology , pp. 136-160
    • Gaffron, H.1    Steward, F.C.2
  • 89
    • 34548172504 scopus 로고
    • Different specificity/photorespiration in diploid vs. tetraploid wheat
    • Garrett MK (1978) Different specificity/photorespiration in diploid vs. tetraploid wheat. Nature 274:913-915
    • (1978) Nature , vol.274 , pp. 913-915
    • Garrett, M.K.1
  • 90
    • 0021821536 scopus 로고
    • Assembly in E. coli of a functional multi-subunit ribulose bisphosphate carboxylase from a blue-green alga
    • Gatenby AA, van der Vies SM, Bradley D (1985) Assembly in E. coli of a functional multi-subunit ribulose bisphosphate carboxylase from a blue-green alga. Nature 314:617-620
    • (1985) Nature , vol.314 , pp. 617-620
    • Gatenby, A.A.1    Van Der Vies, S.M.2    Bradley, D.3
  • 92
    • 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 JT, Gatenby AA, Lorimer GH (1989) Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg-ATP. Nature 342:884-889
    • (1989) Nature , vol.342 , pp. 884-889
    • Goloubinoff, P.1    Christeller, J.T.2    Gatenby, A.A.3    Lorimer, G.H.4
  • 93
    • 34447128483 scopus 로고    scopus 로고
    • Discoveries in oxygenic photosynthesis (1727-2003): A perspective
    • Govindjee, Beatty JT, Gest H, Allen JF (eds). Springer, Dordrecht
    • Govindjee, Krogmann D (2005) Discoveries in oxygenic photosynthesis (1727-2003): a perspective. In: Govindjee, Beatty JT, Gest H, Allen JF (eds) Discoveries in photosynthesis. Advances in photosynthesis and respiration, vol 20. Springer, Dordrecht, pp 63-105
    • (2005) Discoveries in Photosynthesis. Advances in Photosynthesis and Respiration , vol.20 , pp. 63-105
    • Govindjee1    Krogmann, D.2
  • 94
    • 34548156019 scopus 로고
    • Phytochrome as the primary photoregulator of the synthesis of Calvin Cycle enzymes in etiolated pea seedlings
    • Graham D, Grieve AM, Smillie RM (1968) Phytochrome as the primary photoregulator of the synthesis of Calvin Cycle enzymes in etiolated pea seedlings. Nature 218:89-90
    • (1968) Nature , vol.218 , pp. 89-90
    • Graham, D.1    Grieve, A.M.2    Smillie, R.M.3
  • 95
    • 0028843014 scopus 로고
    • Rubisco synthesis, assembly, mechanism, and regulation
    • Gutteridge S, Gatenby AA (1995) Rubisco synthesis, assembly, mechanism, and regulation. Plant Cell 7:809-819
    • (1995) Plant Cell , vol.7 , pp. 809-819
    • Gutteridge, S.1    Gatenby, A.A.2
  • 96
    • 0001167763 scopus 로고
    • A phosphatase from chloroplast stroma of Nicotiana tabacum hydrolyses 2'-carboxyarabinitol 1-phosphate, the natural inhibitor of Rubisco to 2'-carboxyarabinitol
    • Gutteridge S, Julien B (1989) A phosphatase from chloroplast stroma of Nicotiana tabacum hydrolyses 2'-carboxyarabinitol 1-phosphate, the natural inhibitor of Rubisco to 2'-carboxyarabinitol. FEBS Lett 254:225-230
    • (1989) FEBS Lett , vol.254 , pp. 225-230
    • Gutteridge, S.1    Julien, B.2
  • 98
    • 0006819594 scopus 로고
    • A site-specific mutation within the active site of ribulose-1,5- bisphosphate carboxylase of Rhodospirillum rubrum
    • Gutteridge S, Sigal I, Thomas B, Arentzen R, Cordova A, Lorimer G (1984b) A site-specific mutation within the active site of ribulose-1,5-bisphosphate carboxylase of Rhodospirillum rubrum. EMBO J 3:2737-2743
    • (1984) EMBO J , vol.3 , pp. 2737-2743
    • Gutteridge, S.1    Sigal, I.2    Thomas, B.3    Arentzen, R.4    Cordova, A.5    Lorimer, G.6
  • 101
    • 0001062752 scopus 로고
    • Photosynthetic fractionation of the stable isotopes of oxygen and carbon
    • Guy RD, Fogel ML, Berry JA (1993) Photosynthetic fractionation of the stable isotopes of oxygen and carbon. Plant Physiol 101:37-47
    • (1993) Plant Physiol , vol.101 , pp. 37-47
    • Guy, R.D.1    Fogel, M.L.2    Berry, J.A.3
  • 102
    • 0003091390 scopus 로고
    • Ribulose-1,5-bisphosphate carboxylase protein during flag leaf senescence
    • Hall NP, Keys AJ, Merrett MJ (1978) Ribulose-1,5-bisphosphate carboxylase protein during flag leaf senescence. J Exp Bot 29:31-37
    • (1978) J Exp Bot , vol.29 , pp. 31-37
    • Hall, N.P.1    Keys, A.J.2    Merrett, M.J.3
  • 103
    • 7144226594 scopus 로고    scopus 로고
    • Regulation of Rubisco activation in antisense plants of tobacco containing reduced levels of Rubisco activase
    • Hammond ET, Andrews TJ, Mott KA, Woodrow IE (1998a) Regulation of Rubisco activation in antisense plants of tobacco containing reduced levels of Rubisco activase. Plant J 14:101-110
    • (1998) Plant J , vol.14 , pp. 101-110
    • Hammond, E.T.1    Andrews, T.J.2    Mott, K.A.3    Woodrow, I.E.4
  • 104
    • 0000435087 scopus 로고    scopus 로고
    • Regulation of ribulose-1,5-bisphosphate carboxylase/oxygenase by carbamylation and 2-carboxyarabinitol 1-phosphate in tobacco: Insights from studies of antisense plants containing reduced amounts of Rubisco activase
    • Hammond ET, Andrews TJ, Woodrow IE (1998b) Regulation of ribulose-1,5-bisphosphate carboxylase/oxygenase by carbamylation and 2-carboxyarabinitol 1-phosphate in tobacco: insights from studies of antisense plants containing reduced amounts of Rubisco activase. Plant Physiol 118:1463-1471
    • (1998) Plant Physiol , vol.118 , pp. 1463-1471
    • Hammond, E.T.1    Andrews, T.J.2    Woodrow, I.E.3
  • 105
    • 0035836695 scopus 로고    scopus 로고
    • A ribulose-1,5-bisphosphate carboxylase/oxygenase (RubisCO)-like protein from Chlorobium tepidum that is involved with sulfur metabolism and the response to oxidative stress
    • Hanson TE, Tabita FR (2001) A ribulose-1,5-bisphosphate carboxylase/oxygenase (RubisCO)-like protein from Chlorobium tepidum that is involved with sulfur metabolism and the response to oxidative stress. Proc Natl Acad Sci USA 98:4397-4402
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 4397-4402
    • Hanson, T.E.1    Tabita, F.R.2
  • 107
    • 0016431910 scopus 로고
    • Protein synthesis in chloroplasts. V. Translation of messenger RNA for the large subunit of fraction I protein in a heterologous cell-free system
    • Hartley MR, Wheeler A, Ellis RJ (1975) Protein synthesis in chloroplasts. V. Translation of messenger RNA for the large subunit of fraction I protein in a heterologous cell-free system. J Mol Biol 91:67-77
    • (1975) J Mol Biol , vol.91 , pp. 67-77
    • Hartley, M.R.1    Wheeler, A.2    Ellis, R.J.3
  • 108
    • 0027342550 scopus 로고
    • Chemical and genetic probes of the active-site of d-ribulose-1,5- bisphosphate carboxylase oxygenase-a retrospective based on the 3-dimensional structure
    • Hartmen FC, Harpel MR (1993) Chemical and genetic probes of the active-site of d-ribulose-1,5-bisphosphate carboxylase oxygenase-a retrospective based on the 3-dimensional structure. Adv Enzymol 67:1-75
    • (1993) Adv Enzymol , vol.67 , pp. 1-75
    • Hartmen, F.C.1    Harpel, M.R.2
  • 109
    • 0028245595 scopus 로고
    • Structure, function, regulation, and assembly of d-ribulose-1,5- bisphosphate carboxylase-oxygenase
    • Hartman FC, Harpel MR (1994) Structure, function, regulation, and assembly of d-ribulose-1,5-bisphosphate carboxylase-oxygenase. Annu Rev Biochem 63:197-234
    • (1994) Annu Rev Biochem , vol.63 , pp. 197-234
    • Hartman, F.C.1    Harpel, M.R.2
  • 112
    • 85013838124 scopus 로고    scopus 로고
    • 3rd Elsevier Academic Press Amsterdam
    • Heldt HW (2005) Plant biochemistry, 3rd edn. Elsevier Academic Press, Amsterdam
    • (2005) Plant Biochemistry
    • Heldt, H.W.1
  • 114
    • 0017811491 scopus 로고
    • Synthesis and transport of the small subunit of chloroplast ribulose bisphosphate carboxylase
    • Highfield PE, Ellis RJ (1978) Synthesis and transport of the small subunit of chloroplast ribulose bisphosphate carboxylase. Nature 271:420-424
    • (1978) Nature , vol.271 , pp. 420-424
    • Highfield, P.E.1    Ellis, R.J.2
  • 115
    • 0001419896 scopus 로고
    • Changes in activities of enzymes of carbon metabolism in leaves during exposure of plants to low temperature
    • Holiday AS, Martindale W, Alred R, Brooks AL, Leegood RC (1992) Changes in activities of enzymes of carbon metabolism in leaves during exposure of plants to low temperature. Plant Physiol 98:1105-1114
    • (1992) Plant Physiol , vol.98 , pp. 1105-1114
    • Holiday, A.S.1    Martindale, W.2    Alred, R.3    Brooks, A.L.4    Leegood, R.C.5
  • 116
    • 0000126192 scopus 로고
    • Degradation of 2-carboxyarabinitol 1-phosphate by a specific chloroplast phosphatase
    • Holbrook GP, Bowes G, Salvucci ME (1989) Degradation of 2-carboxyarabinitol 1-phosphate by a specific chloroplast phosphatase. Plant Physiol 90:673-678
    • (1989) Plant Physiol , vol.90 , pp. 673-678
    • Holbrook, G.P.1    Bowes, G.2    Salvucci, M.E.3
  • 117
    • 0015158987 scopus 로고
    • The isolation and the partial characterization of the pyrenoid protein from Eremosphaera viridis
    • Holdsworth RH (1971) The isolation and the partial characterization of the pyrenoid protein from Eremosphaera viridis. J Cell Biol 15:499-513
    • (1971) J Cell Biol , vol.15 , pp. 499-513
    • Holdsworth, R.H.1
  • 118
    • 0037073492 scopus 로고    scopus 로고
    • The pentose phosphate pathway
    • Horecker BL (2002) The pentose phosphate pathway. J Biol Chem 277:47965-47971
    • (2002) J Biol Chem , vol.277 , pp. 47965-47971
    • Horecker, B.L.1
  • 119
    • 3042820241 scopus 로고
    • The enzymatic synthesis and properties of ribulose 1,5-diphosphate
    • Horecker BL, Hurwitz J, Weissbach A (1956) The enzymatic synthesis and properties of ribulose 1,5-diphosphate. J Biol Chem 218:785-794
    • (1956) J Biol Chem , vol.218 , pp. 785-794
    • Horecker, B.L.1    Hurwitz, J.2    Weissbach, A.3
  • 120
    • 0037899997 scopus 로고    scopus 로고
    • The life of ribulose 1,5-bisphosphate carboxylase/oxygenase- posttranslational facts and mysteries
    • Houtz RL, Portis AR Jr (2003) The life of ribulose 1,5-bisphosphate carboxylase/oxygenase-posttranslational facts and mysteries. Arch Biochem Biophys 414:150-158
    • (2003) Arch Biochem Biophys , vol.414 , pp. 150-158
    • Houtz, R.L.1    Portis Jr., A.R.2
  • 121
    • 0024636180 scopus 로고
    • Post-translational modifications in the large subunit of ribulose bisphosphate carboxylase/oxygenase
    • Houtz RL, Stults JT, Mulligan RM, Tolbert NE (1989) Post-translational modifications in the large subunit of ribulose bisphosphate carboxylase/ oxygenase. Proc Natl Acad Sci USA 86:1855-1859
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 1855-1859
    • Houtz, R.L.1    Stults, J.T.2    Mulligan, R.M.3    Tolbert, N.E.4
  • 122
    • 27044441759 scopus 로고
    • Differential localization of Fraction I protein between chloroplast types
    • Huber SC, Hall TC, Edwards GE (1976) Differential localization of Fraction I protein between chloroplast types. Plant Physiol 57:730-733
    • (1976) Plant Physiol , vol.57 , pp. 730-733
    • Huber, S.C.1    Hall, T.C.2    Edwards, G.E.3
  • 123
    • 0010637937 scopus 로고
    • Effects of mild water stress on enzymes of nitrate assimilation of carboxylative phase of photosynthesis in barley
    • Huffaker RC, Radin T, Kleinkop GE, Cox EL (1970) Effects of mild water stress on enzymes of nitrate assimilation of carboxylative phase of photosynthesis in barley. Crop Sci 10:471-474
    • (1970) Crop Sci , vol.10 , pp. 471-474
    • Huffaker, R.C.1    Radin, T.2    Kleinkop, G.E.3    Cox, E.L.4
  • 125
    • 0031113714 scopus 로고    scopus 로고
    • The large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase is fragmented into 37-kDa and 16-kDa polypeptides by active oxygen in the lysates of chloroplasts from primary leaves of wheat
    • Ishida H, Nishimori Y, Sugisawa M, Makino A, Mae T (1997) The large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase is fragmented into 37-kDa and 16-kDa polypeptides by active oxygen in the lysates of chloroplasts from primary leaves of wheat. Plant Cell Physiol 38:471-479
    • (1997) Plant Cell Physiol , vol.38 , pp. 471-479
    • Ishida, H.1    Nishimori, Y.2    Sugisawa, M.3    Makino, A.4    Mae, T.5
  • 126
    • 3042744750 scopus 로고
    • Formation of 3-phosphoglyceric acid by carbon dioxide fixation with spinach leaf enzymes
    • Jakoby WB, Drummond DO, Ochoa S (1956) Formation of 3-phosphoglyceric acid by carbon dioxide fixation with spinach leaf enzymes. J Biol Chem 218:811-822
    • (1956) J Biol Chem , vol.218 , pp. 811-822
    • Jakoby, W.B.1    Drummond, D.O.2    Ochoa, S.3
  • 127
    • 7244244031 scopus 로고    scopus 로고
    • 2 assimilation in light
    • 2 assimilation in light. Photosynth Res 82:187-193
    • (2004) Photosynth Res , vol.82 , pp. 187-193
    • Jensen, R.G.1
  • 128
    • 0000162154 scopus 로고
    • Ribulose 1,5-bisphosphate carboxylase-oxygenase
    • Jensen RG, Bahr JT (1977) Ribulose 1,5-bisphosphate carboxylase- oxygenase. Annu Rev Plant Physiol 28:379-400
    • (1977) Annu Rev Plant Physiol , vol.28 , pp. 379-400
    • Jensen, R.G.1    Bahr, J.T.2
  • 129
    • 0014414751 scopus 로고
    • Photosynthesis by isolated chloroplasts. III. Light activation of the carboxylation reaction
    • Jensen RG, Bassham JA (1968) Photosynthesis by isolated chloroplasts. III. Light activation of the carboxylation reaction. Biochim Biophys Acta 153:227-234
    • (1968) Biochim Biophys Acta , vol.153 , pp. 227-234
    • Jensen, R.G.1    Bassham, J.A.2
  • 130
    • 0021016118 scopus 로고
    • Inhibition of ribulose bisphosphate carboxylase by substrate ribulose 1,5-bisphosphate
    • Jordan DB, Chollet R (1983) Inhibition of ribulose bisphosphate carboxylase by substrate ribulose 1,5-bisphosphate. J Biol Chem 258:13752-13758
    • (1983) J Biol Chem , vol.258 , pp. 13752-13758
    • Jordan, D.B.1    Chollet, R.2
  • 131
    • 0019470148 scopus 로고
    • Species variation in the specificity of ribulose bisphosphate carboxylase/oxygenase
    • Jordan DB, Ogren WL (1981) Species variation in the specificity of ribulose bisphosphate carboxylase/oxygenase. Nature 291:513-515
    • (1981) Nature , vol.291 , pp. 513-515
    • Jordan, D.B.1    Ogren, W.L.2
  • 132
    • 0000081033 scopus 로고
    • 2 specificity of ribulose 1,5-bisphosphate carboxylase/oxygenase. Dependence on ribulosebisphosphate concentration, pH and temperature
    • 2 specificity of ribulose 1,5-bisphosphate carboxylase/oxygenase. Dependence on ribulosebisphosphate concentration, pH and temperature. Planta 161:308-313
    • (1984) Planta , vol.161 , pp. 308-313
    • Jordan, D.B.1    Ogren, W.L.2
  • 133
    • 0000663150 scopus 로고
    • Binding of phosphorylated effectors by active and inactive forms of ribulose-1,5-bisphosphate carboxylase
    • Jordan DB, Chollet R, Ogren WL (1983) Binding of phosphorylated effectors by active and inactive forms of ribulose-1,5-bisphosphate carboxylase. Biochemistry 22:3410-3418
    • (1983) Biochemistry , vol.22 , pp. 3410-3418
    • Jordan, D.B.1    Chollet, R.2    Ogren, W.L.3
  • 135
    • 0028264871 scopus 로고
    • Relocation of the plastid rbcL gene to the nucleus yields functional ribulose-1,5-bisphosphate carboxylase in tobacco chloroplasts
    • Kanevski I, Maliga P (1994) Relocation of the plastid rbcL gene to the nucleus yields functional ribulose-1,5-bisphosphate carboxylase in tobacco chloroplasts. Proc Nat Acad Sci USA 91:1969-1973
    • (1994) Proc Nat Acad Sci USA , vol.91 , pp. 1969-1973
    • Kanevski, I.1    Maliga, P.2
  • 136
    • 0032818243 scopus 로고    scopus 로고
    • Plastome engineering of ribulose-1,5-bisphosphate carboxylase/oxygenase in tobacco to form a sunflower large subunit and tobacco small subunit hybrid
    • Kanevski I, Maliga P, Rhoades DF, Gutteridge S (1999) Plastome engineering of ribulose-1,5-bisphosphate carboxylase/oxygenase in tobacco to form a sunflower large subunit and tobacco small subunit hybrid. Plant Physiol 119:133-141
    • (1999) Plant Physiol , vol.119 , pp. 133-141
    • Kanevski, I.1    Maliga, P.2    Rhoades, D.F.3    Gutteridge, S.4
  • 137
    • 0003406285 scopus 로고
    • Phosphorylation of small subunit plays a critical role in the regulation of RuBPCase in moss and spinach
    • Kaul R, Saluja D, Sachar RC (1986) Phosphorylation of small subunit plays a critical role in the regulation of RuBPCase in moss and spinach. FEBS Lett 209:63-70
    • (1986) FEBS Lett , vol.209 , pp. 63-70
    • Kaul, R.1    Saluja, D.2    Sachar, R.C.3
  • 138
    • 0015520411 scopus 로고
    • Studies on Fraction I protein. IV. Mode of inheritance of the primary structure in relation to whether chloroplast or nuclear DNA contains the code for a chloroplast protein
    • Kawashima N, Wildman SG (1972) Studies on Fraction I protein. IV. Mode of inheritance of the primary structure in relation to whether chloroplast or nuclear DNA contains the code for a chloroplast protein. Biochim Biophys Acta 262:42-49
    • (1972) Biochim Biophys Acta , vol.262 , pp. 42-49
    • Kawashima, N.1    Wildman, S.G.2
  • 139
    • 0000661985 scopus 로고
    • Is there another player in the game of Rubisco regulation?
    • Keys AJ, Major I, Parry MAJ (1995) Is there another player in the game of Rubisco regulation? J Exp Bot 46:1245-1251
    • (1995) J Exp Bot , vol.46 , pp. 1245-1251
    • Keys, A.J.1    Major, I.2    Parry, M.A.J.3
  • 140
    • 0033573109 scopus 로고    scopus 로고
    • 2'-carboxy-d-arabinitol 1-phosphate (CA1P) protects ribulose-1,5- bisphosphate carboxylase/oxygenase against proteolytic breakdown
    • Khan S, Andraloj PJ, Lea PJ, Parry MAJ (1999) 2'-carboxy-d-arabinitol 1-phosphate (CA1P) protects ribulose-1,5-bisphosphate carboxylase/oxygenase against proteolytic breakdown. Eur J Biochem 266:840-847
    • (1999) Eur J Biochem , vol.266 , pp. 840-847
    • Khan, S.1    Andraloj, P.J.2    Lea, P.J.3    Parry, M.A.J.4
  • 143
    • 0034984584 scopus 로고    scopus 로고
    • Crystal structure of a novel-type archaeal Rubisco with pentagonal symmetry
    • Kitano K, Maeda N, Fukui T, Atomi H, Imanaka T, Miki K (2001) Crystal structure of a novel-type archaeal Rubisco with pentagonal symmetry. Structure 9:473-481
    • (2001) Structure , vol.9 , pp. 473-481
    • Kitano, K.1    Maeda, N.2    Fukui, T.3    Atomi, H.4    Imanaka, T.5    Miki, K.6
  • 144
    • 0000791842 scopus 로고
    • Mechanisms for light-dependent regulation of ribulose-1,5-bisphosphate carboxylase activity and photosynthesis in intact leaves
    • Kobza J, Seemann JR (1988) Mechanisms for light-dependent regulation of ribulose-1,5-bisphosphate carboxylase activity and photosynthesis in intact leaves. Proc Natl Acad Sci USA 85:3815-3819
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 3815-3819
    • Kobza, J.1    Seemann, J.R.2
  • 145
    • 0037880292 scopus 로고
    • Re-examination of the three-dimensional structure of the small subunit of RuBisCo from higher-plants
    • Knight S, Andersson I, Brändén C-I (1989) Re-examination of the three-dimensional structure of the small subunit of RuBisCo from higher-plants. Science 244:702-705
    • (1989) Science , vol.244 , pp. 702-705
    • Knight, S.1    Andersson, I.2    Brändén, C.-I.3
  • 146
    • 0025160560 scopus 로고
    • Crystallographic analysis of ribulose 1,5-bisphosphate carboxylase from spinach at 2.4 Å resolution: Subunit interactions and active site
    • Knight S, Andersson I, Brändén C-I (1990) Crystallographic analysis of ribulose 1,5-bisphosphate carboxylase from spinach at 2.4 Å resolution: subunit interactions and active site. J Mol Biol 215:113-160
    • (1990) J Mol Biol , vol.215 , pp. 113-160
    • Knight, S.1    Andersson, I.2    Brändén, C.-I.3
  • 147
    • 0003329817 scopus 로고
    • Regulation of the expression of rbcS and other photosynthetic genes by carbohydrates: A mechanism for the 'sink regulation' of photosynthesis?
    • Krapp A, Hofmann B, Schäfer C, Stitt M (1993) Regulation of the expression of rbcS and other photosynthetic genes by carbohydrates: a mechanism for the 'sink regulation' of photosynthesis? Plant J 3:817-828
    • (1993) Plant J , vol.3 , pp. 817-828
    • Krapp, A.1    Hofmann, B.2    Schäfer, C.3    Stitt, M.4
  • 149
    • 0017289421 scopus 로고
    • Tobacco fraction 1 protein: A unique genetic marker
    • Kung S (1976) Tobacco fraction 1 protein: a unique genetic marker. Science 191:429-434
    • (1976) Science , vol.191 , pp. 429-434
    • Kung, S.1
  • 150
    • 36849152778 scopus 로고
    • Regulation of RuBP carboxylase/oxygenase activity and its relationship to plant photorespiration
    • Kung SD, Marsho TV (1976) Regulation of RuBP carboxylase/oxygenase activity and its relationship to plant photorespiration. Nature 259:352-356
    • (1976) Nature , vol.259 , pp. 352-356
    • Kung, S.D.1    Marsho, T.V.2
  • 151
    • 0016267373 scopus 로고
    • Multiple peptide composition of the large and small subunits of Nicotiana tabacum fraction I protein ascertained by fingerprinting and electrofocusing
    • Kung SD, Sakano K, Wildman SG (1974) Multiple peptide composition of the large and small subunits of Nicotiana tabacum fraction I protein ascertained by fingerprinting and electrofocusing. Biochim Biophys Acta 365:138-147
    • (1974) Biochim Biophys Acta , vol.365 , pp. 138-147
    • Kung, S.D.1    Sakano, K.2    Wildman, S.G.3
  • 153
    • 0030764617 scopus 로고    scopus 로고
    • Specificity for activase is changed by a pro-89 to arg substitution in the large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase
    • Larson EM, O'Brien CM, Zhu G, Spreitzer RJ, Portis AR Jr (1997) Specificity for activase is changed by a pro-89 to arg substitution in the large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase. J Biol Chem 272:17033-17037
    • (1997) J Biol Chem , vol.272 , pp. 17033-17037
    • Larson, E.M.1    O'Brien, C.M.2    Zhu, G.3    Spreitzer, R.J.4    Portis Jr., A.R.5
  • 154
    • 0013781793 scopus 로고
    • A mutant strain of Chlamydomonas reinhardi lacking ribulose diphosphate carboxylase activity
    • Levine RP, Togasaki RK (1965) A mutant strain of Chlamydomonas reinhardi lacking ribulose diphosphate carboxylase activity. Proc Natl Acad Sci USA 53:987-990
    • (1965) Proc Natl Acad Sci USA , vol.53 , pp. 987-990
    • Levine, R.P.1    Togasaki, R.K.2
  • 155
    • 21644453935 scopus 로고    scopus 로고
    • Two residues of Rubisco activase involved in recognition of the Rubisco substrate
    • Li C, Salvucci ME, Portis AR Jr (2005) Two residues of Rubisco activase involved in recognition of the Rubisco substrate. J Biol Chem 280:24864-24869
    • (2005) J Biol Chem , vol.280 , pp. 24864-24869
    • Li, C.1    Salvucci, M.E.2    Portis Jr., A.R.3
  • 156
    • 0007796722 scopus 로고
    • Carbon dioxide assimilation by leaves, isolated chloroplasts, and ribulose bisphosphate carboxylase from spinach
    • Lilley RM, Wlaker DA (1975) Carbon dioxide assimilation by leaves, isolated chloroplasts, and ribulose bisphosphate carboxylase from spinach. Plant Physiol 55:1087-1092
    • (1975) Plant Physiol , vol.55 , pp. 1087-1092
    • Lilley, R.M.1    Wlaker, D.A.2
  • 158
  • 159
    • 0000927733 scopus 로고
    • The carboxylation and oxygenation of ribulose 1,5-bisphosphate: The primary events in photosynthesis and photorespiration
    • Lorimer GH (1981) The carboxylation and oxygenation of ribulose 1,5-bisphosphate: the primary events in photosynthesis and photorespiration. Annu Rev Plant Physiol Plant Mol Biol 32:349-383
    • (1981) Annu Rev Plant Physiol Plant Mol Biol , vol.32 , pp. 349-383
    • Lorimer, G.H.1
  • 161
    • 0015911743 scopus 로고
    • Ribulose diphosphate oxygenase. II. Further proof of reaction products and mechanism of action
    • Lorimer GH, Andrews TJ, Tolbert NE (1973) Ribulose diphosphate oxygenase. II. Further proof of reaction products and mechanism of action. Biochemistry 12:18-23
    • (1973) Biochemistry , vol.12 , pp. 18-23
    • Lorimer, G.H.1    Andrews, T.J.2    Tolbert, N.E.3
  • 162
    • 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 GH, Badger MR, Andrews TJ (1976) 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) Biochemistry , vol.15 , pp. 529-536
    • Lorimer, G.H.1    Badger, M.R.2    Andrews, T.J.3
  • 164
    • 0027639650 scopus 로고
    • Reduction of ribulose-bisphosphate carboxylase activase levels in tobacco (Nicotiana tabacum) by antisense RNA reduces ribulose bisphosphate carboxylase carbamylation and impairs photosynthesis
    • Mate CJ, Hudson GS, von Caemmerer S, Evans JR, Andrews TJ (1993) Reduction of ribulose-bisphosphate carboxylase activase levels in tobacco (Nicotiana tabacum) by antisense RNA reduces ribulose bisphosphate carboxylase carbamylation and impairs photosynthesis. Plant Physiol 102:1119-1128
    • (1993) Plant Physiol , vol.102 , pp. 1119-1128
    • Mate, C.J.1    Hudson, G.S.2    Von Caemmerer, S.3    Evans, J.R.4    Andrews, T.J.5
  • 165
    • 70449168712 scopus 로고
    • Study of association between the main nucleoprotein of green leaves and carboxydismutase
    • Mayaudon J (1957) Study of association between the main nucleoprotein of green leaves and carboxydismutase. Enzymologia 18:345-354
    • (1957) Enzymologia , vol.18 , pp. 345-354
    • Mayaudon, J.1
  • 167
    • 0019877105 scopus 로고
    • On the mechanism of effector-mediated activation of ribulose bisphosphate carboxylase/oxygenase
    • McCurry SD, Pierce J, Tolbert NE, Orme-Johnson WH (1981) On the mechanism of effector-mediated activation of ribulose bisphosphate carboxylase/oxygenase. J Biol Chem 256:6623-6628
    • (1981) J Biol Chem , vol.256 , pp. 6623-6628
    • McCurry, S.D.1    Pierce, J.2    Tolbert, N.E.3    Orme-Johnson, W.H.4
  • 169
    • 0019192754 scopus 로고
    • Chloroplast gene sequence for the large subunit of ribulose bisphosphatecarboxylase of maize
    • McIntosh L, Poulsen C, Bogorad L (1980) Chloroplast gene sequence for the large subunit of ribulose bisphosphatecarboxylase of maize. Nature 288:556-560
    • (1980) Nature , vol.288 , pp. 556-560
    • McIntosh, L.1    Poulsen, C.2    Bogorad, L.3
  • 170
    • 0040491415 scopus 로고
    • Amino-acid sequence of the small subunit of ribulose-1,5-bisphosphate carboxylase from spinach
    • Martin PG (1979) Amino-acid sequence of the small subunit of ribulose-1,5-bisphosphate carboxylase from spinach. Aust J Plant Physiol 6:401-408
    • (1979) Aust J Plant Physiol , vol.6 , pp. 401-408
    • Martin, P.G.1
  • 171
    • 0020670459 scopus 로고
    • Ribulose-1,5-bisphosphate carboxylase-oxygenase
    • Miziorko HM, Lorimer GH (1983) Ribulose-1,5-bisphosphate carboxylase-oxygenase. Annu Rev Biochem 52:507-535
    • (1983) Annu Rev Biochem , vol.52 , pp. 507-535
    • Miziorko, H.M.1    Lorimer, G.H.2
  • 172
    • 0027145918 scopus 로고
    • Distribution of 2-carboxyarabinitol among plants
    • Moore BD, Isidoro E, Seemann JR (1993) Distribution of 2-carboxyarabinitol among plants. Phytochem 34:703-707
    • (1993) Phytochem , vol.34 , pp. 703-707
    • Moore, B.D.1    Isidoro, E.2    Seemann, J.R.3
  • 174
    • 34548163888 scopus 로고
    • The path of carbon in photosynthesis. XXII. the identification of carboxy-ketopentitol diphosphates as product of photosynthesis
    • Moses V, Calvin M (1958) The path of carbon in photosynthesis. XXII. The identification of carboxy-ketopentitol diphosphates as product of photosynthesis. Proc Natl Acad Sci USA 44:260-277
    • (1958) Proc Natl Acad Sci USA , vol.44 , pp. 260-277
    • Moses, V.1    Calvin, M.2
  • 175
    • 0031424710 scopus 로고    scopus 로고
    • Kinetics of Rubisco activation as determined from gas-exchange measurements in antisense plants of Arabidopsis thaliana containing reduced levels of Rubisco activase
    • Mott KA, Snyder GW, Woodrow IE (1997) Kinetics of Rubisco activation as determined from gas-exchange measurements in antisense plants of Arabidopsis thaliana containing reduced levels of Rubisco activase. Aust J Plant Physiol 24:811-818
    • (1997) Aust J Plant Physiol , vol.24 , pp. 811-818
    • Mott, K.A.1    Snyder, G.W.2    Woodrow, I.E.3
  • 176
    • 0000760064 scopus 로고
    • The position of carbon-carbon bond cleavage in the ribulose diphosphate carboxydismutase reaction
    • Müllhofer G, Rose IA (1964) The position of carbon-carbon bond cleavage in the ribulose diphosphate carboxydismutase reaction. J Biol Chem 240:1341-1346
    • (1964) J Biol Chem , vol.240 , pp. 1341-1346
    • Müllhofer, G.1    Rose, I.A.2
  • 177
    • 84996367961 scopus 로고
    • Photochemical oxidants injury in rice plants. III. Effect of ozone on physiological activities in rice plants
    • Nakamura H, Saka H (1978) Photochemical oxidants injury in rice plants. III. Effect of ozone on physiological activities in rice plants. Jpn J Crop Sci 47:704-714
    • (1978) Jpn J Crop Sci , vol.47 , pp. 704-714
    • Nakamura, H.1    Saka, H.2
  • 178
    • 0021328927 scopus 로고
    • Nucleotide sequence of the ribulosebisphosphate carboxylase gene from Rhodospirillum rubrum
    • Nargang R, McIntosh L, Somerville CR (1984) Nucleotide sequence of the ribulosebisphosphate carboxylase gene from Rhodospirillum rubrum. Mol Gen Genet 193:220-224
    • (1984) Mol Gen Genet , vol.193 , pp. 220-224
    • Nargang, R.1    McIntosh, L.2    Somerville, C.R.3
  • 179
    • 0001107856 scopus 로고
    • Control of leaf photosynthesis rate by level of assimilate concentration in leaf-a review of the hypothesis
    • Neales TF, Incoll LD (1968) Control of leaf photosynthesis rate by level of assimilate concentration in leaf-a review of the hypothesis. Bot Rev 34:107-125
    • (1968) Bot Rev , vol.34 , pp. 107-125
    • Neales, T.F.1    Incoll, L.D.2
  • 180
    • 0017288199 scopus 로고
    • A mutant strain of Chlamydomonas reinhardi exhibiting altered ribulosebisphosphate carboxylase
    • Nelson PE, Surzycki SJ (1976) A mutant strain of Chlamydomonas reinhardi exhibiting altered ribulosebisphosphate carboxylase. Eur J Biochem 61:465-474
    • (1976) Eur J Biochem , vol.61 , pp. 465-474
    • Nelson, P.E.1    Surzycki, S.J.2
  • 181
    • 0041859262 scopus 로고    scopus 로고
    • Affixing the O to rubisco: Discovering the source of photorespiratory glycolate and its regulation
    • Ogren WL (2003) Affixing the O to rubisco: discovering the source of photorespiratory glycolate and its regulation. Photosynth Res 76:53-63
    • (2003) Photosynth Res , vol.76 , pp. 53-63
    • Ogren, W.L.1
  • 182
    • 0015246690 scopus 로고
    • Ribulose diphosphate carboxylase regulates soybean photorespiration
    • Ogren WL, Bowes G (1971) Ribulose diphosphate carboxylase regulates soybean photorespiration. Nature 230:159-160
    • (1971) Nature , vol.230 , pp. 159-160
    • Ogren, W.L.1    Bowes, G.2
  • 183
    • 0018360036 scopus 로고
    • Hydroxylamine stimulates carboxylase activity and inhibits oxygenase activity of cyanobacterial RuBP carboxylase/oxygenase
    • Okabe KI, Codd GA, Stewart WDP (1979) Hydroxylamine stimulates carboxylase activity and inhibits oxygenase activity of cyanobacterial RuBP carboxylase/oxygenase. Nature 279:525-527
    • (1979) Nature , vol.279 , pp. 525-527
    • Okabe, K.I.1    Codd, G.A.2    Stewart, W.D.P.3
  • 184
    • 9244232372 scopus 로고    scopus 로고
    • The rbcX gene product promotes the production and assembly of ribulose-1,5-bisphosphate carboxylase/oxygenase of Synechococcus sp. PCC7002 in Escherichia coli
    • Onizuka T, Endo S, Akiyama H, Kanai S, Hirano M, Yokota A, Tanaka S, Miyasaka H (2004) The rbcX gene product promotes the production and assembly of ribulose-1,5-bisphosphate carboxylase/oxygenase of Synechococcus sp. PCC7002 in Escherichia coli. Plant Cell Physiol 45:1390-1395
    • (2004) Plant Cell Physiol , vol.45 , pp. 1390-1395
    • Onizuka, T.1    Endo, S.2    Akiyama, H.3    Kanai, S.4    Hirano, M.5    Yokota, A.6    Tanaka, S.7    Miyasaka, H.8
  • 186
    • 0006047088 scopus 로고
    • Mesophyll resistance and carboxylase activity-comparison under water stress conditions
    • O'Toole JC,Crookson RK, Treharne KJ, Ozbun JL (1976) Mesophyll resistance and carboxylase activity-comparison under water stress conditions. Plant Physiol 57:465-468
    • (1976) Plant Physiol , vol.57 , pp. 465-468
    • O'Toole, J.C.1    Crookson, R.K.2    Treharne, K.J.3    Ozbun, J.L.4
  • 187
    • 0034714290 scopus 로고    scopus 로고
    • Activase region on chloroplast ribulose-1,5-bisphosphate carboxylase/oxygenase. Nonconservative substitution in the large subunit alters species specificity of protein interaction
    • Ott CM, Smith BD, Portis AR Jr, Spreitzer RJ (2000) Activase region on chloroplast ribulose-1,5-bisphosphate carboxylase/oxygenase. Nonconservative substitution in the large subunit alters species specificity of protein interaction. J Biol Chem 275:26241-26244
    • (2000) J Biol Chem , vol.275 , pp. 26241-26244
    • Ott, C.M.1    Smith, B.D.2    Portis Jr., A.R.3    Spreitzer, R.J.4
  • 189
    • 85010246733 scopus 로고
    • Carbon isotope fractionation during photosynthesis
    • Park R, Epstein S (1961) Carbon isotope fractionation during photosynthesis. Geochim Cosmochim Acta 21:110-126
    • (1961) Geochim Cosmochim Acta , vol.21 , pp. 110-126
    • Park, R.1    Epstein, S.2
  • 190
    • 0008697288 scopus 로고
    • Correlation of structure with function in Spinacea oleracea chloroplasts
    • Park RB, Pon NG (1961) Correlation of structure with function in Spinacea oleracea chloroplasts. J Mol Biol 3:1-10
    • (1961) J Mol Biol , vol.3 , pp. 1-10
    • Park, R.B.1    Pon, N.G.2
  • 191
    • 0021267172 scopus 로고
    • 2- ions on the reactions of ribulosebisphosphate carboxylase
    • 2- ions on the reactions of ribulosebisphosphate carboxylase. J Exp Bot 35:157-168
    • (1984) J Exp Bot , vol.35 , pp. 157-168
    • Parry, M.A.J.1    Gutteridge, S.2
  • 195
    • 33847030362 scopus 로고    scopus 로고
    • Prospects for increasing photosynthesis by overcoming the limitations of Rubisco
    • Parry MAJ, Madgwick PJ Carvahlo JFC, Andralojc PJ (2007) Prospects for increasing photosynthesis by overcoming the limitations of Rubisco. J Agric Sci 145:31-43
    • (2007) J Agric Sci , vol.145 , pp. 31-43
    • Parry, M.A.J.1    Madgwick, P.J.2    Carvahlo, J.F.C.3    Andralojc, P.J.4
  • 196
    • 0013925697 scopus 로고
    • Spinach ribulose diphosphate carboxylase. I. Purification and properties of the enzyme
    • Paulsen JM, Lane MD (1966) Spinach ribulose diphosphate carboxylase. I. Purification and properties of the enzyme. Biochemisty 5:2350-2357
    • (1966) Biochemisty , vol.5 , pp. 2350-2357
    • Paulsen, J.M.1    Lane, M.D.2
  • 197
    • 0017886089 scopus 로고
    • Inhibition of ribulose-1,5-bisphosphate carboxylase/oxygenase by ribulose-1,5-bisphosphate epimerization and degradation products
    • Paech C, Pierce J, McCurry SD, Tolbert NE (1978) Inhibition of ribulose-1,5-bisphosphate carboxylase/oxygenase by ribulose-1,5-bisphosphate epimerization and degradation products. Biochem Biophys Res Commun 83:1084-1092
    • (1978) Biochem Biophys Res Commun , vol.83 , pp. 1084-1092
    • Paech, C.1    Pierce, J.2    McCurry, S.D.3    Tolbert, N.E.4
  • 198
    • 0013491643 scopus 로고
    • How air pollutants induce disease
    • Academic Press New York
    • Pell EJ (1979) How air pollutants induce disease. In: Horsafll J, Cowling E (eds) Plant disease, vol 4. Academic Press, New York, pp 179-194
    • (1979) Plant Disease , vol.4 , pp. 179-194
    • Pell, E.J.1    Horsafll, J.2    Cowling, E.3
  • 199
    • 0001003044 scopus 로고
    • Ozone-induced reduction in quantity of ribulose-1,5-bisphosphate carboxylase in alfalfa foliage
    • Pell EJ, Pearson NS (1983) Ozone-induced reduction in quantity of ribulose-1,5-bisphosphate carboxylase in alfalfa foliage. Plant Physiol 73:185-187
    • (1983) Plant Physiol , vol.73 , pp. 185-187
    • Pell, E.J.1    Pearson, N.S.2
  • 200
    • 0000809275 scopus 로고
    • Nitrogen redistribution during grain growth in wheat (Triticum aestivum L.). II. Chloroplast senescence and the degradation of ribulose-1,5-bisphosphate carboxylase
    • Peoples MB, Beilharz VC, Waters SP, Simpson RJ, Dalling MJ (1980) Nitrogen redistribution during grain growth in wheat (Triticum aestivum L.). II. Chloroplast senescence and the degradation of ribulose-1,5-bisphosphate carboxylase. Planta 149:241-251
    • (1980) Planta , vol.149 , pp. 241-251
    • Peoples, M.B.1    Beilharz, V.C.2    Waters, S.P.3    Simpson, R.J.4    Dalling, M.J.5
  • 201
    • 0001748327 scopus 로고
    • Light limitation of photosynthesis and activation of ribulose bisphosphate carboxylase in wheat seedlings
    • Perchorowicz JT, Raynes DA, Jensen RG (1981) Light limitation of photosynthesis and activation of ribulose bisphosphate carboxylase in wheat seedlings. Proc Natl Acad Sci USA 78:2985-2989
    • (1981) Proc Natl Acad Sci USA , vol.78 , pp. 2985-2989
    • Perchorowicz, J.T.1    Raynes, D.A.2    Jensen, R.G.3
  • 202
    • 0000594713 scopus 로고
    • Loss of ribulose 1,5-diphosphate carboxylase and increase in proteolytic activity during senescence of detached primary barley leaves
    • Peterson LW, Huffaker RC (1975) Loss of ribulose 1,5-diphosphate carboxylase and increase in proteolytic activity during senescence of detached primary barley leaves. Plant Physiol 55:1009-1015
    • (1975) Plant Physiol , vol.55 , pp. 1009-1015
    • Peterson, L.W.1    Huffaker, R.C.2
  • 203
    • 0019316283 scopus 로고
    • Interaction of ribulosebisphosphate carboxylase/oxygenase with transition-state analogs
    • Pierce J, Tolbert NE, Barker R (1980) Interaction of ribulosebisphosphate carboxylase/oxygenase with transition-state analogs. Biochemistry 19:934-942
    • (1980) Biochemistry , vol.19 , pp. 934-942
    • Pierce, J.1    Tolbert, N.E.2    Barker, R.3
  • 204
    • 0024713252 scopus 로고
    • A cyanobacterial mutant requiring the expression of ribulose bisphosphate carboxylase from a photosynthetic anaerobe
    • Pierce J, Carlson TJ, Williams GK (1989) A cyanobacterial mutant requiring the expression of ribulose bisphosphate carboxylase from a photosynthetic anaerobe. Proc Natl Acad Sci USA 86:5753-5757
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 5753-5757
    • Pierce, J.1    Carlson, T.J.2    Williams, G.K.3
  • 205
    • 0027140545 scopus 로고
    • Differential involvement of the circadian clock in the expression of genes required for ribulose-1,5-bisphosphate carboxylase/oxygenase synthesis, assembly, and activation in Arabidopsis thaliana
    • Pilgrim ML, McClung CR (1993) Differential involvement of the circadian clock in the expression of genes required for ribulose-1,5-bisphosphate carboxylase/oxygenase synthesis, assembly, and activation in Arabidopsis thaliana. Plant Physiol 103:553-564
    • (1993) Plant Physiol , vol.103 , pp. 553-564
    • Pilgrim, M.L.1    McClung, C.R.2
  • 206
    • 0011184853 scopus 로고
    • Mechanism of the carboxydismutase reaction. I. the effect of preliminary incubation of substrates, metal ion, and enzyme on activity
    • Pon NG, Rabin BR, Calvin M (1963) Mechanism of the carboxydismutase reaction. I. The effect of preliminary incubation of substrates, metal ion, and enzyme on activity. Biochem Zeits 338:7-19
    • (1963) Biochem Zeits , vol.338 , pp. 7-19
    • Pon, N.G.1    Rabin, B.R.2    Calvin, M.3
  • 207
    • 0000384908 scopus 로고
    • Regulation of ribulose 1,5-bisphosphate carboxylase/oxygenase activity
    • Portis AR Jr (1992) Regulation of ribulose 1,5-bisphosphate carboxylase/oxygenase activity. Annu Rev Plant Phys Plant Mol Biol 43:415-437
    • (1992) Annu Rev Plant Phys Plant Mol Biol , vol.43 , pp. 415-437
    • Portis Jr., A.R.1
  • 208
    • 0037232721 scopus 로고    scopus 로고
    • Rubisco activase-Rubisco's catalytic chaperone
    • Portis AR Jr (2003) Rubisco activase-Rubisco's catalytic chaperone. Photosynth Res 75:11-27
    • (2003) Photosynth Res , vol.75 , pp. 11-27
    • Portis Jr., A.R.1
  • 209
    • 0036409694 scopus 로고    scopus 로고
    • The discovery of Rubisco activase-yet another story of serendipity
    • Portis AR Jr, Salvucci ME (2002) The discovery of Rubisco activase-yet another story of serendipity. Photosynth Res 73:257-264
    • (2002) Photosynth Res , vol.73 , pp. 257-264
    • Portis Jr., A.R.1    Salvucci, M.E.2
  • 213
    • 0012891918 scopus 로고
    • Mechanism of action of carboxydismutase
    • Rabin BR, Trown PW (1964) Mechanism of action of carboxydismutase. Nature 202:1290-1291
    • (1964) Nature , vol.202 , pp. 1290-1291
    • Rabin, B.R.1    Trown, P.W.2
  • 215
    • 34548185963 scopus 로고
    • Synthesis of carbohydrates from carbon dioxide and hydrogen in a cell-free system
    • Racker E (1955) Synthesis of carbohydrates from carbon dioxide and hydrogen in a cell-free system. Nature 175:249-251
    • (1955) Nature , vol.175 , pp. 249-251
    • Racker, E.1
  • 216
  • 217
    • 0026643280 scopus 로고
    • A hybrid ribulosebisphosphate carboxylase oxygenase enzyme exhibiting a substantial increase in substrate-specificity factor
    • Read BA, Tabita FR (1992) A hybrid ribulosebisphosphate carboxylase oxygenase enzyme exhibiting a substantial increase in substrate-specificity factor. Biochemistry 31:5553-5560
    • (1992) Biochemistry , vol.31 , pp. 5553-5560
    • Read, B.A.1    Tabita, F.R.2
  • 218
    • 84989012164 scopus 로고
    • Changes in ethylene and polyamines in relation to mRNA levels of the large and small subunits of ribulose bisphosphate carboxylase/oxygenase in ozone-stressed potato foliage
    • Reddy G, Arteca RN, Dai Y-R, Flores HE, Negm FB, Pell EJ (1993) Changes in ethylene and polyamines in relation to mRNA levels of the large and small subunits of ribulose bisphosphate carboxylase/oxygenase in ozone-stressed potato foliage. Plant Cell Environ 16:819-826
    • (1993) Plant Cell Environ , vol.16 , pp. 819-826
    • Reddy, G.1    Arteca, R.N.2    Dai, Y.-R.3    Flores, H.E.4    Negm, F.B.5    Pell, E.J.6
  • 219
    • 0002571441 scopus 로고
    • Inorganic carbon fluxes and photosynthesis in cyanobacteria-a quantitative model
    • Martinus, Nijhoff Dordrecht, The Netherlands
    • Reinhold L, Zviman M, Kaplan A (1987) Inorganic carbon fluxes and photosynthesis in cyanobacteria-a quantitative model. In: Biggins J (eds) Progress in photosynthesis, vol IV. Martinus, Nijhoff, Dordrecht, The Netherlands, pp 6.289-6.296
    • (1987) Progress in Photosynthesis , vol.4 , pp. 6289-6296
    • Reinhold, L.1    Zviman, M.2    Kaplan, A.3    Biggins, J.4
  • 220
    • 0002797404 scopus 로고
    • Evolutionary analysis of plant DNA sequences
    • Ritland K, Clegg MT (1987) Evolutionary analysis of plant DNA sequences. Am Nat 130:S74-S100
    • (1987) Am Nat , vol.130
    • Ritland, K.1    Clegg, M.T.2
  • 221
    • 0001509985 scopus 로고
    • Release of the nocturnal inhibitor, carboxyarabinitol-1-phosphate, from ribulose bisphoshate carboxylase/oxygenase by Rubisco activase
    • Robinson SP, Portis AR Jr (1988) Release of the nocturnal inhibitor, carboxyarabinitol-1-phosphate, from ribulose bisphoshate carboxylase/oxygenase by Rubisco activase. FEBS Lett 233:413-416
    • (1988) FEBS Lett , vol.233 , pp. 413-416
    • Robinson, S.P.1    Portis Jr., A.R.2
  • 222
    • 0024485948 scopus 로고
    • Adenosine triphosphate hydrolysis by purified Rubisco activase
    • Robinson SP, Portis AR Jr (1989a) Adenosine triphosphate hydrolysis by purified Rubisco activase. Arch Biochem Biophys 268:93-99
    • (1989) Arch Biochem Biophys , vol.268 , pp. 93-99
    • Robinson, S.P.1    Portis Jr., A.R.2
  • 223
    • 0000174323 scopus 로고
    • Ribulose-1,5-bisphosphate carboxylase/oxygenase activase protein prevents the in vitro decline in activity of ribulose-1,5-bisphosphate carboxylase/oxygenase
    • Robinson SP, Portis AR Jr (1989b) Ribulose-1,5-bisphosphate carboxylase/oxygenase activase protein prevents the in vitro decline in activity of ribulose-1,5-bisphosphate carboxylase/oxygenase. Plant Physiol 88:1008-1014
    • (1989) Plant Physiol , vol.88 , pp. 1008-1014
    • Robinson, S.P.1    Portis Jr., A.R.2
  • 224
    • 0024291358 scopus 로고
    • Nuclear-organelle interactions: Nuclear antisense gene inhibits ribulose bisphosphate carboxylase enzyme levels in transformed tobacco plants
    • Rodermel SR, Abbott MS, Bogorad L (1988) Nuclear-organelle interactions: nuclear antisense gene inhibits ribulose bisphosphate carboxylase enzyme levels in transformed tobacco plants. Cell 55:673-681
    • (1988) Cell , vol.55 , pp. 673-681
    • Rodermel, S.R.1    Abbott, M.S.2    Bogorad, L.3
  • 225
    • 0029935151 scopus 로고    scopus 로고
    • A mechanism for intergenomic integration-abundance of ribulose bisphosphate carboxylase small-subunit protein influences the translation of the large-subunit mRNA
    • Rodermel SR, Haley J, Jiang CZ, Tsai CH, Bogorad L (1996) A mechanism for intergenomic integration-abundance of ribulose bisphosphate carboxylase small-subunit protein influences the translation of the large-subunit mRNA. Proc Natl Acad Sci USA 93:3881-3885
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 3881-3885
    • Rodermel, S.R.1    Haley, J.2    Jiang, C.Z.3    Tsai, C.H.4    Bogorad, L.5
  • 226
    • 0014214772 scopus 로고
    • Nonidentical subunits of ribulose diphosphate carboxylase
    • Rutner AC, Lane MD (1967) Nonidentical subunits of ribulose diphosphate carboxylase. Biochem Biophys Res Commun 28:531-537
    • (1967) Biochem Biophys Res Commun , vol.28 , pp. 531-537
    • Rutner, A.C.1    Lane, M.D.2
  • 227
    • 0036009361 scopus 로고    scopus 로고
    • 4 plants and some implications for photosynthetic performance at high and low temperature
    • 4 plants and some implications for photosynthetic performance at high and low temperature. J Expt Bot 53:609-620
    • (2002) J Expt Bot , vol.53 , pp. 609-620
    • Sage, R.F.1
  • 230
    • 0000116732 scopus 로고
    • Purification and properties of 2-carboxy-d-arabinitol 1-phosphatase
    • Salvucci ME, Holbrook GP (1989) Purification and properties of 2-carboxy-d-arabinitol 1-phosphatase. Plant Physiol 90:679-685
    • (1989) Plant Physiol , vol.90 , pp. 679-685
    • Salvucci, M.E.1    Holbrook, G.P.2
  • 231
    • 0030047366 scopus 로고    scopus 로고
    • The mechanism of Rubisco activase: Insights from studies of the properties and structure of the enzyme
    • Salvucci ME, Ogren WL (1996) The mechanism of Rubisco activase: insights from studies of the properties and structure of the enzyme. Photosynth Res 47:1-11
    • (1996) Photosynth Res , vol.47 , pp. 1-11
    • Salvucci, M.E.1    Ogren, W.L.2
  • 232
    • 34250112628 scopus 로고
    • A soluble chloroplast protein catalyzes ribulosebisphosphate carboxylase/oxygenase activation in vivo
    • Salvucci ME, Portis AR Jr, Ogren WL (1985) A soluble chloroplast protein catalyzes ribulosebisphosphate carboxylase/oxygenase activation in vivo. Photosynth Res 7:193-201
    • (1985) Photosynth Res , vol.7 , pp. 193-201
    • Salvucci, M.E.1    Portis Jr., A.R.2    Ogren, W.L.3
  • 233
    • 10944273663 scopus 로고    scopus 로고
    • Mechanism for deactivation of Rubisco under moderate heat stress
    • Salvucci ME, Crafts-Brandner SJ (2004) Mechanism for deactivation of Rubisco under moderate heat stress. Physiol Plant 122:513-519
    • (2004) Physiol Plant , vol.122 , pp. 513-519
    • Salvucci, M.E.1    Crafts-Brandner, S.J.2
  • 234
    • 0019876692 scopus 로고
    • Light-induced increase of mRNA activity coding for the small subunit of ribulose-1,5-bisphosphate carboxylase
    • Sasaki Y Ishiye M, Sakihama T, Kamikubo T (1981) Light-induced increase of mRNA activity coding for the small subunit of ribulose-1,5-bisphosphate carboxylase. J Biol Chem 256:2315-2320
    • (1981) J Biol Chem , vol.256 , pp. 2315-2320
    • Sasaki Ishiye, Y.M.1    Sakihama, T.2    Kamikubo, T.3
  • 235
    • 0020789449 scopus 로고
    • Phytochrome-mediated regulation of two mRNAs, encoded by nuclei and chloroplasts of ribulose-1,5-bisphosphate carboxylase/oxgenase
    • Sasaki Y, Sakihama T, Kamikubo T, Shinozaki K (1983) Phytochrome-mediated regulation of two mRNAs, encoded by nuclei and chloroplasts of ribulose-1,5-bisphosphate carboxylase/oxgenase. Eur J Biochem 133:617-620
    • (1983) Eur J Biochem , vol.133 , pp. 617-620
    • Sasaki, Y.1    Sakihama, T.2    Kamikubo, T.3    Shinozaki, K.4
  • 236
    • 33847157932 scopus 로고    scopus 로고
    • Archaeal type III RuBisCOs function in a pathway for AMP metabolism
    • Sato T, Atomi H, Imanaka T (2007) Archaeal type III RuBisCOs function in a pathway for AMP metabolism. Science 315:1003-1006
    • (2007) Science , vol.315 , pp. 1003-1006
    • Sato, T.1    Atomi, H.2    Imanaka, T.3
  • 237
    • 0020491931 scopus 로고
    • Ribulose-1,5-bisphosphate carboxylase: Enzyme-catalysed appearance of solvent tritium at carbon 2 of ribulose 1,5-bisphosphate reisolated after partial reaction
    • Saver B, Knowles JR (1982) Ribulose-1,5-bisphosphate carboxylase: enzyme-catalysed appearance of solvent tritium at carbon 2 of ribulose 1,5-bisphosphate reisolated after partial reaction. Biochemistry 21:5398-5403
    • (1982) Biochemistry , vol.21 , pp. 5398-5403
    • Saver, B.1    Knowles, J.R.2
  • 238
    • 0020478953 scopus 로고
    • The stereochemical course of ribulosebisphosphate carboxylase. Reductive trapping of the 6-carbon reaction-intermediate
    • Schloss JV, Lorimer GH (1982) The stereochemical course of ribulosebisphosphate carboxylase. Reductive trapping of the 6-carbon reaction-intermediate. J Biol Chem 257:4691-4694
    • (1982) J Biol Chem , vol.257 , pp. 4691-4694
    • Schloss, J.V.1    Lorimer, G.H.2
  • 239
    • 18844480151 scopus 로고
    • Rapid degradation of unassembled ribulose 1,5-bisphosphate carboxylase small subunits in chloroplasts
    • Schmidt GW, Mishkind ML (1983) Rapid degradation of unassembled ribulose 1,5-bisphosphate carboxylase small subunits in chloroplasts. Proc Natl Acad Sci USA 80:2632-2636
    • (1983) Proc Natl Acad Sci USA , vol.80 , pp. 2632-2636
    • Schmidt, G.W.1    Mishkind, M.L.2
  • 240
    • 34548159502 scopus 로고
    • Effect of hydroxylamine derivatives on photorespiration in the tobacco aurea mutant Nicotiana tabacum Su/su
    • Schmid GH, Bader KP, Radunz A, van Assche CJ, Reinier N, Courtiade B (1987) Effect of hydroxylamine derivatives on photorespiration in the tobacco aurea mutant Nicotiana tabacum Su/su. Z Naturforsch 42c:965-969
    • (1987) Z Naturforsch , vol.42 , pp. 965-969
    • Schmid, G.H.1    Bader, K.P.2    Radunz, A.3    Van Assche, C.J.4    Reinier, N.5    Courtiade, B.6
  • 241
    • 0000505390 scopus 로고
    • Three-dimensional structure of ribulose-1,5-bisphosphate carboxylase/oxygenase from Rhodospirillum rubrum at 2.9 Å resolution
    • Schneider G, Lindqvist Y, Brändén C-I, Lorimer GH (1986) Three-dimensional structure of ribulose-1,5-bisphosphate carboxylase/oxygenase from Rhodospirillum rubrum at 2.9 Å resolution. EMBO J 5:3409-3415
    • (1986) EMBO J , vol.5 , pp. 3409-3415
    • Schneider, G.1    Lindqvist, Y.2    Brändén, C.-I.3    Lorimer, G.H.4
  • 242
    • 33749238362 scopus 로고    scopus 로고
    • High temperature enhances inhibitor production but reduces fallover in tobacco Rubisco
    • Schrader SM, Kane HJ, Sharkey TD, von Caemmerer S (2006) High temperature enhances inhibitor production but reduces fallover in tobacco Rubisco. Funct Plant Biol 33:921-929
    • (2006) Funct Plant Biol , vol.33 , pp. 921-929
    • Schrader, S.M.1    Kane, H.J.2    Sharkey, T.D.3    Von Caemmerer, S.4
  • 243
    • 10644266747 scopus 로고    scopus 로고
    • Rubisco without the Calvin cycle improves the carbon efficiency of developing green seeds
    • Schwender J, Goffman F, Ohlrogge JB, Shachar-Hill Y (2004) Rubisco without the Calvin cycle improves the carbon efficiency of developing green seeds. Nature 432:779-782
    • (2004) Nature , vol.432 , pp. 779-782
    • Schwender, J.1    Goffman, F.2    Ohlrogge, J.B.3    Shachar-Hill, Y.4
  • 244
    • 0000204785 scopus 로고
    • Variations in the specific activity of ribulose-1,5-bisphosphate carboxylase between species utilizing differing photosynthetic pathways
    • Seemann JR, Badger MR, Berry JA (1984) Variations in the specific activity of ribulose-1,5-bisphosphate carboxylase between species utilizing differing photosynthetic pathways. Plant Physiol 74:791-794
    • (1984) Plant Physiol , vol.74 , pp. 791-794
    • Seemann, J.R.1    Badger, M.R.2    Berry, J.A.3
  • 245
    • 0022404626 scopus 로고
    • Regulation of ribulose bisphosphate carboxylase activity in vivo by a light-modulated inhibitor of catalysis
    • Seemann JR, Berry JA, Freas SM, Krump MA (1985) Regulation of ribulose bisphosphate carboxylase activity in vivo by a light-modulated inhibitor of catalysis. Proc Natl Acad Sci USA 82:8024-8028
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 8024-8028
    • Seemann, J.R.1    Berry, J.A.2    Freas, S.M.3    Krump, M.A.4
  • 246
    • 0000933669 scopus 로고
    • Binding of a phosphorylated inhibitor to ribulose bisphosphate carboxylase/oxygenase at night
    • Servaites JC (1985) Binding of a phosphorylated inhibitor to ribulose bisphosphate carboxylase/oxygenase at night. Plant Physiol 78:839-843
    • (1985) Plant Physiol , vol.78 , pp. 839-843
    • Servaites, J.C.1
  • 247
    • 0002599889 scopus 로고
    • Species variation in the predawn inhibition of ribulose-1,5-bisphosphate carboxylase oxygenase
    • Servaites JC, Parry MAJ, Gutteridge S, Keys AJ (1986) Species variation in the predawn inhibition of ribulose-1,5-bisphosphate carboxylase oxygenase. Plant Physiol 82:1161-1163
    • (1986) Plant Physiol , vol.82 , pp. 1161-1163
    • Servaites, J.C.1    Parry, M.A.J.2    Gutteridge, S.3    Keys, A.J.4
  • 249
    • 0015816557 scopus 로고
    • Functional organelles in prokaryotes: Polyhedral inclusions (carboxysomes) of Thiobacillus neapolitanus
    • Shively JM, Ball F, Brown RE, Saunders RE (1973) Functional organelles in prokaryotes: polyhedral inclusions (carboxysomes) of Thiobacillus neapolitanus. Science 182:584-586
    • (1973) Science , vol.182 , pp. 584-586
    • Shively, J.M.1    Ball, F.2    Brown, R.E.3    Saunders, R.E.4
  • 250
    • 0015844770 scopus 로고
    • Chemical and enzymatic evidence for the participation of a 2-carboxy-3-ketoribitiol-1,5-diphosphate intermediate in the carboxylation of ribulose 1,5-diphosphate
    • Siegel MI, Lane MD (1973) Chemical and enzymatic evidence for the participation of a 2-carboxy-3-ketoribitiol-1,5-diphosphate intermediate in the carboxylation of ribulose 1,5-diphosphate. J Biol Chem 248:5486-5498
    • (1973) J Biol Chem , vol.248 , pp. 5486-5498
    • Siegel, M.I.1    Lane, M.D.2
  • 252
    • 0027789898 scopus 로고
    • Atmospheric carbon dioxide and the ocean
    • Siegenthaler U, Sarmiento JL (1993) Atmospheric carbon dioxide and the ocean. Nature 365:119-125
    • (1993) Nature , vol.365 , pp. 119-125
    • Siegenthaler, U.1    Sarmiento, J.L.2
  • 254
    • 0019755032 scopus 로고
    • Light stimulated accumulation of transcripts of nuclear and chloroplast genes for ribulosebisphosphate carboxylase
    • Smith SM, Ellis RJ (1981) Light stimulated accumulation of transcripts of nuclear and chloroplast genes for ribulosebisphosphate carboxylase. J Mol Appl Genet 1:127-137
    • (1981) J Mol Appl Genet , vol.1 , pp. 127-137
    • Smith, S.M.1    Ellis, R.J.2
  • 255
    • 0001596719 scopus 로고
    • A mutant of Arabidopsis-thaliana which lacks activation of ruBP carboxylase in vivo
    • Somerville CR, Portis AR Jr, Ogren WL (1982) A mutant of Arabidopsis-thaliana which lacks activation of RuBP carboxylase in vivo. Plant Physiol 70:381-387
    • (1982) Plant Physiol , vol.70 , pp. 381-387
    • Somerville, C.R.1    Portis Jr., A.R.2    Ogren, W.L.3
  • 256
    • 0021328271 scopus 로고
    • Cloning and expression of the Rhodospirillum rubrum ribulosebisphosphate carboxylase gene in E. coli
    • Somerville CR, Somerville SC (1984) Cloning and expression of the Rhodospirillum rubrum ribulosebisphosphate carboxylase gene in E. coli. Mol Gen Genet 193:214-219
    • (1984) Mol Gen Genet , vol.193 , pp. 214-219
    • Somerville, C.R.1    Somerville, S.C.2
  • 257
    • 0001297575 scopus 로고
    • Genetic dissection of Rubisco structure and function
    • Spreitzer RJ (1993) Genetic dissection of Rubisco structure and function. Annu Rev Plant Physiol Plant Mol Biol 44:411-434
    • (1993) Annu Rev Plant Physiol Plant Mol Biol , vol.44 , pp. 411-434
    • Spreitzer, R.J.1
  • 258
    • 0032817398 scopus 로고    scopus 로고
    • Questions about the complexity of chloroplast ribulose bisphosphate carboxylase/oxygenase
    • Spreitzer RJ (1999) Questions about the complexity of chloroplast ribulose bisphosphate carboxylase/oxygenase. Photosynth Res 60:29-42
    • (1999) Photosynth Res , vol.60 , pp. 29-42
    • Spreitzer, R.J.1
  • 259
    • 0018976083 scopus 로고
    • Non-mendelian mutation affecting ribulose-1,5-bisphosphate carboxylase structure and activity
    • Spreitzer RJ, Mets LJ (1980) Non-mendelian mutation affecting ribulose-1,5-bisphosphate carboxylase structure and activity. Nature 285:114-115
    • (1980) Nature , vol.285 , pp. 114-115
    • Spreitzer, R.J.1    Mets, L.J.2
  • 260
    • 0037001967 scopus 로고    scopus 로고
    • Rubisco: Structure, regulatory interactions, and possibilities for a better enzyme
    • Spreizter RJ, Salvucci ME (2002) Rubisco: structure, regulatory interactions, and possibilities for a better enzyme. Annu Rev Plant Biol 53:449-475
    • (2002) Annu Rev Plant Biol , vol.53 , pp. 449-475
    • Spreizter, R.J.1    Salvucci, M.E.2
  • 261
    • 28044454726 scopus 로고    scopus 로고
    • Phylogenetic engineering at an interface between large and small subunits imparts land-plant kinetic properties to algal Rubisco
    • Spreitzer RJ, Peddi SR, Satagopan S (2005) Phylogenetic engineering at an interface between large and small subunits imparts land-plant kinetic properties to algal Rubisco. Proc Natl Acad Sci USA 102:17225-17230
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 17225-17230
    • Spreitzer, R.J.1    Peddi, S.R.2    Satagopan, S.3
  • 263
    • 0014139344 scopus 로고
    • Structure of chloroplast proteins I. Subunit structure of wheat Fraction-1 protein
    • Sugiyama T, Akazawa T (1967) Structure of chloroplast proteins I. Subunit structure of wheat Fraction-1 protein. J Biochem 62:474-482
    • (1967) J Biochem , vol.62 , pp. 474-482
    • Sugiyama, T.1    Akazawa, T.2
  • 264
    • 0014940689 scopus 로고
    • Subunit structure of spinach leaf ribulose 1,5-diphosphate carboxylase
    • Sugiyama T, Akazawa T (1970) Subunit structure of spinach leaf ribulose 1,5-diphosphate carboxylase. Biochemistry 9:4499-4504
    • (1970) Biochemistry , vol.9 , pp. 4499-4504
    • Sugiyama, T.1    Akazawa, T.2
  • 265
  • 266
    • 0032840522 scopus 로고    scopus 로고
    • Microbial ribulose 1,5-bisphosphate carboxylase/oxygenase: A different perspective
    • Tabita FR (1999) Microbial ribulose 1,5-bisphosphate carboxylase/ oxygenase: a different perspective. Photosynth Res 60:1-28
    • (1999) Photosynth Res , vol.60 , pp. 1-28
    • Tabita, F.R.1
  • 267
    • 3042723377 scopus 로고    scopus 로고
    • Research on carbon dioxide fixation in photosynthetic microorganisms (1971-present)
    • Tabita FR (2004) Research on carbon dioxide fixation in photosynthetic microorganisms (1971-present). Photosyn Res 80:315-332
    • (2004) Photosyn Res , vol.80 , pp. 315-332
    • Tabita, F.R.1
  • 268
    • 0016137330 scopus 로고
    • D-Ribulose 1,5-diphosphate carboxylase from Rhodospirillum rubrum I. Levels, purification, and effects of metallic ions
    • Tabita FR, McFadden BA (1974a) d-Ribulose 1,5-diphosphate carboxylase from Rhodospirillum rubrum I. Levels, purification, and effects of metallic ions. J Biol Chem 249:3453-3458
    • (1974) J Biol Chem , vol.249 , pp. 3453-3458
    • Tabita, F.R.1    McFadden, B.A.2
  • 269
    • 0016165638 scopus 로고
    • D-Ribulose 1,5-diphosphate carboxylase from Rhodospirillum rubrum. II. Quarternary structure, composition, catalytic, and immunological properties
    • Tabita FR, McFadden BA (1974b) d-Ribulose 1,5-diphosphate carboxylase from Rhodospirillum rubrum. II. Quarternary structure, composition, catalytic, and immunological properties. J Biol Chem 249:3459-3464
    • (1974) J Biol Chem , vol.249 , pp. 3459-3464
    • Tabita, F.R.1    McFadden, B.A.2
  • 270
    • 0022401680 scopus 로고
    • Expression and assembly of active cyanobacterial ribulose-1,5- bisphosphate carboxylase/oxygenase in Escherichia coli containing stoichiometric amounts of large and small subunits
    • Tabita FR, Small CL (1985) Expression and assembly of active cyanobacterial ribulose-1,5-bisphosphate carboxylase/oxygenase in Escherichia coli containing stoichiometric amounts of large and small subunits. Proc Natl Acad Sci USA 82:6100-6103
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 6100-6103
    • Tabita, F.R.1    Small, C.L.2
  • 271
    • 0011176008 scopus 로고
    • Effect of oxygen on the dark reaction of photosynthesis
    • Tamiya H, Huzisige H (1949) Effect of oxygen on the dark reaction of photosynthesis. Acta Phytochim 15:83-104
    • (1949) Acta Phytochim , vol.15 , pp. 83-104
    • Tamiya, H.1    Huzisige, H.2
  • 272
    • 33646583168 scopus 로고    scopus 로고
    • Despite slow catalysis and confused substrate specificity, all ribulose bisphosphate carboxylases may be nearly perfectly optimized
    • Tcherkez GGB, Farquhar GD, Andrews TJ (2006) Despite slow catalysis and confused substrate specificity, all ribulose bisphosphate carboxylases may be nearly perfectly optimized. Proc Natl Acad Sci USA 103:7246-7251
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 7246-7251
    • Tcherkez, G.G.B.1    Farquhar, G.D.2    Andrews, T.J.3
  • 273
    • 0013797332 scopus 로고
    • Isolation and partial characterization of Fraction I protein from spinach-beet chloroplasts
    • Thornber JP, Ridley SM, Bailey JL (1965) Isolation and partial characterization of Fraction I protein from spinach-beet chloroplasts. Biochem J 96:29-31
    • (1965) Biochem J , vol.96 , pp. 29-31
    • Thornber, J.P.1    Ridley, S.M.2    Bailey, J.L.3
  • 274
    • 0018090063 scopus 로고
    • Light regulation of specific mRNA species in Lemna gibba L. G-3
    • Tobin EM (1978) Light regulation of specific mRNA species in Lemna gibba L. G-3. Proc Natl Acad Sci USA 75:4749-4753
    • (1978) Proc Natl Acad Sci USA , vol.75 , pp. 4749-4753
    • Tobin, E.M.1
  • 275
    • 0004857491 scopus 로고
    • Phytochrome-mediated regulation of messenger RNAs for the small subunit of ribulose 1,5-bisphosphate carboxylase and the light-harvesting chlorophyll a/b-protein in Lemna gibba
    • Tobin EM (1981) Phytochrome-mediated regulation of messenger RNAs for the small subunit of ribulose 1,5-bisphosphate carboxylase and the light-harvesting chlorophyll a/b-protein in Lemna gibba. Plant Mol Biol 1:35-51
    • (1981) Plant Mol Biol , vol.1 , pp. 35-51
    • Tobin, E.M.1
  • 276
    • 3042820240 scopus 로고
    • An improved method for the isolation of carboxydismutase. Probable identity with Fraction 1 protein and the protein moiety of protochlorophyll holochrome
    • Trown PW (1965) An improved method for the isolation of carboxydismutase. Probable identity with Fraction 1 protein and the protein moiety of protochlorophyll holochrome. Biochemistry 4:908-918
    • (1965) Biochemistry , vol.4 , pp. 908-918
    • Trown, P.W.1
  • 277
    • 34548185964 scopus 로고
    • Chemical control of photorespiration: Steady-state kinetic and conformational changes of ribulose-1,5-bisphosphate carboxylase/oygenase obtained with O-p-nitrophenylhydroxylamine
    • Van Assche CJ, Reinier N, Courtiade B, Chancel A, Huber S (1987) Chemical control of photorespiration: steady-state kinetic and conformational changes of ribulose-1,5-bisphosphate carboxylase/oygenase obtained with O-p-nitrophenylhydroxylamine. Z Naturforsch 42c:837-844
    • (1987) Z Naturforsch , vol.42 , pp. 837-844
    • Van Assche, C.J.1    Reinier, N.2    Courtiade, B.3    Chancel, A.4    Huber, S.5
  • 278
    • 0021967344 scopus 로고
    • Targeting of a foreign protein to chloroplast by fusion to the transit peptide from the small subunit of ribulose 1,5-bisphosphate carboxylase
    • Van den Broeck G, Timko MP, Kausch AP, Cashmore AR, Montau MV, Herrera-Estrella L (1985) Targeting of a foreign protein to chloroplast by fusion to the transit peptide from the small subunit of ribulose 1,5-bisphosphate carboxylase. Nature 313:358-363
    • (1985) Nature , vol.313 , pp. 358-363
    • Van Den Broeck, G.1    Timko, M.P.2    Kausch, A.P.3    Cashmore, A.R.4    Montau, M.V.5    Herrera-Estrella, L.6
  • 279
    • 0028312420 scopus 로고
    • The kinetics of ribulose-1,5-bisphosphate carboxylase/oxygenase in vivo inferred from measurements of photosynthesis in leaves of transgenic tobacco
    • von Caemmerer S, Evans JR, Hudson GS, Andrews TJ (1994) The kinetics of ribulose-1,5-bisphosphate carboxylase/oxygenase in vivo inferred from measurements of photosynthesis in leaves of transgenic tobacco. Planta 195:88-97
    • (1994) Planta , vol.195 , pp. 88-97
    • Von Caemmerer, S.1    Evans, J.R.2    Hudson, G.S.3    Andrews, T.J.4
  • 280
    • 0001653031 scopus 로고
    • 2 on the ribulose bisphosphate carboxylase activity and ribulose bisphosphate level of soybean leaves
    • 2 on the ribulose bisphosphate carboxylase activity and ribulose bisphosphate level of soybean leaves. Plant Physiol 73:729-734
    • (1983) Plant Physiol , vol.73 , pp. 729-734
    • Vu, C.V.1    Allen Jr., L.H.2    Bowes, G.3
  • 281
    • 0026311257 scopus 로고
    • Expression dynamics of the tomato rbcS gene family during development
    • Wanner LA, Gruissem W (1991) Expression dynamics of the tomato rbcS gene family during development. Plant Cell 3:1289-1303
    • (1991) Plant Cell , vol.3 , pp. 1289-1303
    • Wanner, L.A.1    Gruissem, W.2
  • 282
    • 0009164379 scopus 로고
    • Über die Geschwindigkeit der photochemischen Kohlensä urezersetzung in lebenden Zellen. II
    • Warburg O (1920) Über die Geschwindigkeit der photochemischen Kohlensäurezersetzung in lebenden Zellen. II. Biochem Z 103:188-217
    • (1920) Biochem Z , vol.103 , pp. 188-217
    • Warburg, O.1
  • 283
    • 0014401314 scopus 로고
    • Rate-limiting processes in photosynthesis at saturating light intensities
    • Waring PF, Khalifa MM, Treharne KJ (1968) Rate-limiting processes in photosynthesis at saturating light intensities. Nature 220:453-457
    • (1968) Nature , vol.220 , pp. 453-457
    • Waring, P.F.1    Khalifa, M.M.2    Treharne, K.J.3
  • 284
    • 0033027258 scopus 로고    scopus 로고
    • Unusual ribulose 1,5-bisphosphate carboxylase/oxygenase of anoxic Archaea
    • Watson GFM, Yu J-P, Tabita FR (1999) Unusual ribulose 1,5-bisphosphate carboxylase/oxygenase of anoxic Archaea. J Bacteriol 181:1569-1575
    • (1999) J Bacteriol , vol.181 , pp. 1569-1575
    • Watson, G.F.M.1    Yu, J.-P.2    Tabita, F.R.3
  • 285
    • 0002473289 scopus 로고
    • Reversible heat-inactivation of the Calvin cycle: A possible mechanism of the temperature regulation of photosynthesis
    • Weis E (1981a) Reversible heat-inactivation of the Calvin cycle: a possible mechanism of the temperature regulation of photosynthesis. Planta 151:33-39
    • (1981) Planta , vol.151 , pp. 33-39
    • Weis, E.1
  • 286
    • 0000687223 scopus 로고
    • The temperature sensitivity of dark-inactivation and light-activation of the ribulose-1,5-bisphosphate carboxylase in spinach chloroplasts
    • Weis E (1981b) The temperature sensitivity of dark-inactivation and light-activation of the ribulose-1,5-bisphosphate carboxylase in spinach chloroplasts. FEBS Lett 129:197-200
    • (1981) FEBS Lett , vol.129 , pp. 197-200
    • Weis, E.1
  • 288
    • 0001329772 scopus 로고
    • The enzymatic formation of phosphoglyceric acid from ribulose diphosphate and carbon dioxide
    • Weissbach A, Horecker BL, Hurwitz J (1956) The enzymatic formation of phosphoglyceric acid from ribulose diphosphate and carbon dioxide. J Biol Chem 218:795-810
    • (1956) J Biol Chem , vol.218 , pp. 795-810
    • Weissbach, A.1    Horecker, B.L.2    Hurwitz, J.3
  • 289
    • 0023953674 scopus 로고
    • Structure and expression of spinach leaf cDNA encoding ribulosebisphosphate carboxylase/oxygenase activase
    • Werneke JM, Zielinski RE, Ogren WL (1988) Structure and expression of spinach leaf cDNA encoding ribulosebisphosphate carboxylase/oxygenase activase. Proc Natl Acad Sci USA 85:787-791
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 787-791
    • Werneke, J.M.1    Zielinski, R.E.2    Ogren, W.L.3
  • 290
    • 0024707622 scopus 로고
    • Alternative mRNA splicing generates the two ribulosebisphosphate carboxylase/oxygenase activase polypeptides in spinach and Arabidopsis
    • Werneke JM, Chatfield JM, Ogren WL (1989) Alternative mRNA splicing generates the two ribulosebisphosphate carboxylase/oxygenase activase polypeptides in spinach and Arabidopsis. Plant Cell 1:815-825
    • (1989) Plant Cell , vol.1 , pp. 815-825
    • Werneke, J.M.1    Chatfield, J.M.2    Ogren, W.L.3
  • 291
    • 0035807976 scopus 로고    scopus 로고
    • Plastome-encoded bacterial ribulose-1,5-bisphosphate carboxylase/ oxygenase (RubisCO) supports photosynthesis and growth in tobacco
    • Whitney SM, Andrews TJ (2001a) Plastome-encoded bacterial ribulose-1,5-bisphosphate carboxylase/oxygenase (RubisCO) supports photosynthesis and growth in tobacco. Proc Natl Acad Sci USA 98:14738-14743
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 14738-14743
    • Whitney, S.M.1    Andrews, T.J.2
  • 292
    • 0035101397 scopus 로고    scopus 로고
    • The gene for the ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) small subunit relocated to the plastid genome of tobacco directs the synthesis of small subunits that assemble into Rubisco
    • Whitney SM, Andrews TJ (2001b) The gene for the ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) small subunit relocated to the plastid genome of tobacco directs the synthesis of small subunits that assemble into Rubisco. Plant Cell 13:193-205
    • (2001) Plant Cell , vol.13 , pp. 193-205
    • Whitney, S.M.1    Andrews, T.J.2
  • 293
    • 0036415213 scopus 로고    scopus 로고
    • Along the trail from Faction I protein to Rubisco (ribulose bisphosphate carboxylase-oxygenase)
    • Wildman SG (2002) Along the trail from Faction I protein to Rubisco (ribulose bisphosphate carboxylase-oxygenase). Photosynth Res 73:243-250
    • (2002) Photosynth Res , vol.73 , pp. 243-250
    • Wildman, S.G.1
  • 294
    • 84872625210 scopus 로고
    • The proteins of green leaves. I. Isolation, enzymatic properties, and auxin content of spinach cytoplasmic proteins
    • Wildman SG, Bonner J (1947) The proteins of green leaves. I. Isolation, enzymatic properties, and auxin content of spinach cytoplasmic proteins. Arch Biochem Biophys 14:381-413
    • (1947) Arch Biochem Biophys , vol.14 , pp. 381-413
    • Wildman, S.G.1    Bonner, J.2
  • 296
    • 0014664127 scopus 로고
    • Ribulose disphosphate carboxylase I. a factor involved in light activation of the enzyme
    • Wildner GF, Criddle RS (1969) Ribulose disphosphate carboxylase I. A factor involved in light activation of the enzyme. Biochem Biophys Res Commun 37:952-960
    • (1969) Biochem Biophys Res Commun , vol.37 , pp. 952-960
    • Wildner, G.F.1    Criddle, R.S.2
  • 297
    • 0017286367 scopus 로고
    • Specific inhibition of the oxygenase activity of ribulose-1,5- bisphosphate carboxylase.
    • Wildner GF, Henkel J (1976) Specific inhibition of the oxygenase activity of ribulose-1,5-bisphosphate carboxylase. Biochem Biophys Res Commun 69:268-275
    • (1976) Biochem Biophys Res Commun , vol.69 , pp. 268-275
    • Wildner, G.F.1    Henkel, J.2
  • 298
    • 34548148734 scopus 로고
    • Preservation of RuBP carboxylase without oxygenase activity during anaerobiosis
    • Wildner GF, Henkel J (1980) Preservation of RuBP carboxylase without oxygenase activity during anaerobiosis. FEBS Lett 113:81-84
    • (1980) FEBS Lett , vol.113 , pp. 81-84
    • Wildner, G.F.1    Henkel, J.2
  • 300
    • 3242655621 scopus 로고    scopus 로고
    • Metabolic channeling in plants
    • Winkel BSJ (2004) Metabolic channeling in plants. Annu Rev Plant Biol 55:85-107
    • (2004) Annu Rev Plant Biol , vol.55 , pp. 85-107
    • Winkel, B.S.J.1
  • 301
    • 0008450317 scopus 로고
    • Activity and quantity of ribulose bisphosphate carboxylase- and phosphoenolpyruvate carboxylase-protein in two Crassulacean acid metabolism plants in relation to leaf age, nitrogen nutrition, and point in time during a day/night cycle
    • Winter K, Foster JG, Schmitt MR, Edwards GE (1982) Activity and quantity of ribulose bisphosphate carboxylase- and phosphoenolpyruvate carboxylase-protein in two Crassulacean acid metabolism plants in relation to leaf age, nitrogen nutrition, and point in time during a day/night cycle. Planta 154:309-317
    • (1982) Planta , vol.154 , pp. 309-317
    • Winter, K.1    Foster, J.G.2    Schmitt, M.R.3    Edwards, G.E.4
  • 302
    • 0014940380 scopus 로고
    • The interaction of metal ions with ribulose 1,5-diphosphate carboxylase from spinach
    • Wishnick M, Lane MD, Scrutton MC (1970) The interaction of metal ions with ribulose 1,5-diphosphate carboxylase from spinach. J Biol Chem 245:4939-4947
    • (1970) J Biol Chem , vol.245 , pp. 4939-4947
    • Wishnick, M.1    Lane, M.D.2    Scrutton, M.C.3
  • 303
    • 0038059584 scopus 로고
    • Ribulose bisphosphate carboxylase and proteolytic activity in wheat leaves from anthesis through senescence
    • Wittenbach VA (1979) Ribulose bisphosphate carboxylase and proteolytic activity in wheat leaves from anthesis through senescence. Plant Physiol 64:884-887
    • (1979) Plant Physiol , vol.64 , pp. 884-887
    • Wittenbach, V.A.1
  • 304
    • 0002979975 scopus 로고
    • Changes in photosynthesis, ribulose bisphosphate carboxylase, proteolytic activity, and ultrastructure of soybean leaves during senescence
    • Wittenbach VA, Ackerson RC, Giaquinta RT, Hebert RR (1980) Changes in photosynthesis, ribulose bisphosphate carboxylase, proteolytic activity, and ultrastructure of soybean leaves during senescence. Crop Sci 20:225-231
    • (1980) Crop Sci , vol.20 , pp. 225-231
    • Wittenbach, V.A.1    Ackerson, R.C.2    Giaquinta, R.T.3    Hebert, R.R.4
  • 306
    • 0000056033 scopus 로고
    • Rate limitation of non-steady-state photosynthesis by ribulose-1,5-bisphosphate carboxylase in spinach
    • Woodrow IE, Mott KA (1989) Rate limitation of non-steady-state photosynthesis by ribulose-1,5-bisphosphate carboxylase in spinach. Aust J Plant Physiol 16:487-500
    • (1989) Aust J Plant Physiol , vol.16 , pp. 487-500
    • Woodrow, I.E.1    Mott, K.A.2
  • 307
    • 0000365258 scopus 로고
    • Variations in the kinetic properties of ribulose-1,5-bisphosphate carboxylases among plants
    • Yeoh HH, Badger MR, Watson L (1981) Variations in the kinetic properties of ribulose-1,5-bisphosphate carboxylases among plants. Plant Physiol 67:1151-1155
    • (1981) Plant Physiol , vol.67 , pp. 1151-1155
    • Yeoh, H.H.1    Badger, M.R.2    Watson, L.3
  • 308
    • 0033529948 scopus 로고    scopus 로고
    • Mechanism of light regulation of Rubisco: A specific role for the larger Rubisco activase isoform involving reductive activation by thioredoxin-f
    • Zhang N, Portis AR Jr (1999) Mechanism of light regulation of Rubisco: a specific role for the larger Rubisco activase isoform involving reductive activation by thioredoxin-f. Proc Natl Acad Sci USA 96:9438-9443
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 9438-9443
    • Zhang, N.1    Portis Jr., A.R.2
  • 309
    • 0037022664 scopus 로고    scopus 로고
    • Light modulation of Rubisco in Arabidopsis requires a capacity for redox regulation of the larger Rubisco activase isoform
    • Zhang N, Kallis RP, Ewy RG, Portis AR Jr (2002) Light modulation of Rubisco in Arabidopsis requires a capacity for redox regulation of the larger Rubisco activase isoform. Proc Natl Acad Sci USA 99:3330-3334
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 3330-3334
    • Zhang, N.1    Kallis, R.P.2    Ewy, R.G.3    Portis Jr., A.R.4
  • 310
    • 1242344163 scopus 로고    scopus 로고
    • 3 crop plants with foreign Rubisco increase productivity? a computational analysis extrapolating from kinetic properties to canopy photosynthesis
    • 3 crop plants with foreign Rubisco increase productivity? A computational analysis extrapolating from kinetic properties to canopy photosynthesis. Plant Cell Environ 27:155-165
    • (2004) Plant Cell Environ , vol.27 , pp. 155-165
    • Zhu, X.-G.1    Portis Jr., A.R.2    Long, S.P.3
  • 311
    • 1442355726 scopus 로고
    • - On the activity of ribulose-1,5-diphosphate carboxylase in isolated spinach chloroplasts
    • - on the activity of ribulose-1,5-diphosphate carboxylase in isolated spinach chloroplasts. Planta 103:155-163
    • (1972) Planta , vol.103 , pp. 155-163
    • Zeigler, I.1
  • 312
    • 12044257739 scopus 로고
    • Xylulose 1,5-bisphosphate synthesized by ribulose 1,5-bisphosphate carboxylase/oxygenase during catalysis binds to decarbamylated enzyme
    • Zhu G, Jensen RG (1991a) Xylulose 1,5-bisphosphate synthesized by ribulose 1,5-bisphosphate carboxylase/oxygenase during catalysis binds to decarbamylated enzyme. Plant Physiol 97:1348-1353
    • (1991) Plant Physiol , vol.97 , pp. 1348-1353
    • Zhu, G.1    Jensen, R.G.2
  • 313
    • 12044257526 scopus 로고
    • Fallover of ribulose 1,5-bisphosphate carboxylase/oxygenase activity. Decarbamylation of catalytic sites depends on pH
    • Zhu G, Jensen RG (1991b) Fallover of ribulose 1,5-bisphosphate carboxylase/oxygenase activity. Decarbamylation of catalytic sites depends on pH. Plant Physiol 97:1354-1358
    • (1991) Plant Physiol , vol.97 , pp. 1354-1358
    • Zhu, G.1    Jensen, R.G.2


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