메뉴 건너뛰기




Volumn 132, Issue 4, 2003, Pages 2126-2134

An anaplerotic role for mitochondrial carbonic anhydrase in Chlamydomonas reinhardtii

Author keywords

[No Author keywords available]

Indexed keywords

CATALYST ACTIVITY; ENZYME KINETICS; GENETIC ENGINEERING; GROWTH KINETICS; PHOTOSYNTHESIS;

EID: 0043011570     PISSN: 00320889     EISSN: None     Source Type: Journal    
DOI: 10.1104/pp.103.023424     Document Type: Article
Times cited : (94)

References (76)
  • 1
    • 0031785343 scopus 로고    scopus 로고
    • 2 in cells and chloroplasts from the microalgae Chlamydomonas reinhardtii and Dunaliella tertiolecta
    • 2 in cells and chloroplasts from the microalgae Chlamydomonas reinhardtii and Dunaliella tertiolecta. Plant Physiol 116: 193-201
    • (1998) Plant Physiol , vol.116 , pp. 193-201
    • Amoroso, G.1    Sültemeyer, D.2    Thyssen, C.3    Fock, H.P.4
  • 4
    • 0041411082 scopus 로고    scopus 로고
    • 2 concentrating mechanisms and their regulation
    • 2 concentrating mechanisms and their regulation. Funct Plant Biol 29: 333-347
    • (2002) Funct Plant Biol , vol.29 , pp. 333-347
    • Beardall, J.1    Giordano, M.2
  • 5
    • 0001935796 scopus 로고
    • Pathways and mechanisms of respiration in microalgae
    • Beardall J, Raven JA (1990). Pathways and mechanisms of respiration in microalgae. Mar Microb Food Webs 4: 7-30
    • (1990) Mar Microb Food Webs , vol.4 , pp. 7-30
    • Beardall, J.1    Raven, J.A.2
  • 6
    • 0000481192 scopus 로고
    • Effects of nitrogen limitation on uptake of inorganic carbon and specific activity of ribulose-1,5-bisphosphate carboxylase/oxygenase in green microalgae
    • Beardall J, Roberts S, Millhouse J (1991) Effects of nitrogen limitation on uptake of inorganic carbon and specific activity of ribulose-1, 5-bisphosphate carboxylase/oxygenase in green microalgae. Can J Bot 69: 1146-1150
    • (1991) Can J Bot , vol.69 , pp. 1146-1150
    • Beardall, J.1    Roberts, S.2    Millhouse, J.3
  • 8
    • 0041911531 scopus 로고
    • Variability of mitochondrial population in Chlamydomonas reinhardtii
    • Blank R, Arnold CG (1980) Variability of mitochondrial population in Chlamydomonas reinhardtii. Protoplasma 104: 187-191
    • (1980) Protoplasma , vol.104 , pp. 187-191
    • Blank, R.1    Arnold, C.G.2
  • 9
    • 0000267963 scopus 로고
    • Variety of mitochondrial shapes, sizes and volumes in Chlamydomonas reinhardtii
    • Blank R, Hauptmann E, Arnold CG (1980) Variety of mitochondrial shapes, sizes and volumes in Chlamydomonas reinhardtii. Planta 50: 236-241
    • (1980) Planta , vol.50 , pp. 236-241
    • Blank, R.1    Hauptmann, E.2    Arnold, C.G.3
  • 10
    • 0035957145 scopus 로고    scopus 로고
    • Futile membrane ion cycle cycling: A new cellular hypothesis to explain ammonium toxicity in plants
    • Britto DT, Siddiqui MY, Glass ADM, Kronzucker HJ (2001) Futile membrane ion cycle cycling: a new cellular hypothesis to explain ammonium toxicity in plants. Proc Natl Acad Sci USA 98: 4255-4258
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 4255-4258
    • Britto, D.T.1    Siddiqui, M.Y.2    Glass, A.D.M.3    Kronzucker, H.J.4
  • 12
    • 0000756509 scopus 로고    scopus 로고
    • Phosphoenolpyruvate carboxylase: A ubiquitous, highly regulated enzyme in plants
    • Chollet R, Vidal J, O'Leary MH (1996) Phosphoenolpyruvate carboxylase: a ubiquitous, highly regulated enzyme in plants. Annu Rev Plant Physiol Plant Mol Biol 47: 273-298
    • (1996) Annu Rev Plant Physiol Plant Mol Biol , vol.47 , pp. 273-298
    • Chollet, R.1    Vidal, J.2    O'Leary, M.H.3
  • 13
    • 0028913220 scopus 로고
    • Behavior of mitochondria in synchronized cells of Chlamydomonas reinhardtii (Chlorophyta)
    • Ehana T, Osafune T, Hase E (1995) Behavior of mitochondria in synchronized cells of Chlamydomonas reinhardtii (Chlorophyta). J Cell Sci 108: 499-507
    • (1995) J Cell Sci , vol.108 , pp. 499-507
    • Ehana, T.1    Osafune, T.2    Hase, E.3
  • 16
    • 0040737617 scopus 로고    scopus 로고
    • p53 and tumor necrosis factor alpha regulate the expression of a mitochondrial chloride channel protein
    • Fernandez-Sala E, Sagan M, Cheng C, Yusha SH, Weinberg WC (1999) p53 and tumor necrosis factor alpha regulate the expression of a mitochondrial chloride channel protein. J Biol Chem 274: 36488-36498
    • (1999) J Biol Chem , vol.274 , pp. 36488-36498
    • Fernandez-Sala, E.1    Sagan, M.2    Cheng, C.3    Yusha, S.H.4    Weinberg, W.C.5
  • 17
    • 0022160007 scopus 로고
    • Electrogenic transport of bicarbonate ions through the internal mitochondrial membrane induced by cytosplasmic glycopeptide
    • Gainutdinov MK, Konov VV, Luchenko MV, Turakulov IK (1985) Electrogenic transport of bicarbonate ions through the internal mitochondrial membrane induced by cytosplasmic glycopeptide. Biul Ecksp Biol Med 100: 561-563
    • (1985) Biul Ecksp Biol Med , vol.100 , pp. 561-563
    • Gainutdinov, M.K.1    Konov, V.V.2    Luchenko, M.V.3    Turakulov, I.K.4
  • 18
  • 19
    • 0002260231 scopus 로고    scopus 로고
    • Mineral nutrition in photolithotrophs: Cellular mechanisms controlling growth in terrestrial and aquatic habitats
    • Giordano M, Hell R (2001) Mineral nutrition in photolithotrophs: cellular mechanisms controlling growth in terrestrial and aquatic habitats. Recent Res Dev Plant Physiol 2: 95-123
    • (2001) Recent Res Dev Plant Physiol , vol.2 , pp. 95-123
    • Giordano, M.1    Hell, R.2
  • 20
    • 0033794301 scopus 로고    scopus 로고
    • Strategies for the allocation of resources under sulphur limitation in the green alga Dunaliella salina
    • Giordano M, Pezzoni V, Hell R (2000) Strategies for the allocation of resources under sulphur limitation in the green alga Dunaliella salina. Plant Physiol 124: 857-864
    • (2000) Plant Physiol , vol.124 , pp. 857-864
    • Giordano, M.1    Pezzoni, V.2    Hell, R.3
  • 23
    • 0017407487 scopus 로고
    • Enzymes concerned with β-carboxylation in marine phytoplankton: Purification and properties of PEPck
    • Holdsworth ES, Bruck J (1977) Enzymes concerned with β-carboxylation in marine phytoplankton: purification and properties of PEPck. Arch Biochem Biophys 182: 87-94
    • (1977) Arch Biochem Biophys , vol.182 , pp. 87-94
    • Holdsworth, E.S.1    Bruck, J.2
  • 24
    • 0036010675 scopus 로고    scopus 로고
    • Biochemical and molecular inhibition of plastidial carbonic anhydrase reduces the incorporation of acetate into lipids in cotton embryos and tobacco cell suspensions and leaves
    • Huang CV, Chapman KD (2002) Biochemical and molecular inhibition of plastidial carbonic anhydrase reduces the incorporation of acetate into lipids in cotton embryos and tobacco cell suspensions and leaves. Plant Physiol 128: 1417-1427
    • (2002) Plant Physiol , vol.128 , pp. 1417-1427
    • Huang, C.V.1    Chapman, K.D.2
  • 25
    • 0033709984 scopus 로고    scopus 로고
    • Regulation of pyc1 encoding pyruvate carboxylase isozyme I by nitrogen sources in Saccharomyces cerevisiae
    • Huet C, Menendez J, Gancedo C, Francois JM (2000). Regulation of pyc1 encoding pyruvate carboxylase isozyme I by nitrogen sources in Saccharomyces cerevisiae. Eur J Biochem 267: 6817-6823
    • (2000) Eur J Biochem , vol.267 , pp. 6817-6823
    • Huet, C.1    Menendez, J.2    Gancedo, C.3    Francois, J.M.4
  • 26
    • 0000088919 scopus 로고
    • Some approaches to the study of the role of metals in the metabolism of microorganisms
    • Hutner SH, Provasoli L, Schatz A, Haskins CP (1950). Some approaches to the study of the role of metals in the metabolism of microorganisms. Proc Am Philos Soc 94: 152-170
    • (1950) Proc Am Philos Soc , vol.94 , pp. 152-170
    • Hutner, S.H.1    Provasoli, L.2    Schatz, A.3    Haskins, C.P.4
  • 27
    • 0029816220 scopus 로고    scopus 로고
    • 2+ and ATP in rat submandibular acinar cells
    • 2+ and ATP in rat submandibular acinar cells. J Membr Biol 153: 147-159
    • (1996) J Membr Biol , vol.153 , pp. 147-159
    • Ishikawa, T.1
  • 30
    • 0014425378 scopus 로고
    • Protein turnover and macromolecular synthesis during growth and gametic differentiation in Chlamydomonas reinhardtii
    • Jones RF, Kates JR, Keller SJ (1968) Protein turnover and macromolecular synthesis during growth and gametic differentiation in Chlamydomonas reinhardtii. Biochim Biophys Acta 157: 589-598
    • (1968) Biochim Biophys Acta , vol.157 , pp. 589-598
    • Jones, R.F.1    Kates, J.R.2    Keller, S.J.3
  • 32
    • 0014214149 scopus 로고
    • Periodic increases in enzyme activity in synchronized cultures of Chlamydomonas reinhardtii
    • Kates JR, Jones RF (1967) Periodic increases in enzyme activity in synchronized cultures of Chlamydomonas reinhardtii. Biochim Biophys Acta 145: 153-158
    • (1967) Biochim Biophys Acta , vol.145 , pp. 153-158
    • Kates, J.R.1    Jones, R.F.2
  • 34
    • 0021933402 scopus 로고
    • 2 fixation by Klebsiella pneumoniae
    • 2 fixation by Klebsiella pneumoniae. FEBS Lett 187: 237-239
    • (1985) FEBS Lett , vol.187 , pp. 237-239
    • Kleiner, D.1
  • 35
    • 0021796811 scopus 로고
    • Bacterial ammonium transporters
    • Kleiner D (1985b) Bacterial ammonium transporters. FEMS Microbiol Rev 32: 87-100
    • (1985) FEMS Microbiol Rev , vol.32 , pp. 87-100
    • Kleiner, D.1
  • 38
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 277: 680-685
    • (1970) Nature , vol.277 , pp. 680-685
    • Laemmli, U.K.1
  • 39
    • 0035209841 scopus 로고    scopus 로고
    • Characterization of a cadmium-inducible isoform of pyruvate carboxylase from Caenorhabditis elegans
    • Liao VHC, Freedman JH (2001) Characterization of a cadmium-inducible isoform of pyruvate carboxylase from Caenorhabditis elegans. DNA Sequence 12: 137-145
    • (2001) DNA Sequence , vol.12 , pp. 137-145
    • Liao, V.H.C.1    Freedman, J.H.2
  • 40
    • 0037131246 scopus 로고    scopus 로고
    • Beta-cell adaptation to insulin resistance: Increased pyruvate carboxylase and malate-pyruvate shuttle activity in islets of nondiabetic Zicker fatty rats
    • Liu YQ, Jetton TL, Leahy JL (2002) Beta-cell adaptation to insulin resistance: increased pyruvate carboxylase and malate-pyruvate shuttle activity in islets of nondiabetic Zicker fatty rats. J Biol Chem 277: 39163-39168
    • (2002) J Biol Chem , vol.277 , pp. 39163-39168
    • Liu, Y.Q.1    Jetton, T.L.2    Leahy, J.L.3
  • 41
    • 3543049099 scopus 로고
    • Utilization modes of inorganic carbon for photosynthesis in various species of Chlorella
    • Miyachi S, Tsuuki M, Avramova T (1983) Utilization modes of inorganic carbon for photosynthesis in various species of Chlorella. Plant Cell Physiol 29: 441-445
    • (1983) Plant Cell Physiol , vol.29 , pp. 441-445
    • Miyachi, S.1    Tsuuki, M.2    Avramova, T.3
  • 44
    • 0036787636 scopus 로고    scopus 로고
    • Role of phosphoenolpyruvate carboxylase in anaplerosis in the green microalga Dunaliella salina cultured under different nitrogen regimes
    • Norici A, Dalsass A, Giordano M (2002) Role of phosphoenolpyruvate carboxylase in anaplerosis in the green microalga Dunaliella salina cultured under different nitrogen regimes. Physiol Plant 116: 186-191
    • (2002) Physiol Plant , vol.116 , pp. 186-191
    • Norici, A.1    Dalsass, A.2    Giordano, M.3
  • 46
    • 0042412603 scopus 로고
    • Enzymes of nitrogen assimilation in maize roots
    • Oaks A, Stulen J, Jones MJ, Boosel IL (1980) Enzymes of nitrogen assimilation in maize roots. Planta 148: 186-191
    • (1980) Planta , vol.148 , pp. 186-191
    • Oaks, A.1    Stulen, J.2    Jones, M.J.3    Boosel, I.L.4
  • 47
    • 84989715067 scopus 로고
    • The role of extracellular carbonic anhydrase for accumulation of inorganic carbon in the green alga Chlamydomonas reinhardtii: A comparison between wild-type and cell-wall-less mutant cells
    • Palmqvist K, Ramazanov Z, Samuelsson G (1990). The role of extracellular carbonic anhydrase for accumulation of inorganic carbon in the green alga Chlamydomonas reinhardtii: a comparison between wild-type and cell-wall-less mutant cells. Physiol Plant 80: 267-276
    • (1990) Physiol Plant , vol.80 , pp. 267-276
    • Palmqvist, K.1    Ramazanov, Z.2    Samuelsson, G.3
  • 48
    • 0028232830 scopus 로고
    • Bicarbonate conductance and pH regulatory capacity of cystic-fibrosis transmembrane conductance regulation
    • Paulsen JH, Fischer H, Illek B, Machen TE (1994) Bicarbonate conductance and pH regulatory capacity of cystic-fibrosis transmembrane conductance regulation. Proc Natl Acad Sci USA 91: 5340-5344
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 5340-5344
    • Paulsen, J.H.1    Fischer, H.2    Illek, B.3    Machen, T.E.4
  • 49
    • 0017613512 scopus 로고
    • Simplification of the protein assay method of Lowry which is more generally applicable
    • Peterson GL (1977) Simplification of the protein assay method of Lowry which is more generally applicable. Arch Biochem Biophys 83: 246-356
    • (1977) Arch Biochem Biophys , vol.83 , pp. 246-356
    • Peterson, G.L.1
  • 50
    • 0019248377 scopus 로고
    • Nutrient transport in micro-algae
    • Raven JA (1980) Nutrient transport in micro-algae. Adv Microbiol Physiol 21: 47-226
    • (1980) Adv Microbiol Physiol , vol.21 , pp. 47-226
    • Raven, J.A.1
  • 52
    • 0029139126 scopus 로고
    • Photosynthetic and non-photosynthetic roles of carbonic anhydrase in algae and cyanobacteria
    • Raven JA (1995) Photosynthetic and non-photosynthetic roles of carbonic anhydrase in algae and cyanobacteria. Phycologia 34: 93-101
    • (1995) Phycologia , vol.34 , pp. 93-101
    • Raven, J.A.1
  • 53
    • 0031043931 scopus 로고    scopus 로고
    • 2 concentrating mechanisms: A direct role for thylakoid lumen acidification?
    • 2 concentrating mechanisms: a direct role for thylakoid lumen acidification? Plant Cell Environ 20: 147-154
    • (1997) Plant Cell Environ , vol.20 , pp. 147-154
    • Raven, J.A.1
  • 54
    • 0035134950 scopus 로고    scopus 로고
    • 2-grown cells of Chlamydomonas reinhardtii
    • 2-grown cells of Chlamydomonas reinhardtii. Plant Cell Environ 24: 261-265
    • (2001) Plant Cell Environ , vol.24 , pp. 261-265
    • Raven, J.A.1
  • 55
    • 84987031634 scopus 로고
    • The influence of N metabolism and organic acid synthesis on the natural abundance of isotopes of carbon in plants
    • Raven JA, Farquhar GD (1990) The influence of N metabolism and organic acid synthesis on the natural abundance of isotopes of carbon in plants. New Phytol 116: 505-529
    • (1990) New Phytol , vol.116 , pp. 505-529
    • Raven, J.A.1    Farquhar, G.D.2
  • 56
    • 0028011184 scopus 로고
    • Requirement for carbonic anhydrase activity in processes other than photosynthetic inorganic carbon assimilation
    • Raven JA, Newman JR (1994) Requirement for carbonic anhydrase activity in processes other than photosynthetic inorganic carbon assimilation. Plant Cell Environ 20: 123-130
    • (1994) Plant Cell Environ , vol.20 , pp. 123-130
    • Raven, J.A.1    Newman, J.R.2
  • 58
    • 0015490471 scopus 로고
    • Die architektur und organisation der Chlamydomonas-zelle: Ergebnisse der elektronmikroskoscopie yon serienschnitten und der darous resulterenden dreidimensional rekonstruktion
    • Schötz F, Bathelt H, Arnold C-G, Schimmer O (1972) Die Architektur und Organisation der Chlamydomonas-Zelle: Ergebnisse der Elektronmikroskoscopie yon Serienschnitten und der darous resulterenden dreidimensional Rekonstruktion. Protoplasma 75: 229-254
    • (1972) Protoplasma , vol.75 , pp. 229-254
    • Schötz, F.1    Bathelt, H.2    Arnold, C.-G.3    Schimmer, O.4
  • 59
    • 0017664451 scopus 로고
    • Permeability of the mitochondrial membrane to bicarbonate ions
    • Selwyn MJ, Walker HA (1977) Permeability of the mitochondrial membrane to bicarbonate ions. Biochem J 166: 137-139
    • (1977) Biochem J , vol.166 , pp. 137-139
    • Selwyn, M.J.1    Walker, H.A.2
  • 60
    • 0020923710 scopus 로고
    • Mitochondrial bicarbonate carrier: A site of regulation of renal substrate metabolism by acid-base changes
    • Simpson DP (1983) Mitochondrial bicarbonate carrier: a site of regulation of renal substrate metabolism by acid-base changes. Trans Assoc Am Physicians 96: 918-924
    • (1983) Trans Assoc Am Physicians , vol.96 , pp. 918-924
    • Simpson, D.P.1
  • 61
    • 0001445055 scopus 로고    scopus 로고
    • 2 acquisition: Acclimation to changing carbon availability
    • J-D Rochaix, M Goldschmidt-Clermont, S Merchant, eds. Kluwer Academic Publishers, Dordrecht, The Netherlands
    • 2 acquisition: acclimation to changing carbon availability In J-D Rochaix, M Goldschmidt-Clermont, S Merchant, eds, The Molecular Biology of Chloroplasts and Mitochondria in Chlamydomonas Kluwer Academic Publishers, Dordrecht, The Netherlands, pp 529-547
    • (1998) The Molecular Biology of Chloroplasts and Mitochondria in Chlamydomonas , pp. 529-547
    • Spalding, M.H.1
  • 62
    • 0000281646 scopus 로고
    • A model for carbon dioxide assimilation in Chlamydomonas reinhardtii
    • Spalding MH, Portis AR Jr (1985) A model for carbon dioxide assimilation in Chlamydomonas reinhardtii. Planta 164: 308-320
    • (1985) Planta , vol.164 , pp. 308-320
    • Spalding, M.H.1    Portis A.R., Jr.2
  • 63
    • 0024550918 scopus 로고
    • Reversed-phase high-performance liquid-chromatography separation of dimethylaminoazobenzene sulfonylaminoazobenzene and dimethylaminoazobenzene thiohydantoin amino-acid derivatives for aminoacid analysis and microsequencing studies at the picomole level
    • Stocchi V, Piccoli G, Magnani M, Palma F, Biagiarelli B, Cucchiarini L (1989) Reversed-phase high-performance liquid-chromatography separation of dimethylaminoazobenzene sulfonylaminoazobenzene and dimethylaminoazobenzene thiohydantoin amino-acid derivatives for aminoacid analysis and microsequencing studies at the picomole level. Anal Biochem 178: 107-117
    • (1989) Anal Biochem , vol.178 , pp. 107-117
    • Stocchi, V.1    Piccoli, G.2    Magnani, M.3    Palma, F.4    Biagiarelli, B.5    Cucchiarini, L.6
  • 64
    • 0002257867 scopus 로고
    • Mitotic replication of deoxyribonucleic acid in Chlamydomonas reinhardtii
    • Sueoka N (1960) Mitotic replication of deoxyribonucleic acid in Chlamydomonas reinhardtii. Proc Natl Acad Sci USA 46: 83-91
    • (1960) Proc Natl Acad Sci USA , vol.46 , pp. 83-91
    • Sueoka, N.1
  • 65
    • 0040804577 scopus 로고    scopus 로고
    • Carbonic anhydrase in eukaryotic algae: Characterization, regulation and possible function during photosynthesis
    • Sültemeyer D (1998) Carbonic anhydrase in eukaryotic algae: characterization, regulation and possible function during photosynthesis. Can J Bot 76: 962-972
    • (1998) Can J Bot , vol.76 , pp. 962-972
    • Sültemeyer, D.1
  • 66
    • 0030452158 scopus 로고    scopus 로고
    • 2 in suspensions of carbonic anhydrase-loaded plasma membrane vesicles
    • 2 in suspensions of carbonic anhydrase-loaded plasma membrane vesicles. Planta 200: 258-268
    • (1996) Planta , vol.200 , pp. 258-268
    • Sültemeyer, D.1    Rinast, K.-A.2
  • 67
    • 0035819504 scopus 로고    scopus 로고
    • Model of the carbon concentrating mechanism in chloroplast of eukaryotic algae
    • Thoms S, Pahlow M, Wolf-Gladrow DA (2001) Model of the carbon concentrating mechanism in chloroplast of eukaryotic algae. J Theor Biol 208: 201-260
    • (2001) J Theor Biol , vol.208 , pp. 201-260
    • Thoms, S.1    Pahlow, M.2    Wolf-Gladrow, D.A.3
  • 68
    • 0035126785 scopus 로고    scopus 로고
    • Identification and localization of a thylakoid-bound carbonic anhydrase from the green algae Tetraedron minimum (Chlorophyta) and Chlamydomonas noctigama (Chlorophyta)
    • van Hunnik E, Livne A, Pogenberg V, Spijkerman E, van den Ende H, Garcia EM, Sültemeyer D, de Leeuw JW (2001) Identification and localization of a thylakoid-bound carbonic anhydrase from the green algae Tetraedron minimum (Chlorophyta) and Chlamydomonas noctigama (Chlorophyta). Planta 212: 454-459
    • (2001) Planta , vol.212 , pp. 454-459
    • Van Hunnik, E.1    Livne, A.2    Pogenberg, V.3    Spijkerman, E.4    Van Den Ende, H.5    Garcia, E.M.6    Sültemeyer, D.7    De Leeuw, J.W.8
  • 69
    • 0000309161 scopus 로고
    • + assimilation rate and in vivo phosphoenolpyruvate carboxylase activity. Regulation of anaplerotic carbon flow in the green alga Selenastrum minutum
    • + assimilation rate and in vivo phosphoenolpyruvate carboxylase activity. Regulation of anaplerotic carbon flow in the green alga Selenastrum minutum. Plant Physiol 94: 284-290
    • (1990) Plant Physiol , vol.94 , pp. 284-290
    • Vanlerberghe, G.C.1    Schuller, K.A.2    Smith, R.G.3    Feil, R.4    Plaxton, W.C.5    Turpin, D.H.6
  • 70
    • 0030660457 scopus 로고    scopus 로고
    • Carbon dioxide and light regulation of promoters controlling the expression of mitochondrial carbonic anhydrase in Chlamydomonas reinhardtii
    • Villand P, Eriksson M, Samuelsson G (1997) Carbon dioxide and light regulation of promoters controlling the expression of mitochondrial carbonic anhydrase in Chlamydomonas reinhardtii. Biochem J 327: 51-57
    • (1997) Biochem J , vol.327 , pp. 51-57
    • Villand, P.1    Eriksson, M.2    Samuelsson, G.3
  • 71
    • 0034942688 scopus 로고    scopus 로고
    • A new chloroplast envelope carbonic anhydrase activity is induced during acclimation to low carbon dioxide concentrations in Chlamydomonas reinhardtii
    • Villarejo A, Rolland N, Martinez F, Sültemeyer DF (2001) A new chloroplast envelope carbonic anhydrase activity is induced during acclimation to low carbon dioxide concentrations in Chlamydomonas reinhardtii. Planta 213: 286-295
    • (2001) Planta , vol.213 , pp. 286-295
    • Villarejo, A.1    Rolland, N.2    Martinez, F.3    Sültemeyer, D.F.4
  • 72
    • 0037090474 scopus 로고    scopus 로고
    • A photosystem II-associated carbonic anhydrase regulates the efficiency of photosynthetic oxygen evolution
    • Villarejo A, Shutora T, Moshkin O, Forssén M, Klimov VV, Samuelsson G (2002) A photosystem II-associated carbonic anhydrase regulates the efficiency of photosynthetic oxygen evolution. EMBO J 21: 1930-1938
    • (2002) EMBO J , vol.21 , pp. 1930-1938
    • Villarejo, A.1    Shutora, T.2    Moshkin, O.3    Forssén, M.4    Klimov, V.V.5    Samuelsson, G.6
  • 73
    • 0038063439 scopus 로고
    • Cytochrome and alternative pathway respiration during transient ammonium assimilation by N-limited Chlamydomonas reinhardtii
    • Weger HG, Chadderton AR, Lin M, Guy RD, Turpin DH (1990) Cytochrome and alternative pathway respiration during transient ammonium assimilation by N-limited Chlamydomonas reinhardtii. Plant Physiol 94: 1131-1136
    • (1990) Plant Physiol , vol.94 , pp. 1131-1136
    • Weger, H.G.1    Chadderton, A.R.2    Lin, M.3    Guy, R.D.4    Turpin, D.H.5
  • 74
    • 84957894255 scopus 로고
    • Electrometric and colorimetric determination of carbonic anhydrase
    • Wilbur KM, Anderson NG (1948) Electrometric and colorimetric determination of carbonic anhydrase. J Biol Chem 176: 147-154
    • (1948) J Biol Chem , vol.176 , pp. 147-154
    • Wilbur, K.M.1    Anderson, N.G.2
  • 75
    • 0000715503 scopus 로고
    • Differential accumulation of biotin enzymes during carrot somatic embryogenesis
    • Wurtele ES, Nikolau BJ (1992) Differential accumulation of biotin enzymes during carrot somatic embryogenesis. Plant Physiol 99: 1699-1703
    • (1992) Plant Physiol , vol.99 , pp. 1699-1703
    • Wurtele, E.S.1    Nikolau, B.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.