메뉴 건너뛰기




Volumn 226, Issue 5, 2007, Pages 1075-1086

Photosynthetic H2 metabolism in Chlamydomonas reinhardtii (unicellular green algae)

Author keywords

Chlamydomonas reinhardtii; Green algae; H2; Hydrogen production; Hydrogenase; Photosynthesis; Sulfur deprivation

Indexed keywords

ALGAE; CHLAMYDOMONAS REINHARDTII; CHLOROPHYTA;

EID: 34548528653     PISSN: 00320935     EISSN: 14322048     Source Type: Journal    
DOI: 10.1007/s00425-007-0609-9     Document Type: Review
Times cited : (219)

References (113)
  • 1
    • 0025000128 scopus 로고
    • The structure and mechanism of iron-hydrogenases
    • Adams MWW (1990) The structure and mechanism of iron-hydrogenases. Biochim Biophys Acta 1020:115-145
    • (1990) Biochim Biophys Acta , vol.1020 , pp. 115-145
    • Adams, M.W.W.1
  • 2
    • 0034124718 scopus 로고    scopus 로고
    • Organometallic iron: The key to biological hydrogen metabolism
    • Adams MWW, Stiefel EI (2000) Organometallic iron: the key to biological hydrogen metabolism. Curr Opin Chem Biol 4:214-220
    • (2000) Curr Opin Chem Biol , vol.4 , pp. 214-220
    • Adams, M.W.W.1    Stiefel, E.I.2
  • 3
    • 12344288213 scopus 로고    scopus 로고
    • Production of H-2 by sulphur-deprived cells of the unicellular cyanobacteria Gloeocapsa alpicola and Synechocystis sp PCC 6803 during dark incubation with methane or at various extracellular pH
    • Antal TK, Lindblad P (2005) Production of H-2 by sulphur-deprived cells of the unicellular cyanobacteria Gloeocapsa alpicola and Synechocystis sp PCC 6803 during dark incubation with methane or at various extracellular pH. J Appl Microbiol 98:114-120
    • (2005) J Appl Microbiol , vol.98 , pp. 114-120
    • Antal, T.K.1    Lindblad, P.2
  • 5
    • 0032216314 scopus 로고    scopus 로고
    • Hydrogen metabolism in organisms with oxygenic photosynthesis: Hydrogenases as important regulatory devices for a proper redox poising?
    • Appel J, Schulz R (1998) Hydrogen metabolism in organisms with oxygenic photosynthesis: hydrogenases as important regulatory devices for a proper redox poising?. J Photochem Photobiol B Biol 47:1-11
    • (1998) J Photochem Photobiol B Biol , vol.47 , pp. 1-11
    • Appel, J.1    Schulz, R.2
  • 6
    • 0001666285 scopus 로고
    • Photoproduction of hydrogen gas coupled with photosynthetic phosphorylation
    • Arnon DI, Mitsui A, Paneque A (1961) Photoproduction of hydrogen gas coupled with photosynthetic phosphorylation. Science 134:1425
    • (1961) Science , vol.134 , pp. 1425
    • Arnon, D.I.1    Mitsui, A.2    Paneque, A.3
  • 7
    • 0003006270 scopus 로고
    • A Chlamydomonas reinhardtii low-starch mutant is defective for 3-phosphoglycerate activation and orthophosphate inhibition of ADP-glucose pyrophosphorylase
    • Ball S, Marianne T, Dirick L, Fresnoy M, Delrue B, Decq A (1991) A Chlamydomonas reinhardtii low-starch mutant is defective for 3-phosphoglycerate activation and orthophosphate inhibition of ADP-glucose pyrophosphorylase. Planta 185:17-26
    • (1991) Planta , vol.185 , pp. 17-26
    • Ball, S.1    Marianne, T.2    Dirick, L.3    Fresnoy, M.4    Delrue, B.5    Decq, A.6
  • 9
    • 0025435099 scopus 로고
    • The biotechnology of cultivating the halotolerant alga Dunaliella
    • Ben-Amotz A, Avron M (1990) The biotechnology of cultivating the halotolerant alga Dunaliella. Trends Biotechnol 8:121-128
    • (1990) Trends Biotechnol , vol.8 , pp. 121-128
    • Ben-Amotz, A.1    Avron, M.2
  • 10
    • 0035902934 scopus 로고    scopus 로고
    • Chlororespiration and the process of carotenoid biosynthesis
    • Bennoun P (2001) Chlororespiration and the process of carotenoid biosynthesis. Biochim Biophys Acta 1506:133-142
    • (2001) Biochim Biophys Acta , vol.1506 , pp. 133-142
    • Bennoun, P.1
  • 11
    • 0001985809 scopus 로고
    • On the interrelation of the mechanisms for oxygen and hydrogen evolution in adapted algae
    • Natl Acad Sci Natl Res Council, Washington, DC
    • Bishop NI, Gaffron H (1963) On the interrelation of the mechanisms for oxygen and hydrogen evolution in adapted algae. In: Publ 1145, Photosynthetic mechanisms in green plants. Natl Acad Sci Natl Res Council, Washington, DC, pp 441-451
    • (1963) Publ 1145, Photosynthetic Mechanisms in Green Plants , pp. 441-451
    • Bishop, N.I.1    Gaffron, H.2
  • 12
    • 0003112872 scopus 로고
    • Photohydrogen production in green algae: Water serves as the primary substrate for hydrogen and oxygen production
    • Academic Press New York
    • Bishop NI, Frick M, Jones LW (1977) Photohydrogen production in green algae: water serves as the primary substrate for hydrogen and oxygen production. In: Mitsui A, Miyachi S, San Pietro A, Tamura S (eds) Biological solar energy conversion. Academic Press, New York, pp 3-22
    • (1977) Biological Solar Energy Conversion , pp. 3-22
    • Bishop, N.I.1    Frick, M.2    Jones, L.W.3    Mitsui, A.4    Miyachi, S.5    San Pietro, A.6    Tamura, S.7
  • 13
    • 0035120961 scopus 로고    scopus 로고
    • Bioenergetic and metabolic processes for the survival of sulfur-deprived Dunaliella salina (Chlorophyta)
    • Cao H, Zhang L, Melis A (2001) Bioenergetic and metabolic processes for the survival of sulfur-deprived Dunaliella salina (Chlorophyta). J Appl Phycol 13:25-34
    • (2001) J Appl Phycol , vol.13 , pp. 25-34
    • Cao, H.1    Zhang, L.2    Melis, A.3
  • 14
    • 11844282214 scopus 로고    scopus 로고
    • Localization and function of SulP, a nuclear-encoded chloroplast sulfate permease in Chlamydomonas reinhardtii
    • Chen H-C, Melis A (2004) Localization and function of SulP, a nuclear-encoded chloroplast sulfate permease in Chlamydomonas reinhardtii. Planta 220:198-210
    • (2004) Planta , vol.220 , pp. 198-210
    • Chen, H.-C.1    Melis, A.2
  • 15
    • 0347300314 scopus 로고    scopus 로고
    • SulP, a nuclear gene encoding a putative chloroplast-targeted sulfate permease in Chlamydomonas reinhardtii
    • Chen HC, Yokthongwattana K, Newton AJ, Melis A (2003) SulP, a nuclear gene encoding a putative chloroplast-targeted sulfate permease in Chlamydomonas reinhardtii. Planta 218:98-106
    • (2003) Planta , vol.218 , pp. 98-106
    • Chen, H.C.1    Yokthongwattana, K.2    Newton, A.J.3    Melis, A.4
  • 17
    • 0027130451 scopus 로고
    • The role of carbon dioxide in light-activated hydrogen production by Chlamydomonas reinhardtii
    • Cinco RM, Macinnis JM, Greenbaum E (1993) The role of carbon dioxide in light-activated hydrogen production by Chlamydomonas reinhardtii. Photosynth Res 38:27-33
    • (1993) Photosynth Res , vol.38 , pp. 27-33
    • Cinco, R.M.1    MacInnis, J.M.2    Greenbaum, E.3
  • 18
    • 0036836471 scopus 로고    scopus 로고
    • Limiting steps of hydrogen production in Chlamydomonas reinhardtii and Synechocystis PCC 6803 as analysed by light-induced gas exchange transients
    • Cournac L, Mus F, Bernard L, Guedeney G, Vignais P, Peltier G (2002) Limiting steps of hydrogen production in Chlamydomonas reinhardtii and Synechocystis PCC 6803 as analysed by light-induced gas exchange transients. Int J Hydrogen Energy 27:1229-1237
    • (2002) Int J Hydrogen Energy , vol.27 , pp. 1229-1237
    • Cournac, L.1    Mus, F.2    Bernard, L.3    Guedeney, G.4    Vignais, P.5    Peltier, G.6
  • 20
    • 0028105642 scopus 로고
    • Mutants of Chlamydomonas with aberrant responses to sulfur deprivation
    • Davies JP, Yildiz F, Grossman AR (1994) Mutants of Chlamydomonas with aberrant responses to sulfur deprivation. Plant Cell 6:53-63
    • (1994) Plant Cell , vol.6 , pp. 53-63
    • Davies, J.P.1    Yildiz, F.2    Grossman, A.R.3
  • 21
    • 0001657280 scopus 로고    scopus 로고
    • NAD(P)H dehydrogenase-dependent, antimycin A-sensitive electron donation to plastoquinone in tobacco chloroplasts
    • Endo T, Shikanai T, Sato F, Asada K (1998) NAD(P)H dehydrogenase- dependent, antimycin A-sensitive electron donation to plastoquinone in tobacco chloroplasts. Plant Cell Physiol 39:1226-1231
    • (1998) Plant Cell Physiol , vol.39 , pp. 1226-1231
    • Endo, T.1    Shikanai, T.2    Sato, F.3    Asada, K.4
  • 22
    • 0000792290 scopus 로고    scopus 로고
    • Nonphotochemical reduction of the plastoquinone pool in sunflower leaves originates from chlororespiration
    • Feild TS, Nedbal L, Ort DR (1998) Nonphotochemical reduction of the plastoquinone pool in sunflower leaves originates from chlororespiration. Plant Physiol 116:1209-1218
    • (1998) Plant Physiol , vol.116 , pp. 1209-1218
    • Feild, T.S.1    Nedbal, L.2    Ort, D.R.3
  • 23
    • 0035794131 scopus 로고    scopus 로고
    • A novel type of [Fe]-hydrogenase in the green alga Scenedesmus obliquus is linked to the photosynthetical electron transport chain
    • Florin L, Tsokoglou A, Happe T (2001) A novel type of [Fe]-hydrogenase in the green alga Scenedesmus obliquus is linked to the photosynthetical electron transport chain. J Biol Chem 276:6125-6132
    • (2001) J Biol Chem , vol.276 , pp. 6125-6132
    • Florin, L.1    Tsokoglou, A.2    Happe, T.3
  • 26
    • 0001474307 scopus 로고
    • Correlation between respiration and hydrogenase adaptation in Scenedesmus obliquus
    • Francis K, Senger H (1985) Correlation between respiration and hydrogenase adaptation in Scenedesmus obliquus. Physiol Plant 65:167-170
    • (1985) Physiol Plant , vol.65 , pp. 167-170
    • Francis, K.1    Senger, H.2
  • 27
    • 0000397742 scopus 로고
    • 2 in green plants
    • 2 in green plants. Nature 143:204-205
    • (1939) Nature , vol.143 , pp. 204-205
    • Gaffron, H.1
  • 28
    • 0000031606 scopus 로고
    • Carbon dioxide reduction with molecular hydrogen in green algae
    • Gaffron H (1940) Carbon dioxide reduction with molecular hydrogen in green algae. Am J Bot 27:273-283
    • (1940) Am J Bot , vol.27 , pp. 273-283
    • Gaffron, H.1
  • 29
    • 85013539590 scopus 로고
    • Reduction of carbon dioxide coupled with the oxyhydrogen reaction in algae
    • Gaffron H (1942) Reduction of carbon dioxide coupled with the oxyhydrogen reaction in algae. J Gen Physiol 26:241-267
    • (1942) J Gen Physiol , vol.26 , pp. 241-267
    • Gaffron, H.1
  • 30
    • 84941787599 scopus 로고
    • Fermentative and photochemical production of hydrogen in algae
    • Gaffron H, Rubin J (1942) Fermentative and photochemical production of hydrogen in algae. J Gen Physiol 26:219-240
    • (1942) J Gen Physiol , vol.26 , pp. 219-240
    • Gaffron, H.1    Rubin, J.2
  • 31
    • 0002104918 scopus 로고
    • Fermentative metabolism of Chlamydomonas reinhardtii
    • Gfeller RP, Gibbs M (1984) Fermentative metabolism of Chlamydomonas reinhardtii. Analysis of fermentative products from starch in dark-light. Plant Physiol 75:212-218
    • (1984) Plant Physiol , vol.75 , pp. 212-218
    • Gfeller, R.P.1    Gibbs, M.2
  • 34
    • 0000690486 scopus 로고
    • Fermentative metabolism of Chlamydomonas reinhardtii. III. Photo-assimilation of acetate
    • Gibbs M, Gfeller RP, Chen C (1986) Fermentative metabolism of Chlamydomonas reinhardtii. III. Photo-assimilation of acetate. Plant Physiol 82:160-166
    • (1986) Plant Physiol , vol.82 , pp. 160-166
    • Gibbs, M.1    Gfeller, R.P.2    Chen, C.3
  • 35
    • 0033794301 scopus 로고    scopus 로고
    • Strategies for the allocation of resources under sulfur limitation in the green alga Dunaliella salina
    • Giordano M, Pezzoni V, Hell R (2000) Strategies for the allocation of resources under sulfur 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
  • 36
    • 18444393412 scopus 로고    scopus 로고
    • Homologous and heterologous overexpression in Clostridium acetobutylicum and characterization of purified clostridial and algal Fe-only hydrogenases with high specific activities
    • Girbal L Von Abendroth G Winkler M, Benton BMC, Meynial-Salles I Croux C, Peters JW, Happe T, Soucaille P (2005) Homologous and heterologous overexpression in Clostridium acetobutylicum and characterization of purified clostridial and algal Fe-only hydrogenases with high specific activities. Appl Environ Microbiol 71:2777-2781
    • (2005) Appl Environ Microbiol , vol.71 , pp. 2777-2781
    • Girbal, L.1    Von Abendroth, G.2    Winkler, M.3    Benton, B.M.C.4    Meynial-Salles, I.5    Croux, C.6    Peters, J.W.7    Happe, T.8    Soucaille, P.9
  • 37
    • 0019126116 scopus 로고
    • NADH as electron donor for the photosynthetic membrane of Chlamydomonas reinhardtii
    • Godde D, Trebst A (1980) NADH as electron donor for the photosynthetic membrane of Chlamydomonas reinhardtii. Arch Microbiol 127:245-252
    • (1980) Arch Microbiol , vol.127 , pp. 245-252
    • Godde, D.1    Trebst, A.2
  • 38
    • 0000802846 scopus 로고
    • Photosynthetic hydrogen and oxygen production: Kinetic studies
    • Greenbaum E (1982) Photosynthetic hydrogen and oxygen production: kinetic studies. Science 196:879-880
    • (1982) Science , vol.196 , pp. 879-880
    • Greenbaum, E.1
  • 39
    • 0001090049 scopus 로고
    • 2 photoevolution by algal water-splitting
    • 2 photoevolution by algal water-splitting. Biophys J 54:365-368
    • (1988) Biophys J , vol.54 , pp. 365-368
    • Greenbaum, E.1
  • 41
    • 0036186921 scopus 로고    scopus 로고
    • Differential regulation of the [Fe]-hydrogenase during anaerobic adaptation in the green alga Chlamydomonas reinhardtii
    • Happe T, Kaminski A (2002) Differential regulation of the [Fe]-hydrogenase during anaerobic adaptation in the green alga Chlamydomonas reinhardtii. Eur J Biochem 269:1022-1032
    • (2002) Eur J Biochem , vol.269 , pp. 1022-1032
    • Happe, T.1    Kaminski, A.2
  • 42
    • 0027153213 scopus 로고
    • Isolation, characterization and N-terminal amino acid sequence of hydrogenase from the green alga Chlamydomonas reinhardtii
    • Happe T, Naber JD (1993) Isolation, characterization and N-terminal amino acid sequence of hydrogenase from the green alga Chlamydomonas reinhardtii. Eur J Biochem 214:475-481
    • (1993) Eur J Biochem , vol.214 , pp. 475-481
    • Happe, T.1    Naber, J.D.2
  • 43
    • 0028285551 scopus 로고
    • Induction, localization and metal content of hydrogenase in the green alga Chlamydomonas reinhardtii
    • Happe T, Mosler B, Naber JD (1994) Induction, localization and metal content of hydrogenase in the green alga Chlamydomonas reinhardtii. Eur J Biochem 222:769-774
    • (1994) Eur J Biochem , vol.222 , pp. 769-774
    • Happe, T.1    Mosler, B.2    Naber, J.D.3
  • 44
    • 14644441716 scopus 로고    scopus 로고
    • The exceptional photofermentative hydrogen metabolism of the green alga Chlamydomonas reinhardtii
    • Hemschemeier A, Happe T (2005) The exceptional photofermentative hydrogen metabolism of the green alga Chlamydomonas reinhardtii. Biochem Soc Trans 33:39-41
    • (2005) Biochem Soc Trans , vol.33 , pp. 39-41
    • Hemschemeier, A.1    Happe, T.2
  • 45
    • 85047684869 scopus 로고    scopus 로고
    • When simpler is better. Unicellular green algae for discovering new genes and functions in carbohydrate metabolism
    • Hicks GR, Hironaka CM, Dauvillee D, Funke RP, d'Hulst C, Waffenschmidt S, Ball SG (2001) When simpler is better. Unicellular green algae for discovering new genes and functions in carbohydrate metabolism. Plant Physiol 127:1334-1338
    • (2001) Plant Physiol , vol.127 , pp. 1334-1338
    • Hicks, G.R.1    Hironaka, C.M.2    Dauvillee, D.3    Funke, R.P.4    D'Hulst, C.5    Waffenschmidt, S.6    Ball, S.G.7
  • 47
    • 0014005438 scopus 로고
    • The effect of glucose on hydrogenase activity in Chlorella
    • Kessler E (1966) The effect of glucose on hydrogenase activity in Chlorella. Biochim Biophys Acta 112:173-175
    • (1966) Biochim Biophys Acta , vol.112 , pp. 173-175
    • Kessler, E.1
  • 48
    • 0015810074 scopus 로고
    • Effect of anaerobiosis on photosynthetic reactions and nitrogen metabolism of algae with and without hydrogenase
    • Kessler E (1973) Effect of anaerobiosis on photosynthetic reactions and nitrogen metabolism of algae with and without hydrogenase. Arch Microbiol 93:91-100
    • (1973) Arch Microbiol , vol.93 , pp. 91-100
    • Kessler, E.1
  • 49
    • 0002056160 scopus 로고
    • Hydrogenase, photoreduction and anaerobic growth of algae
    • Blackwell, Oxford
    • Kessler E (1974) Hydrogenase, photoreduction and anaerobic growth of algae. In: Algal physiology and biochemistry. Blackwell, Oxford, pp 454-473
    • (1974) Algal Physiology and Biochemistry , pp. 454-473
    • Kessler, E.1
  • 51
    • 33644850541 scopus 로고    scopus 로고
    • Functional studies of [FeFe] hydrogenase maturation in an Escherichia coli biosynthetic system
    • King PW, Posewitz MC, Ghirardi ML, Seibert M (2006) Functional studies of [FeFe] hydrogenase maturation in an Escherichia coli biosynthetic system. J Bacteriol 188:2163-2172
    • (2006) J Bacteriol , vol.188 , pp. 2163-2172
    • King, P.W.1    Posewitz, M.C.2    Ghirardi, M.L.3    Seibert, M.4
  • 52
    • 0027344304 scopus 로고
    • Nucleotide sequence and homology comparison of two genes of the sulfate transport operon from the cyanobacterium Synechocystis sp. PCC6803
    • Kohn C, Schumann J (1993) Nucleotide sequence and homology comparison of two genes of the sulfate transport operon from the cyanobacterium Synechocystis sp. PCC6803. Plant Mol Biol 21:409-412
    • (1993) Plant Mol Biol , vol.21 , pp. 409-412
    • Kohn, C.1    Schumann, J.2
  • 54
    • 33847340991 scopus 로고    scopus 로고
    • A comparison of hydrogen photoproduction by sulfur-deprived Chlamydomonas reinhardtii under different growth conditions
    • Kosourov S, Patrusheva E, Ghirardi ML, Seibert M, Tsygankov A (2007) A comparison of hydrogen photoproduction by sulfur-deprived Chlamydomonas reinhardtii under different growth conditions J Biotech 128:776-787
    • (2007) J Biotech , vol.128 , pp. 776-787
    • Kosourov, S.1    Patrusheva, E.2    Ghirardi, M.L.3    Seibert, M.4    Tsygankov, A.5
  • 56
    • 0029740614 scopus 로고    scopus 로고
    • Differential expression of plastome-encoded ndh genes in mesophyll and bundle-sheath chloroplasts of the C-4 plant sorghum bicolor indicates that the complex I-homologous NAD(P)H-plastoquinone oxidoreductase is involved
    • Kubicki A, Funk E, Westhoff P, Steinmuller K (1996) Differential expression of plastome-encoded ndh genes in mesophyll and bundle-sheath chloroplasts of the C-4 plant sorghum bicolor indicates that the complex I-homologous NAD(P)H-plastoquinone oxidoreductase is involved. Planta 199:276-281
    • (1996) Planta , vol.199 , pp. 276-281
    • Kubicki, A.1    Funk, E.2    Westhoff, P.3    Steinmuller, K.4
  • 57
    • 0036938981 scopus 로고    scopus 로고
    • Chloroplast division machinery as revealed by immunofluorescence and electron microscopy
    • Kuroiwa H, Mori T, Takahara M, Miyagishima S, Kuroiwa T (2002) Chloroplast division machinery as revealed by immunofluorescence and electron microscopy. Planta 215:185-190
    • (2002) Planta , vol.215 , pp. 185-190
    • Kuroiwa, H.1    Mori, T.2    Takahara, M.3    Miyagishima, S.4    Kuroiwa, T.5
  • 58
    • 0025793667 scopus 로고
    • Characterization and mutagenesis of sulfur-regulated genes in a cyanobacterium: Evidence for function in sulfate transport
    • Laudenbach DE, Grossman A (1991) Characterization and mutagenesis of sulfur-regulated genes in a cyanobacterium: evidence for function in sulfate transport. J Bacteriol 173:2739-2750
    • (1991) J Bacteriol , vol.173 , pp. 2739-2750
    • Laudenbach, D.E.1    Grossman, A.2
  • 59
    • 0002678945 scopus 로고
    • Absolute absorption cross sections for photosystem II and the minimum quantum requirement for photosynthesis in Chlorella vulgaris
    • Ley AC, Mauzerall DC (1982) Absolute absorption cross sections for photosystem II and the minimum quantum requirement for photosynthesis in Chlorella vulgaris. Biochim Biophys Acta 680:95-106
    • (1982) Biochim Biophys Acta , vol.680 , pp. 95-106
    • Ley, A.C.1    Mauzerall, D.C.2
  • 60
    • 0000688294 scopus 로고
    • Association of the chlorplastic respiratory and photosynthetic electron transport chains of C. reinhardii with photoreduction and the oxyhydrogen reaction
    • Maione TE, Gibbs M (1986a) Association of the chlorplastic respiratory and photosynthetic electron transport chains of C. reinhardii with photoreduction and the oxyhydrogen reaction. Plant Physiol 80:364-368
    • (1986) Plant Physiol , vol.80 , pp. 364-368
    • Maione, T.E.1    Gibbs, M.2
  • 61
    • 0000572642 scopus 로고
    • Hydrogenase-mediated activities in isolated chloroplasts of Chlamydomonas reinhardii
    • Maione TE, Gibbs M (1986b) Hydrogenase-mediated activities in isolated chloroplasts of Chlamydomonas reinhardii. Plant Physiol 80:360-363
    • (1986) Plant Physiol , vol.80 , pp. 360-363
    • Maione, T.E.1    Gibbs, M.2
  • 63
    • 0032948239 scopus 로고    scopus 로고
    • Photosystem-II damage and repair cycle in chloroplasts: What modulates the rate of photodamage in vivo?
    • Melis A (1999) Photosystem-II damage and repair cycle in chloroplasts: what modulates the rate of photodamage in vivo?. Trends Plant Sci 4:130-135
    • (1999) Trends Plant Sci , vol.4 , pp. 130-135
    • Melis, A.1
  • 64
    • 0036827174 scopus 로고    scopus 로고
    • Green alga hydrogen production: Progress, challenges and prospects
    • Melis A (2002) Green alga hydrogen production: progress, challenges and prospects. Int J Hydrogen Energy 27:1217-1228
    • (2002) Int J Hydrogen Energy , vol.27 , pp. 1217-1228
    • Melis, A.1
  • 65
    • 29944431657 scopus 로고    scopus 로고
    • Chloroplast sulfate transport in green algae: Genes, proteins and effects
    • Melis A, Chen HC (2005) Chloroplast sulfate transport in green algae: genes, proteins and effects. Photosynth Res 86:299-307
    • (2005) Photosynth Res , vol.86 , pp. 299-307
    • Melis, A.1    Chen, H.C.2
  • 66
    • 0035197070 scopus 로고    scopus 로고
    • Hydrogen production: Green algae as a source of energy
    • Melis A, Happe T (2001) Hydrogen production: green algae as a source of energy. Plant Physiol 127:740-748
    • (2001) Plant Physiol , vol.127 , pp. 740-748
    • Melis, A.1    Happe, T.2
  • 67
    • 0032423858 scopus 로고    scopus 로고
    • Dunaliella salina (Chlorophyta) with small chlorophyll antenna sizes exhibit higher photosynthetic productivities and photon use efficiencies than normally pigmented cells
    • Melis A, Neidhardt J, Benemann JR (1998) Dunaliella salina (Chlorophyta) with small chlorophyll antenna sizes exhibit higher photosynthetic productivities and photon use efficiencies than normally pigmented cells. J Appl Phycol 10:515-525
    • (1998) J Appl Phycol , vol.10 , pp. 515-525
    • Melis, A.1    Neidhardt, J.2    Benemann, J.R.3
  • 68
    • 0033759410 scopus 로고    scopus 로고
    • Sustained photobiological hydrogen gas production upon reversible inactivation of oxygen evolution in the green alga Chlamydomonas reinhardtii
    • Melis A, Zhang L, Forestier M, Ghirardi ML, Seibert M (2000) Sustained photobiological hydrogen gas production upon reversible inactivation of oxygen evolution in the green alga Chlamydomonas reinhardtii. Plant Physiol 122:127-136
    • (2000) Plant Physiol , vol.122 , pp. 127-136
    • Melis, A.1    Zhang, L.2    Forestier, M.3    Ghirardi, M.L.4    Seibert, M.5
  • 69
    • 29944442773 scopus 로고    scopus 로고
    • Genomics of green algal hydrogen research
    • Melis A, Seibert M, Happe T (2004) Genomics of green algal hydrogen research. Photosynth Res 82:277-288
    • (2004) Photosynth Res , vol.82 , pp. 277-288
    • Melis, A.1    Seibert, M.2    Happe, T.3
  • 70
    • 0026040877 scopus 로고
    • Primary structure of hydrogenase I from Clostridium pasterianum
    • Meyer J, Gagnon J (1991) Primary structure of hydrogenase I from Clostridium pasterianum. Biochemistry 30:9697-9704
    • (1991) Biochemistry , vol.30 , pp. 9697-9704
    • Meyer, J.1    Gagnon, J.2
  • 71
    • 0035087599 scopus 로고    scopus 로고
    • The timing and manner of disassembly of the apparatuses for chloroplast and mitochondrial division in the red alga Cyanidioschyzon merolae
    • Miyagishima S, Kuroiwa H, Kuroiwa T (2001) The timing and manner of disassembly of the apparatuses for chloroplast and mitochondrial division in the red alga Cyanidioschyzon merolae. Planta 212:517-528
    • (2001) Planta , vol.212 , pp. 517-528
    • Miyagishima, S.1    Kuroiwa, H.2    Kuroiwa, T.3
  • 72
    • 21744446408 scopus 로고    scopus 로고
    • Inhibitor studies on non-photochemical plastoquinone reduction and H-2 photoproduction in Chlamydomonas reinhardtii
    • Mus F, Cournac L, Cardettini W, Caruana A, Peltier G (2005) Inhibitor studies on non-photochemical plastoquinone reduction and H-2 photoproduction in Chlamydomonas reinhardtii. Biochim Biophys Acta 1708:322-332
    • (2005) Biochim Biophys Acta , vol.1708 , pp. 322-332
    • Mus, F.1    Cournac, L.2    Cardettini, W.3    Caruana, A.4    Peltier, G.5
  • 73
    • 0029854243 scopus 로고    scopus 로고
    • The ndhf chloroplast gene detected in all vascular plant divisions
    • Neyland R, Urbatsch LE (1996) The ndhf chloroplast gene detected in all vascular plant divisions. Planta 200:273-277
    • (1996) Planta , vol.200 , pp. 273-277
    • Neyland, R.1    Urbatsch, L.E.2
  • 74
    • 0022546644 scopus 로고
    • Chloroplast gene organization deduced from complete sequence of liverwort Marchantia polymorpha chloroplast DNA
    • Ohyma K, Fukuzawa H, Kohchi T, Shirai H, Sano T, others (1986) Chloroplast gene organization deduced from complete sequence of liverwort Marchantia polymorpha chloroplast DNA. Nature 322:572-574
    • (1986) Nature , vol.322 , pp. 572-574
    • Ohyma, K.1    Fukuzawa, H.2    Kohchi, T.3    Shirai, H.4    Sano, T.5    Others6
  • 76
    • 0032240930 scopus 로고    scopus 로고
    • Plastid division: Evidence for a prokaryotically derived mechanism
    • Osteryoung KW, Pyke KA (1998) Plastid division: evidence for a prokaryotically derived mechanism. Curr Opin Plant Biol 1:475-479
    • (1998) Curr Opin Plant Biol , vol.1 , pp. 475-479
    • Osteryoung, K.W.1    Pyke, K.A.2
  • 77
    • 0032287069 scopus 로고    scopus 로고
    • Chloroplast division in higher plants requires members of two functionally divergent gene families with homology to bacterial ftsZ
    • Osteryoung KW, Stokes KD, Rutherford SM, Percival AL, Lee WY (1998) Chloroplast division in higher plants requires members of two functionally divergent gene families with homology to bacterial ftsZ. Plant Cell 10:1991-2004
    • (1998) Plant Cell , vol.10 , pp. 1991-2004
    • Osteryoung, K.W.1    Stokes, K.D.2    Rutherford, S.M.3    Percival, A.L.4    Lee, W.Y.5
  • 78
    • 0032804337 scopus 로고    scopus 로고
    • Structure and mechanism of iron-only hydrogenases
    • Peters JW (1999) Structure and mechanism of iron-only hydrogenases. Curr Opin Struct Biol 9:670-676
    • (1999) Curr Opin Struct Biol , vol.9 , pp. 670-676
    • Peters, J.W.1
  • 79
    • 0032483966 scopus 로고    scopus 로고
    • X-ray crystal structure of the Fe-only hydrogenase (CpI) from Clostridium pasteurianum to 1.8 angstrom resolution
    • Peters JW, Lanzilotta WN, Lemon BJ, Seefeldt LC (1998) X-ray crystal structure of the Fe-only hydrogenase (CpI) from Clostridium pasteurianum to 1.8 angstrom resolution. Science 282:1853-1858
    • (1998) Science , vol.282 , pp. 1853-1858
    • Peters, J.W.1    Lanzilotta, W.N.2    Lemon, B.J.3    Seefeldt, L.C.4
  • 80
    • 0037596752 scopus 로고    scopus 로고
    • Tla1, a DNA insertional transformant of the green alga Chlamydomonas reinhardtii with a truncated light-harvesting chlorophyll antenna size
    • Polle JEW, Kanakagiri S, Melis A (2003) tla1, a DNA insertional transformant of the green alga Chlamydomonas reinhardtii with a truncated light-harvesting chlorophyll antenna size. Planta 217:49-59
    • (2003) Planta , vol.217 , pp. 49-59
    • Polle, J.E.W.1    Kanakagiri, S.2    Melis, A.3
  • 81
    • 2942586665 scopus 로고    scopus 로고
    • Discovery of two novel radical S-adenosylmethionine proteins required for the assembly of an active [Fe] hydrogenase
    • Posewitz MC, King PW, Smolinski SL, Zhang LP, Seibert M, Ghirardi ML (2004a) Discovery of two novel radical S-adenosylmethionine proteins required for the assembly of an active [Fe] hydrogenase. J Biol Chem 279:25711-25720
    • (2004) J Biol Chem , vol.279 , pp. 25711-25720
    • Posewitz, M.C.1    King, P.W.2    Smolinski, S.L.3    Zhang, L.P.4    Seibert, M.5    Ghirardi, M.L.6
  • 82
    • 4043114949 scopus 로고    scopus 로고
    • Hydrogen photoproduction is attenuated by disruption of an isoamylase gene in Chlamydomonas reinhardtii
    • Posewitz MC, Smolinski SL, Kanakagiri S, Melis A, Seibert M, Ghirardi ML (2004b) Hydrogen photoproduction is attenuated by disruption of an isoamylase gene in Chlamydomonas reinhardtii. Plant Cell 16:2151-2163
    • (2004) Plant Cell , vol.16 , pp. 2151-2163
    • Posewitz, M.C.1    Smolinski, S.L.2    Kanakagiri, S.3    Melis, A.4    Seibert, M.5    Ghirardi, M.L.6
  • 83
    • 0031431069 scopus 로고    scopus 로고
    • The genetic control of plastid division in higher plants
    • Pyke KA (1997) The genetic control of plastid division in higher plants. Am J Bot 84:1017-1027
    • (1997) Am J Bot , vol.84 , pp. 1017-1027
    • Pyke, K.A.1
  • 84
    • 0032725631 scopus 로고    scopus 로고
    • Plastid division and development
    • Pyke KA (1999) Plastid division and development. Plant Cell 11:549-556
    • (1999) Plant Cell , vol.11 , pp. 549-556
    • Pyke, K.A.1
  • 85
    • 84989701125 scopus 로고
    • Participation of the two photosystems in light dependent hydrogen evolution in Scenedesmus obliquus
    • Randt C, Senger H (1985) Participation of the two photosystems in light dependent hydrogen evolution in Scenedesmus obliquus. Photochem Photobiol 42:553-557
    • (1985) Photochem Photobiol , vol.42 , pp. 553-557
    • Randt, C.1    Senger, H.2
  • 86
    • 0001206507 scopus 로고
    • Activation and de novo synthesis of hydrogenase in Chlamydomonas
    • Roessler PG, Lien S (1984) Activation and de novo synthesis of hydrogenase in Chlamydomonas. Plant Physiol 76:1086-1089
    • (1984) Plant Physiol , vol.76 , pp. 1086-1089
    • Roessler, P.G.1    Lien, S.2
  • 88
    • 0032477715 scopus 로고    scopus 로고
    • The plastid ndh genes code for an NADH-specific dehydrogenase: Isolation of a complex I analogue from pea thylakoid membranes
    • Sazanov LA, Burrows PA, Nixon PJ (1998) The plastid ndh genes code for an NADH-specific dehydrogenase: isolation of a complex I analogue from pea thylakoid membranes. Proc Natl Acad Sci USA 95:1319-1324
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 1319-1324
    • Sazanov, L.A.1    Burrows, P.A.2    Nixon, P.J.3
  • 89
    • 0027165223 scopus 로고
    • Characterization and purification of a hydrogenase from the eukaryotic green alga Scenedesmus obliquus
    • Schnackenberg J, Schulz R, Senger H (1993) Characterization and purification of a hydrogenase from the eukaryotic green alga Scenedesmus obliquus. FEBS Lett 327:21-24
    • (1993) FEBS Lett , vol.327 , pp. 21-24
    • Schnackenberg, J.1    Schulz, R.2    Senger, H.3
  • 90
    • 0001922519 scopus 로고    scopus 로고
    • Hydrogenases and hydrogen production in eukaryotic organisms and cyanobacteria
    • Schulz R (1996) Hydrogenases and hydrogen production in eukaryotic organisms and cyanobacteria. J Mar Biotechnol 4:16-22
    • (1996) J Mar Biotechnol , vol.4 , pp. 16-22
    • Schulz, R.1
  • 93
    • 0001980282 scopus 로고
    • Simultaneous photoproduction of hydrogen and oxygen by Chlorella
    • Spruit CP (1958) Simultaneous photoproduction of hydrogen and oxygen by Chlorella. Meded Landbouwhogeschool Wageningen 58:1-17
    • (1958) Meded Landbouwhogeschool Wageningen , vol.58 , pp. 1-17
    • Spruit, C.P.1
  • 94
    • 0001649666 scopus 로고
    • The mechanism of hydrogen photoproduction by several algae. II the contribution of photosystem II
    • Stuart TS, Gaffron H (1972) The mechanism of hydrogen photoproduction by several algae. II The contribution of photosystem II. Planta 106:101-112
    • (1972) Planta , vol.106 , pp. 101-112
    • Stuart, T.S.1    Gaffron, H.2
  • 95
    • 33847289819 scopus 로고    scopus 로고
    • Development of the light-harvesting chlorophyll antenna in the green alga Chlamydomonas reinhardtii is regulated by the novel Tla1 gene
    • Tetali S, Mitra M, Melis A (2007) Development of the light-harvesting chlorophyll antenna in the green alga Chlamydomonas reinhardtii is regulated by the novel Tla1 gene. Planta 225:813-829
    • (2007) Planta , vol.225 , pp. 813-829
    • Tetali, S.1    Mitra, M.2    Melis, A.3
  • 98
    • 0033621040 scopus 로고    scopus 로고
    • The complete chloroplast DNA sequence of the green alga Nephroselmis olivacea: Insights into the architecture of ancestral chloroplast genomes
    • Turmel M, Otis C, Lemieux C (1999) The complete chloroplast DNA sequence of the green alga Nephroselmis olivacea: insights into the architecture of ancestral chloroplast genomes. Proc Natl Acad Sci USA 96:10248-10253
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 10248-10253
    • Turmel, M.1    Otis, C.2    Lemieux, C.3
  • 101
    • 0035795421 scopus 로고    scopus 로고
    • FtsZ ring formation at the chloroplast division site in plants
    • Vitha S, McAndrew RS, Osteryoung KW (2001) FtsZ ring formation at the chloroplast division site in plants. J Cell Biol 153:111-119
    • (2001) J Cell Biol , vol.153 , pp. 111-119
    • Vitha, S.1    McAndrew, R.S.2    Osteryoung, K.W.3
  • 102
    • 0024322748 scopus 로고
    • Organization of the genes encoding (Fe) hydrogenase in Desulfovibrio vulgaris
    • Voordouw G, Strang JD, Wilson FR (1989) Organization of the genes encoding (Fe) hydrogenase in Desulfovibrio vulgaris. J Bacteriol 171:3881-3889
    • (1989) J Bacteriol , vol.171 , pp. 3881-3889
    • Voordouw, G.1    Strang, J.D.2    Wilson, F.R.3
  • 104
    • 31444440257 scopus 로고    scopus 로고
    • Biochemistry of hydrogen metabolism in Chlamydomonas reinhardtii wild type and a Rubisco-less mutant
    • White AL, Melis A (2006) Biochemistry of hydrogen metabolism in Chlamydomonas reinhardtii wild type and a Rubisco-less mutant. Int J Hydrogen Energy 31:455-464
    • (2006) Int J Hydrogen Energy , vol.31 , pp. 455-464
    • White, A.L.1    Melis, A.2
  • 105
    • 0036827189 scopus 로고    scopus 로고
    • [Fe]-hydrogenases in green algae: Photo-fermentation and hydrogen evolution under sulfur deprivation
    • Winkler M, Hemschemeier A, Gotor C, Melis A, Happe T (2002) [Fe]-hydrogenases in green algae: photo-fermentation and hydrogen evolution under sulfur deprivation. Intl J Hydrogen Energy 27:1431-1439
    • (2002) Intl J Hydrogen Energy , vol.27 , pp. 1431-1439
    • Winkler, M.1    Hemschemeier, A.2    Gotor, C.3    Melis, A.4    Happe, T.5
  • 106
    • 0035078604 scopus 로고    scopus 로고
    • Molecular evidence for a [Fe]-hydrogenase in the green alga Scenedesmus obliquus
    • Wünschiers R, Stangier K, Senger H, Schulz R (2001a) Molecular evidence for a [Fe]-hydrogenase in the green alga Scenedesmus obliquus. Curr Microbiol 42:353-360
    • (2001) Curr Microbiol , vol.42 , pp. 353-360
    • Wünschiers, R.1    Stangier, K.2    Senger, H.3    Schulz, R.4
  • 107
    • 0035910671 scopus 로고    scopus 로고
    • Electron pathways involved in H-2-metabolism in the green alga Scenedesmus obliquus
    • Wünschiers R, Senger H, Schulz R (2001b) Electron pathways involved in H-2-metabolism in the green alga Scenedesmus obliquus. Biochim Biophys Acta 1503:271-278
    • (2001) Biochim Biophys Acta , vol.1503 , pp. 271-278
    • Wünschiers, R.1    Senger, H.2    Schulz, R.3
  • 108
    • 0032068061 scopus 로고    scopus 로고
    • The regulation of photosynthetic electron-transport during nutrient deprivation in Chlamydomonas reinhardtii
    • Wykoff DD, Davies JP, Melis A, Grossman AR (1998) The regulation of photosynthetic electron-transport during nutrient deprivation in Chlamydomonas reinhardtii. Plant Physiol 117:129-139
    • (1998) Plant Physiol , vol.117 , pp. 129-139
    • Wykoff, D.D.1    Davies, J.P.2    Melis, A.3    Grossman, A.R.4
  • 109
    • 0027966651 scopus 로고
    • Characterization of sulfate transport in Chlamydomonas reinhardtii during sulfur-limited and sulfur-sufficient growth
    • Yildiz FH, Davies JP, Grossman AR (1994) Characterization of sulfate transport in Chlamydomonas reinhardtii during sulfur-limited and sulfur-sufficient growth. Plant Physiol 104:981-987
    • (1994) Plant Physiol , vol.104 , pp. 981-987
    • Yildiz, F.H.1    Davies, J.P.2    Grossman, A.R.3
  • 111
    • 18644374880 scopus 로고    scopus 로고
    • Probing green algal hydrogen production
    • Zhang L, Melis A (2002) Probing green algal hydrogen production. Phil Trans R Soc Lond Biol Sci 357:1499-1509
    • (2002) Phil Trans R Soc Lond Biol Sci , vol.357 , pp. 1499-1509
    • Zhang, L.1    Melis, A.2
  • 112
    • 0036481398 scopus 로고    scopus 로고
    • 2-producing Chlamydomonas reinhardtii (green alga)
    • 2-producing Chlamydomonas reinhardtii (green alga). Planta 214:552-561
    • (2002) Planta , vol.214 , pp. 552-561
    • Zhang, L.1    Happe, T.2    Melis, A.3
  • 113
    • 6344221872 scopus 로고    scopus 로고
    • Insights into the survival of Chlamydomonas reinhardtii during sulfur starvation based on microarray analysis of gene expression
    • Zhang ZD, Shrager J, Jain M, Chang CW, Vallon O, Grossman AR (2004) Insights into the survival of Chlamydomonas reinhardtii during sulfur starvation based on microarray analysis of gene expression. Eukaryotic Cell 3:1331-1348
    • (2004) Eukaryotic Cell , vol.3 , pp. 1331-1348
    • Zhang, Z.D.1    Shrager, J.2    Jain, M.3    Chang, C.W.4    Vallon, O.5    Grossman, A.R.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.