메뉴 건너뛰기




Volumn 75, Issue , 2011, Pages 71-110

Solar-driven hydrogen production in green algae

Author keywords

Algae; Chlamydomonas; Hydrogen; Renewable energy; Solar power

Indexed keywords

ACETIC ACID; ANTIMYCIN A1; FERREDOXIN; HYDROGEN; METAL; OXYGEN; PROTON; PYRUVIC ACID; STARCH; SULFUR; HYDROGENASE;

EID: 79960908002     PISSN: 00652164     EISSN: None     Source Type: Book Series    
DOI: 10.1016/B978-0-12-387046-9.00004-9     Document Type: Chapter
Times cited : (43)

References (224)
  • 1
    • 0025000128 scopus 로고
    • The structure and mechanism of iron-hydrogenases
    • Adams M.W. The structure and mechanism of iron-hydrogenases. Biochim. Biophys. Acta 1990, 1020:115-145.
    • (1990) Biochim. Biophys. Acta , vol.1020 , pp. 115-145
    • Adams, M.W.1
  • 2
    • 0036827173 scopus 로고    scopus 로고
    • Photobiological hydrogen production: Photochemical efficiency and bioreactor design
    • Akkerman I., Janssen M., Rocha J., Wijffels R.H. Photobiological hydrogen production: Photochemical efficiency and bioreactor design. Int. J. Hydrogen Energy 2002, 27:1195-1208.
    • (2002) Int. J. Hydrogen Energy , vol.27 , pp. 1195-1208
    • Akkerman, I.1    Janssen, M.2    Rocha, J.3    Wijffels, R.H.4
  • 5
    • 71849095917 scopus 로고    scopus 로고
    • Relationships between H2 photoproduction and different electron transport pathways in sulfur-deprived Chlamydomonas reinhardtii
    • Antal T.K., Volgusheva A.A., Kukarskih G.P., Krendeleva T.E., Rubin A.B. Relationships between H2 photoproduction and different electron transport pathways in sulfur-deprived Chlamydomonas reinhardtii. Int. J. Hydrogen Energy 2009, 34:9087-9094.
    • (2009) Int. J. Hydrogen Energy , vol.34 , pp. 9087-9094
    • Antal, T.K.1    Volgusheva, A.A.2    Kukarskih, G.P.3    Krendeleva, T.E.4    Rubin, A.B.5
  • 6
    • 0033621284 scopus 로고    scopus 로고
    • A large scale structural analysis of cDNAs in a unicellular green alga, Chlamydomonas reinhardtii. I. Generation of 3433 non-redundant expressed sequence tags
    • Asamizu E., Nakamura Y., Sato S., Fukuzawa H., Tabata S. A large scale structural analysis of cDNAs in a unicellular green alga, Chlamydomonas reinhardtii. I. Generation of 3433 non-redundant expressed sequence tags. DNA Res. 1999, 6:369-373.
    • (1999) DNA Res. , vol.6 , pp. 369-373
    • Asamizu, E.1    Nakamura, Y.2    Sato, S.3    Fukuzawa, H.4    Tabata, S.5
  • 9
    • 66749108480 scopus 로고    scopus 로고
    • A proteomic survey of Chlamydomonas reinhardtii mitochondria sheds new light on the metabolic plasticity of the organelle and on the nature of the α-proteobacterial mitochondrial ancestor
    • Atteia A., Adrait A., Brugière S., Tardif M., van Lis R., Deusch O., Dagan T., Kuhn L., Gontero B., Martin W., Garin J., Joyard J., et al. A proteomic survey of Chlamydomonas reinhardtii mitochondria sheds new light on the metabolic plasticity of the organelle and on the nature of the α-proteobacterial mitochondrial ancestor. Mol. Biol. Evol. 2009, 26:1533-1548.
    • (2009) Mol. Biol. Evol. , vol.26 , pp. 1533-1548
    • Atteia, A.1    Adrait, A.2    Brugière, S.3    Tardif, M.4    van Lis, R.5    Deusch, O.6    Dagan, T.7    Kuhn, L.8    Gontero, B.9    Martin, W.10    Garin, J.11    Joyard, J.12
  • 10
    • 0001914508 scopus 로고
    • Physiology of starch storage in the monocellular alga Chlamydomonas reinhardtii
    • Ball S.G., Dirick L., Decq A., Martiat J.-C., Matagne R. Physiology of starch storage in the monocellular alga Chlamydomonas reinhardtii. Plant Sci. 1990, 66:1-9.
    • (1990) Plant Sci. , vol.66 , pp. 1-9
    • Ball, S.G.1    Dirick, L.2    Decq, A.3    Martiat, J.-C.4    Matagne, R.5
  • 11
    • 0001027763 scopus 로고
    • H2 and CO2 evolution by anaerobically adapted Chlamydomonas reinhardtii F-60
    • Bamberger E.S., King D., Erbes D.L., Gibbs M. H2 and CO2 evolution by anaerobically adapted Chlamydomonas reinhardtii F-60. Plant Physiol. 1982, 69:1268-1273.
    • (1982) Plant Physiol. , vol.69 , pp. 1268-1273
    • Bamberger, E.S.1    King, D.2    Erbes, D.L.3    Gibbs, M.4
  • 12
    • 78651475398 scopus 로고    scopus 로고
    • High rates of photobiological H2 production by a cyanobacterium under aerobic conditions
    • Bandyopadhyay A., Stöckel J., Min H., Sherman L.A., Pakrasi H.B. High rates of photobiological H2 production by a cyanobacterium under aerobic conditions. Nat. Commun. 2010, 1:139.
    • (2010) Nat. Commun. , vol.1 , pp. 139
    • Bandyopadhyay, A.1    Stöckel, J.2    Min, H.3    Sherman, L.A.4    Pakrasi, H.B.5
  • 13
    • 77955564513 scopus 로고    scopus 로고
    • An economic survey of hydrogen production from conventional and alternative energy sources
    • Bartels J.R., Pate M.B., Olson N.K. An economic survey of hydrogen production from conventional and alternative energy sources. Int. J. Hydrogen Energy 2010, 35:8371-8384.
    • (2010) Int. J. Hydrogen Energy , vol.35 , pp. 8371-8384
    • Bartels, J.R.1    Pate, M.B.2    Olson, N.K.3
  • 14
    • 67349200011 scopus 로고    scopus 로고
    • Improvement of light to biomass conversion by de-regulation of light-harvesting protein translation in Chlamydomonas reinhardtii
    • Beckmann J., Lehr F., Finazzi G., Hankamer B., Posten C., Wobbe L., Kruse O. Improvement of light to biomass conversion by de-regulation of light-harvesting protein translation in Chlamydomonas reinhardtii. J. Biotechnol. 2009, 142:70-77.
    • (2009) J. Biotechnol. , vol.142 , pp. 70-77
    • Beckmann, J.1    Lehr, F.2    Finazzi, G.3    Hankamer, B.4    Posten, C.5    Wobbe, L.6    Kruse, O.7
  • 16
    • 0002547744 scopus 로고
    • H2 metabolism in photosynthetic organisms: I. Dark H2 evolution and uptake by algae and mosses
    • Ben-Amotz A., Erbes D.L., Riederer-Henderson M.A., Peavey D.G., Gibbs M. H2 metabolism in photosynthetic organisms: I. Dark H2 evolution and uptake by algae and mosses. Plant Physiol. 1975, 56:72-77.
    • (1975) Plant Physiol. , vol.56 , pp. 72-77
    • Ben-Amotz, A.1    Erbes, D.L.2    Riederer-Henderson, M.A.3    Peavey, D.G.4    Gibbs, M.5
  • 17
    • 0029763232 scopus 로고    scopus 로고
    • Hydrogen biotechnology: Progress and prospects
    • Benemann J. Hydrogen biotechnology: Progress and prospects. Nat. Biotech. 1996, 14:1101-1103.
    • (1996) Nat. Biotech. , vol.14 , pp. 1101-1103
    • Benemann, J.1
  • 18
    • 84954358493 scopus 로고    scopus 로고
    • Radiation characteristics of Chlamydomonas reinhardtii CC125 and its truncated chlorophyll antenna transformants tla1, tlaX and tla1-CW+
    • Berberoglu H., Pilon L., Melis A. Radiation characteristics of Chlamydomonas reinhardtii CC125 and its truncated chlorophyll antenna transformants tla1, tlaX and tla1-CW+. Int. J. Hydrogen Energy 2008, 33:6467-6483.
    • (2008) Int. J. Hydrogen Energy , vol.33 , pp. 6467-6483
    • Berberoglu, H.1    Pilon, L.2    Melis, A.3
  • 19
    • 38049071594 scopus 로고    scopus 로고
    • A hydrogen economy and its impact on the world as we know it
    • Blanchette S. A hydrogen economy and its impact on the world as we know it. Energy Pol. 2008, 36:522-530.
    • (2008) Energy Pol. , vol.36 , pp. 522-530
    • Blanchette, S.1
  • 20
    • 0033034325 scopus 로고    scopus 로고
    • Commercial production of microalgae: Ponds, tanks, tubes and fermenters
    • Borowitzka M.A. Commercial production of microalgae: Ponds, tanks, tubes and fermenters. J. Biotechnol. 1999, 70:313-321.
    • (1999) J. Biotechnol. , vol.70 , pp. 313-321
    • Borowitzka, M.A.1
  • 24
    • 33644852344 scopus 로고    scopus 로고
    • The [Fe-Fe]-hydrogenase maturation protein HydF from Thermotoga maritima is a GTPase with an iron-sulfur cluster
    • Brazzolotto X., Rubach J.K., Gaillard J., Gambarelli S., Atta M., Fontecave M. The [Fe-Fe]-hydrogenase maturation protein HydF from Thermotoga maritima is a GTPase with an iron-sulfur cluster. J. Biol. Chem. 2006, 281:769-774.
    • (2006) J. Biol. Chem. , vol.281 , pp. 769-774
    • Brazzolotto, X.1    Rubach, J.K.2    Gaillard, J.3    Gambarelli, S.4    Atta, M.5    Fontecave, M.6
  • 25
    • 0026058315 scopus 로고
    • Introduction of exogenous DNA into Chlamydomonas reinhardtii by electroporation
    • Brown L.E., Sprecher S.L., Keller L.R. Introduction of exogenous DNA into Chlamydomonas reinhardtii by electroporation. Mol. Cell. Biol. 1991, 11:2328-2332.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 2328-2332
    • Brown, L.E.1    Sprecher, S.L.2    Keller, L.R.3
  • 27
    • 33845531710 scopus 로고    scopus 로고
    • Microalgal reactors: A review of enclosed system designs and performances
    • Carvalho A.P., Meireles L.A., Malcata F.X. Microalgal reactors: A review of enclosed system designs and performances. Biotechnol. Prog. 2006, 22:1490-1506.
    • (2006) Biotechnol. Prog. , vol.22 , pp. 1490-1506
    • Carvalho, A.P.1    Meireles, L.A.2    Malcata, F.X.3
  • 28
    • 36049005713 scopus 로고    scopus 로고
    • Atomic resolution modeling of the ferredoxin:[FeFe] hydrogenase complex from Chlamydomonas reinhardtii
    • Chang C.H., King P.W., Ghirardi M.L., Kim K. Atomic resolution modeling of the ferredoxin:[FeFe] hydrogenase complex from Chlamydomonas reinhardtii. Biophys. J. 2007, 93:3034-3045.
    • (2007) Biophys. J. , vol.93 , pp. 3034-3045
    • Chang, C.H.1    King, P.W.2    Ghirardi, M.L.3    Kim, K.4
  • 29
    • 0024039934 scopus 로고
    • Reduced CO2/O2 specificity of ribulose-bisphosphate carboxylase/oxygenase in a temperature-sensitive chloroplast mutant of Chlamydomonas
    • Chen Z.X., Chastain C.J., Al-Abed S.R., Chollet R., Spreitzer R.J. Reduced CO2/O2 specificity of ribulose-bisphosphate carboxylase/oxygenase in a temperature-sensitive chloroplast mutant of Chlamydomonas. Proc. Natl. Acad. Sci. USA 1988, 85:4696-4699.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 4696-4699
    • Chen, Z.X.1    Chastain, C.J.2    Al-Abed, S.R.3    Chollet, R.4    Spreitzer, R.J.5
  • 30
    • 23444454349 scopus 로고    scopus 로고
    • Role of SulP, a nuclear-encoded chloroplast sulfate permease, in sulfate transport and H2 evolution in Chlamydomonas reinhardtii
    • Chen H.-C., Newton A.J., Melis A. Role of SulP, a nuclear-encoded chloroplast sulfate permease, in sulfate transport and H2 evolution in Chlamydomonas reinhardtii. Photosynth. Res. 2005, 84:289-296.
    • (2005) Photosynth. Res. , vol.84 , pp. 289-296
    • Chen, H.-C.1    Newton, A.J.2    Melis, A.3
  • 32
    • 79960899927 scopus 로고    scopus 로고
    • Hydrogen production in Chlamydomonas: PSII-dependent and independent pathways differ in their requirement on starch metabolism
    • Chochois V., Dauvillee D., Beyly A., Tolleter D., Cuine S., Timpano H., Ball S., Cournac L., Peltier G. Hydrogen production in Chlamydomonas: PSII-dependent and independent pathways differ in their requirement on starch metabolism. Plant Physiol. 2009, 151:613-640.
    • (2009) Plant Physiol. , vol.151 , pp. 613-640
    • Chochois, V.1    Dauvillee, D.2    Beyly, A.3    Tolleter, D.4    Cuine, S.5    Timpano, H.6    Ball, S.7    Cournac, L.8    Peltier, G.9
  • 33
    • 77957278521 scopus 로고    scopus 로고
    • Relationships between PSII-independent hydrogen bioproduction and starch metabolism as evidenced from isolation of starch catabolism mutants in the green alga Chlamydomonas reinhardtii
    • Chochois V., Constans L., Dauvillée D., Beyly A., Solivérès M., Ball S., Peltier G., Cournac L. Relationships between PSII-independent hydrogen bioproduction and starch metabolism as evidenced from isolation of starch catabolism mutants in the green alga Chlamydomonas reinhardtii. Int. J. Hydrogen Energy 2010, 35:10731-10740.
    • (2010) Int. J. Hydrogen Energy , vol.35 , pp. 10731-10740
    • Chochois, V.1    Constans, L.2    Dauvillée, D.3    Beyly, A.4    Solivérès, M.5    Ball, S.6    Peltier, G.7    Cournac, L.8
  • 35
    • 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. Limiting steps of hydrogen production in Chlamydomonas reinhardtii and Synechocystis PCC 6803 as analysed by light-induced gas exchange transients. Int. J. Hydrogen Energy 2002, 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
  • 37
  • 38
    • 68349152509 scopus 로고    scopus 로고
    • Advances in biohydrogen production processes: An approach towards commercialization
    • Das D. Advances in biohydrogen production processes: An approach towards commercialization. Int. J. Hydrogen Energy 2009, 34:7349-7357.
    • (2009) Int. J. Hydrogen Energy , vol.34 , pp. 7349-7357
    • Das, D.1
  • 39
    • 77957252570 scopus 로고    scopus 로고
    • Recent trends on the development of photobiological processes and photobioreactors for the improvement of hydrogen production
    • Dasgupta C.N., Jose Gilbert J., Lindblad P., Heidorn T., Borgvang S.A., Skjanes K., Das D. Recent trends on the development of photobiological processes and photobioreactors for the improvement of hydrogen production. Int. J. Hydrogen Energy 2010, 35:10218-10238.
    • (2010) Int. J. Hydrogen Energy , vol.35 , pp. 10218-10238
    • Dasgupta, C.N.1    Jose Gilbert, J.2    Lindblad, P.3    Heidorn, T.4    Borgvang, S.A.5    Skjanes, K.6    Das, D.7
  • 40
    • 0024743663 scopus 로고
    • The argininosuccinate lyase gene of Chlamydomonas reinhardtii: An important tool for nuclear transformation and for correlating the genetic and molecular maps of the ARG7 locus
    • Debuchy R., Purton S., Rochaix J.D. The argininosuccinate lyase gene of Chlamydomonas reinhardtii: An important tool for nuclear transformation and for correlating the genetic and molecular maps of the ARG7 locus. EMBO J. 1989, 8:2803-2809.
    • (1989) EMBO J. , vol.8 , pp. 2803-2809
    • Debuchy, R.1    Purton, S.2    Rochaix, J.D.3
  • 41
    • 0037423885 scopus 로고    scopus 로고
    • Role of chloroplast protein kinase Stt7 in LHCII phosphorylation and state transition in Chlamydomonas
    • Depège N., Bellafiore S., Rochaix J.-D. Role of chloroplast protein kinase Stt7 in LHCII phosphorylation and state transition in Chlamydomonas. Science 2003, 299:1572-1575.
    • (2003) Science , vol.299 , pp. 1572-1575
    • Depège, N.1    Bellafiore, S.2    Rochaix, J.-D.3
  • 42
    • 63249099166 scopus 로고    scopus 로고
    • Characterization of Nda2, a plastoquinone-reducing type II NAD(P)H dehydrogenase in Chlamydomonas chloroplasts
    • Desplats C., Mus F., Cuine S., Billon E., Cournac L., Peltier G. Characterization of Nda2, a plastoquinone-reducing type II NAD(P)H dehydrogenase in Chlamydomonas chloroplasts. J. Biol. Chem. 2008, 284:4148-4157.
    • (2008) J. Biol. Chem. , vol.284 , pp. 4148-4157
    • Desplats, C.1    Mus, F.2    Cuine, S.3    Billon, E.4    Cournac, L.5    Peltier, G.6
  • 43
    • 34447277915 scopus 로고    scopus 로고
    • Functional integration of the HUP1 hexose symporter gene into the genome of C. reinhardtii: Impacts on biological H(2) production
    • Doebbe A., Rupprecht J., Beckmann J., Mussgnug J.H., Hallmann A., Hankamer B., Kruse O. Functional integration of the HUP1 hexose symporter gene into the genome of C. reinhardtii: Impacts on biological H(2) production. J. Biotechnol. 2007, 131:27-33.
    • (2007) J. Biotechnol. , vol.131 , pp. 27-33
    • Doebbe, A.1    Rupprecht, J.2    Beckmann, J.3    Mussgnug, J.H.4    Hallmann, A.5    Hankamer, B.6    Kruse, O.7
  • 44
    • 77956942339 scopus 로고    scopus 로고
    • The interplay of proton, electron and metabolite supply for photosynthetic H2 production in C. reinhardtii
    • Doebbe A., Keck M., La Russa M., Mussgnug J.H., Hankamer B., Tekce E., Niehaus K., Kruse O. The interplay of proton, electron and metabolite supply for photosynthetic H2 production in C. reinhardtii. J. Biol. Chem. 2010, 285:30247-30260.
    • (2010) J. Biol. Chem. , vol.285 , pp. 30247-30260
    • Doebbe, A.1    Keck, M.2    La Russa, M.3    Mussgnug, J.H.4    Hankamer, B.5    Tekce, E.6    Niehaus, K.7    Kruse, O.8
  • 45
    • 33244470640 scopus 로고    scopus 로고
    • Characterization of mitochondrial alternative NAD(P)H dehydrogenases in arabidopsis: Intraorganelle location and expression
    • Elhafez D., Murcha M.W., Clifton R., Soole K.L., Day D.A., Whelan J. Characterization of mitochondrial alternative NAD(P)H dehydrogenases in arabidopsis: Intraorganelle location and expression. Plant Cell Physiol. 2006, 47:43-54.
    • (2006) Plant Cell Physiol. , vol.47 , pp. 43-54
    • Elhafez, D.1    Murcha, M.W.2    Clifton, R.3    Soole, K.L.4    Day, D.A.5    Whelan, J.6
  • 46
    • 33750337726 scopus 로고    scopus 로고
    • Photosynthesis as a power supply for (bio-)hydrogen production
    • Esper B., Badura A., Rögner M. Photosynthesis as a power supply for (bio-)hydrogen production. Trends Plant Sci. 2006, 11:543-549.
    • (2006) Trends Plant Sci. , vol.11 , pp. 543-549
    • Esper, B.1    Badura, A.2    Rögner, M.3
  • 47
    • 77955291191 scopus 로고    scopus 로고
    • Phenotypic characterization and hydrogen production in Chlamydomonas reinhardtii QB-binding D1-protein mutants under sulphur starvation: Changes in Chl fluorescence and pigment composition
    • Faraloni C., Torzillo G. Phenotypic characterization and hydrogen production in Chlamydomonas reinhardtii QB-binding D1-protein mutants under sulphur starvation: Changes in Chl fluorescence and pigment composition. J. Phycol. 2010, 46:788-799.
    • (2010) J. Phycol. , vol.46 , pp. 788-799
    • Faraloni, C.1    Torzillo, G.2
  • 50
    • 0036208158 scopus 로고    scopus 로고
    • Involvement of state transitions in the switch between linear and cyclic electron flow in Chlamydomonas reinhardtii
    • Finazzi G., Rappaport F., Furia A., Fleischmann M., Rochaix J.D., Zito F., Forti G. Involvement of state transitions in the switch between linear and cyclic electron flow in Chlamydomonas reinhardtii. EMBO Rep. 2002, 3:280-285.
    • (2002) EMBO Rep. , vol.3 , pp. 280-285
    • Finazzi, G.1    Rappaport, F.2    Furia, A.3    Fleischmann, M.4    Rochaix, J.D.5    Zito, F.6    Forti, G.7
  • 52
    • 0000397742 scopus 로고
    • Reduction of CO2 with H2 in green plants
    • Gaffron H. Reduction of CO2 with H2 in green plants. Nature 1939, 143:204-205.
    • (1939) Nature , vol.143 , pp. 204-205
    • Gaffron, H.1
  • 53
    • 0343953574 scopus 로고    scopus 로고
    • Glutamate synthase from Chlamydomonas reinhardtii: Interaction studies with its substrate ferredoxin and molecular cloning
    • García-Sánchez M., Gotor C., Jacquot J.-P., Vega J. Glutamate synthase from Chlamydomonas reinhardtii: Interaction studies with its substrate ferredoxin and molecular cloning. Plant Soil 2000, 221:59-65.
    • (2000) Plant Soil , vol.221 , pp. 59-65
    • García-Sánchez, M.1    Gotor, C.2    Jacquot, J.-P.3    Vega, J.4
  • 54
    • 33745699777 scopus 로고    scopus 로고
    • Small-subunit cysteine-65 substitutions can suppress or induce alterations in the large-subunit catalytic efficiency and holoenzyme thermal stability of ribulose-1,5-bisphosphate carboxylase/oxygenase
    • Genkov T., Du Y.-C., Spreitzer R.J. Small-subunit cysteine-65 substitutions can suppress or induce alterations in the large-subunit catalytic efficiency and holoenzyme thermal stability of ribulose-1,5-bisphosphate carboxylase/oxygenase. Arch. Biochem. Biophys. 2006, 451:167-174.
    • (2006) Arch. Biochem. Biophys. , vol.451 , pp. 167-174
    • Genkov, T.1    Du, Y.-C.2    Spreitzer, R.J.3
  • 58
    • 69249095798 scopus 로고    scopus 로고
    • Interplay between light intensity, chlorophyll concentration and culture mixing on the hydrogen production in sulfur-deprived Chlamydomonas reinhardtii cultures grown in laboratory photobioreactors
    • Giannelli L., Scoma A., Torzillo G. Interplay between light intensity, chlorophyll concentration and culture mixing on the hydrogen production in sulfur-deprived Chlamydomonas reinhardtii cultures grown in laboratory photobioreactors. Biotechnol. Bioeng. 2009, 104:76-90.
    • (2009) Biotechnol. Bioeng. , vol.104 , pp. 76-90
    • Giannelli, L.1    Scoma, A.2    Torzillo, G.3
  • 59
    • 0035955213 scopus 로고    scopus 로고
    • Biomimetic hydrogen evolution catalyzed by an iron carbonyl thiolate
    • Gloaguen F.d.r., Lawrence J.D., Rauchfuss T.B. Biomimetic hydrogen evolution catalyzed by an iron carbonyl thiolate. J. Am. Chem. Soc. 2001, 123:9476-9477.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 9476-9477
    • Gloaguen, F.1    Lawrence, J.D.2    Rauchfuss, T.B.3
  • 60
    • 78049255865 scopus 로고    scopus 로고
    • RNA silencing of hydrogenase(-like) genes and investigation of their physiological roles in the green alga Chlamydomonas reinhardtii
    • Godman J.E., Molnár A., Baulcombe D.C., Balk J. RNA silencing of hydrogenase(-like) genes and investigation of their physiological roles in the green alga Chlamydomonas reinhardtii. Biochem. J. 2010, 431:345-351.
    • (2010) Biochem. J. , vol.431 , pp. 345-351
    • Godman, J.E.1    Molnár, A.2    Baulcombe, D.C.3    Balk, J.4
  • 62
    • 77955686486 scopus 로고    scopus 로고
    • RNA-Seq analysis of sulfur-deprived Chlamydomonas cells reveals aspects of acclimation critical for cell survival
    • Gonzalez-Ballester D., Casero D., Cokus S., Pellegrini M., Merchant S.S., Grossman A.R. RNA-Seq analysis of sulfur-deprived Chlamydomonas cells reveals aspects of acclimation critical for cell survival. Plant Cell 2010, 22:2058-2084.
    • (2010) Plant Cell , vol.22 , pp. 2058-2084
    • Gonzalez-Ballester, D.1    Casero, D.2    Cokus, S.3    Pellegrini, M.4    Merchant, S.S.5    Grossman, A.R.6
  • 64
    • 43949105847 scopus 로고    scopus 로고
    • Photosystem I/molecular wire/metal nanoparticle bioconjugates for the photocatalytic production of H2
    • Grimme R.A., Lubner C.E., Bryant D.A., Golbeck J.H. Photosystem I/molecular wire/metal nanoparticle bioconjugates for the photocatalytic production of H2. J. Am. Chem. Soc. 2008, 130:6308-6309.
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 6308-6309
    • Grimme, R.A.1    Lubner, C.E.2    Bryant, D.A.3    Golbeck, J.H.4
  • 68
    • 64749085304 scopus 로고    scopus 로고
    • Advances in fermentative biohydrogen production: The way forward?
    • Hallenbeck P.C., Ghosh D. Advances in fermentative biohydrogen production: The way forward?. Trends Biotechnol. 2010, 27:287-297.
    • (2010) Trends Biotechnol. , vol.27 , pp. 287-297
    • Hallenbeck, P.C.1    Ghosh, D.2
  • 70
    • 0036186921 scopus 로고    scopus 로고
    • Differential regulation of the Fe-hydrogenase during anaerobic adaptation in the green alga Chlamydomonas reinhardtii
    • Happe T., Kaminski A. Differential regulation of the Fe-hydrogenase during anaerobic adaptation in the green alga Chlamydomonas reinhardtii. Eur. J. Biochem. 2002, 269:1022-1032.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 1022-1032
    • Happe, T.1    Kaminski, A.2
  • 71
    • 0027153213 scopus 로고
    • Isolation, characterization and N-terminal amino acid sequence of hydrogenase from the green alga Chlamydomonas reinhardtii
    • Happe T., Naber J.D. Isolation, characterization and N-terminal amino acid sequence of hydrogenase from the green alga Chlamydomonas reinhardtii. Eur. J. Biochem. 1993, 214:475-481.
    • (1993) Eur. J. Biochem. , vol.214 , pp. 475-481
    • Happe, T.1    Naber, J.D.2
  • 72
    • 0010322340 scopus 로고
    • Hydrogen evolution by several algae
    • Healey F.P. Hydrogen evolution by several algae. Planta 1970, 91:220-226.
    • (1970) Planta , vol.91 , pp. 220-226
    • Healey, F.P.1
  • 73
    • 14644441716 scopus 로고    scopus 로고
    • The exceptional photofermentative hydrogen metabolism of the green alga Chlamydomonas reinhardtii
    • Hemschemeier A., Happe T. The exceptional photofermentative hydrogen metabolism of the green alga Chlamydomonas reinhardtii. Biochem. Soc. Trans. 2005, 33:39-41.
    • (2005) Biochem. Soc. Trans. , vol.33 , pp. 39-41
    • Hemschemeier, A.1    Happe, T.2
  • 74
    • 40949128266 scopus 로고    scopus 로고
    • Hydrogen production by Chlamydomonas reinhardtii: An elaborate interplay of electron sources and sinks
    • Hemschemeier A., Fouchard S., Cournac L., Peltier G., Happe T. Hydrogen production by Chlamydomonas reinhardtii: An elaborate interplay of electron sources and sinks. Planta 2008, 227:397-407.
    • (2008) Planta , vol.227 , pp. 397-407
    • Hemschemeier, A.1    Fouchard, S.2    Cournac, L.3    Peltier, G.4    Happe, T.5
  • 75
    • 40949115388 scopus 로고    scopus 로고
    • Biochemical and physiological characterization of the pyruvate formate-lyase Pfl1 of Chlamydomonas reinhardtii, a typically bacterial enzyme in a eukaryotic alga
    • Hemschemeier A., Jacobs J., Happe T. Biochemical and physiological characterization of the pyruvate formate-lyase Pfl1 of Chlamydomonas reinhardtii, a typically bacterial enzyme in a eukaryotic alga. Eukaryot. Cell 2008, 7:518-526.
    • (2008) Eukaryot. Cell , vol.7 , pp. 518-526
    • Hemschemeier, A.1    Jacobs, J.2    Happe, T.3
  • 76
    • 76149124197 scopus 로고    scopus 로고
    • Analytical approaches to photobiological hydrogen production in unicellular green algae
    • Hemschemeier A., Melis A., Happe T. Analytical approaches to photobiological hydrogen production in unicellular green algae. Photosynth. Res. 2009, 102:523-540.
    • (2009) Photosynth. Res. , vol.102 , pp. 523-540
    • Hemschemeier, A.1    Melis, A.2    Happe, T.3
  • 78
    • 3142546273 scopus 로고    scopus 로고
    • Toward an understanding of the mechanism of nonphotochemical quenching in green plants
    • Holt N.E., Fleming G.R., Niyogi K.K. Toward an understanding of the mechanism of nonphotochemical quenching in green plants. Biochemistry 2004, 43:8281-8289.
    • (2004) Biochemistry , vol.43 , pp. 8281-8289
    • Holt, N.E.1    Fleming, G.R.2    Niyogi, K.K.3
  • 79
    • 0011045854 scopus 로고
    • Anaerobic formation of d-lactate and partial purification and characterization of a pyruvate reductase from Chlamydomonas reinhardtii
    • Husic D.W., Tolbert N.E. Anaerobic formation of d-lactate and partial purification and characterization of a pyruvate reductase from Chlamydomonas reinhardtii. Plant Physiol. 1985, 78:277-284.
    • (1985) Plant Physiol. , vol.78 , pp. 277-284
    • Husic, D.W.1    Tolbert, N.E.2
  • 80
    • 34548125919 scopus 로고    scopus 로고
    • IEA, OECD/IEA, Paris
    • Key World Energy Statistics 2010, IEA, OECD/IEA, Paris. http://www.iea.org/textbase/nppdf/free/2010/key_stats_2010.pdf.
    • (2010) Key World Energy Statistics
  • 81
    • 77951622488 scopus 로고    scopus 로고
    • Isolation of the elusive supercomplex that drives cyclic electron flow in photosynthesis
    • Iwai M., Takizawa K., Tokutsu R., Okamuro A., Takahashi Y., Minagawa J. Isolation of the elusive supercomplex that drives cyclic electron flow in photosynthesis. Nature 2010, 464:1210-1213.
    • (2010) Nature , vol.464 , pp. 1210-1213
    • Iwai, M.1    Takizawa, K.2    Tokutsu, R.3    Okamuro, A.4    Takahashi, Y.5    Minagawa, J.6
  • 83
    • 58249096361 scopus 로고    scopus 로고
    • A novel, anaerobically induced ferredoxin in Chlamydomonas reinhardtii
    • Jacobs J., Pudollek S., Hemschemeier A., Happe T. A novel, anaerobically induced ferredoxin in Chlamydomonas reinhardtii. FEBS Lett. 2009, 583:325-329.
    • (2009) FEBS Lett. , vol.583 , pp. 325-329
    • Jacobs, J.1    Pudollek, S.2    Hemschemeier, A.3    Happe, T.4
  • 85
    • 0037454638 scopus 로고    scopus 로고
    • Enclosed outdoor photobioreactors: light regime, photosynthetic efficiency, scale-up and future prospects
    • Janssen M., Tramper J., Mur L.R., Wijffels R.H. Enclosed outdoor photobioreactors: light regime, photosynthetic efficiency, scale-up and future prospects. Biotechnol. Bioeng. 2003, 81:193-210.
    • (2003) Biotechnol. Bioeng. , vol.81 , pp. 193-210
    • Janssen, M.1    Tramper, J.2    Mur, L.R.3    Wijffels, R.H.4
  • 86
    • 33646019836 scopus 로고    scopus 로고
    • Modeling and optimization of photosynthetic hydrogen gas production by green alga Chlamydomonas reinhardtii in sulfur-deprived circumstance
    • Jo J.H., Lee D.S., Park J.M. Modeling and optimization of photosynthetic hydrogen gas production by green alga Chlamydomonas reinhardtii in sulfur-deprived circumstance. Biotechnol. Prog. 2006, 22:431-437.
    • (2006) Biotechnol. Prog. , vol.22 , pp. 431-437
    • Jo, J.H.1    Lee, D.S.2    Park, J.M.3
  • 87
    • 0033977854 scopus 로고    scopus 로고
    • Herbicide resistance and supersensitivity in Ala250 or Ala251 mutants of the D1 protein in Chlamydomonas reinhardtii
    • Johanningmeier U., Sopp G., Brauner M., Altenfeld U., Orawski G., Oettmeier W. Herbicide resistance and supersensitivity in Ala250 or Ala251 mutants of the D1 protein in Chlamydomonas reinhardtii. Pestic. Biochem. Physiol. 2000, 66:9-19.
    • (2000) Pestic. Biochem. Physiol. , vol.66 , pp. 9-19
    • Johanningmeier, U.1    Sopp, G.2    Brauner, M.3    Altenfeld, U.4    Orawski, G.5    Oettmeier, W.6
  • 89
    • 50149121231 scopus 로고    scopus 로고
    • In situ formation of an oxygen-evolving catalyst in neutral water containing phosphate and Co2+
    • Kanan M.W., Nocera D.G. In situ formation of an oxygen-evolving catalyst in neutral water containing phosphate and Co2+. Science 2008, 321:1072-1075.
    • (2008) Science , vol.321 , pp. 1072-1075
    • Kanan, M.W.1    Nocera, D.G.2
  • 90
    • 77954822316 scopus 로고    scopus 로고
    • Towards a super H2 producer: Improvements in photofermentative biohydrogen production by genetic manipulations
    • Kars G., Gündüz U. Towards a super H2 producer: Improvements in photofermentative biohydrogen production by genetic manipulations. Int. J. Hydrogen Energy 2010, 35:6646-6656.
    • (2010) Int. J. Hydrogen Energy , vol.35 , pp. 6646-6656
    • Kars, G.1    Gündüz, U.2
  • 91
    • 0000424706 scopus 로고
    • Nuclear and chloroplast transformation in Chlamydomonas reinhardtii: Strategies for genetic manipulation and gene expression
    • Kindle K., Sodeinde O. Nuclear and chloroplast transformation in Chlamydomonas reinhardtii: Strategies for genetic manipulation and gene expression. J. Appl. Phycol. 1994, 6:231-238.
    • (1994) J. Appl. Phycol. , vol.6 , pp. 231-238
    • Kindle, K.1    Sodeinde, O.2
  • 92
    • 0024791910 scopus 로고
    • Stable nuclear transformation of Chlamydomonas using the Chlamydomonas gene for nitrate reductase
    • Kindle K.L., Schnell R.A., Fernández E., Lefebvre P.A. Stable nuclear transformation of Chlamydomonas using the Chlamydomonas gene for nitrate reductase. J. Cell Biol. 1989, 109:2589-2601.
    • (1989) J. Cell Biol. , vol.109 , pp. 2589-2601
    • Kindle, K.L.1    Schnell, R.A.2    Fernández, E.3    Lefebvre, P.A.4
  • 93
    • 33644850541 scopus 로고    scopus 로고
    • Functional studies of [FeFe] hydrogenase maturation in an Escherichia coli biosynthetic system
    • King P.W., Posewitz M.C., Ghirardi M.L., Seibert M. Functional studies of [FeFe] hydrogenase maturation in an Escherichia coli biosynthetic system. J. Bacteriol. 2006, 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
  • 94
    • 0028696191 scopus 로고
    • A cDNA clone encoding a ferredoxin-NADP+ reductase from Chlamydomonas reinhardtii
    • Kitayama M., Kitayama K., Togasaki R.K. A cDNA clone encoding a ferredoxin-NADP+ reductase from Chlamydomonas reinhardtii. Plant Physiol. 1994, 106:1715-1716.
    • (1994) Plant Physiol. , vol.106 , pp. 1715-1716
    • Kitayama, M.1    Kitayama, K.2    Togasaki, R.K.3
  • 96
    • 58149218801 scopus 로고    scopus 로고
    • Hydrogen photoproduction by nutrient-deprived Chlamydomonas reinhardtii cells immobilized within thin alginate films under aerobic and anaerobic conditions
    • Kosourov S., Seibert M. Hydrogen photoproduction by nutrient-deprived Chlamydomonas reinhardtii cells immobilized within thin alginate films under aerobic and anaerobic conditions. Biotechnol. Bioeng. 2009, 102:50-58.
    • (2009) Biotechnol. Bioeng. , vol.102 , pp. 50-58
    • Kosourov, S.1    Seibert, M.2
  • 97
    • 0037199137 scopus 로고    scopus 로고
    • Sustained hydrogen photoproduction by Chlamydomonas reinhardtii: Effects of culture parameters
    • Kosourov S., Tsygankov A.A., Seibert M., Ghirardi M.L. Sustained hydrogen photoproduction by Chlamydomonas reinhardtii: Effects of culture parameters. Biotechnol. Bioeng. 2002, 78:731-740.
    • (2002) Biotechnol. Bioeng. , vol.78 , pp. 731-740
    • Kosourov, S.1    Tsygankov, A.A.2    Seibert, M.3    Ghirardi, M.L.4
  • 98
    • 0037330899 scopus 로고    scopus 로고
    • Effects of extracellular pH on the metabolic pathways in sulfur-deprived, H2-producing Chlamydomonas reinhardtii cultures
    • Kosourov S., Seibert M., Ghirardi M.L. Effects of extracellular pH on the metabolic pathways in sulfur-deprived, H2-producing Chlamydomonas reinhardtii cultures. Plant Cell Physiol. 2003, 44:146-155.
    • (2003) Plant Cell Physiol. , vol.44 , pp. 146-155
    • Kosourov, S.1    Seibert, M.2    Ghirardi, M.L.3
  • 99
    • 33847340991 scopus 로고    scopus 로고
    • A comparison of hydrogen photoproduction by sulfur-deprived Chlamydomonas reinhardtii under different growth conditions
    • Kosourov S., Patrusheva E., Ghirardi M.L., Seibert M., Tsygankov A. A comparison of hydrogen photoproduction by sulfur-deprived Chlamydomonas reinhardtii under different growth conditions. J. Biotechnol. 2007, 128:776-787.
    • (2007) J. Biotechnol. , vol.128 , pp. 776-787
    • Kosourov, S.1    Patrusheva, E.2    Ghirardi, M.L.3    Seibert, M.4    Tsygankov, A.5
  • 100
    • 79551637766 scopus 로고    scopus 로고
    • A truncated antenna mutant of Chlamydomonas reinhardtii can produce more hydrogen than the parental strain
    • Kosourov S.N., Ghirardi M.L., Seibert M. A truncated antenna mutant of Chlamydomonas reinhardtii can produce more hydrogen than the parental strain. Int. J. Hydrogen Energy 2011, 36:2044-2048.
    • (2011) Int. J. Hydrogen Energy , vol.36 , pp. 2044-2048
    • Kosourov, S.N.1    Ghirardi, M.L.2    Seibert, M.3
  • 101
    • 0027385123 scopus 로고
    • The concerted reduction of the high- and low-potential chains of the bf complex by plastoquinol
    • Kramer D.M., Crofts A.R. The concerted reduction of the high- and low-potential chains of the bf complex by plastoquinol. Biochim. Biophys. Acta Bioenergy 1993, 1183:72-84.
    • (1993) Biochim. Biophys. Acta Bioenergy , vol.1183 , pp. 72-84
    • Kramer, D.M.1    Crofts, A.R.2
  • 102
    • 85017128117 scopus 로고
    • Subcellular distribution of pyruvate-degrading enzymes in Chlamydomonas reinhardtii studied by an improved protoplast fractionation procedure
    • Kreuzberg K., Klock G., Grobheiser D. Subcellular distribution of pyruvate-degrading enzymes in Chlamydomonas reinhardtii studied by an improved protoplast fractionation procedure. Physiol. Plantarum 1987, 69:481-488.
    • (1987) Physiol. Plantarum , vol.69 , pp. 481-488
    • Kreuzberg, K.1    Klock, G.2    Grobheiser, D.3
  • 106
    • 0033375901 scopus 로고    scopus 로고
    • CO2-responsive transcriptional regulation of CAH1 encoding carbonic anhydrase is mediated by enhancer and silencer regions in Chlamydomonas reinhardtii
    • Kucho K.-i., Ohyama K., Fukuzawa H. CO2-responsive transcriptional regulation of CAH1 encoding carbonic anhydrase is mediated by enhancer and silencer regions in Chlamydomonas reinhardtii. Plant Physiol. 1999, 121:1329-1337.
    • (1999) Plant Physiol. , vol.121 , pp. 1329-1337
    • Kucho, K.-I.1    Ohyama, K.2    Fukuzawa, H.3
  • 107
    • 78149238653 scopus 로고    scopus 로고
    • The anaerobic expression of the ferredoxin encoding FDX5 gene of Chlamydomonas reinhardtii is regulated by the Crr1 transcription factor
    • Lambertz C., Hemschemeier A., Happe T. The anaerobic expression of the ferredoxin encoding FDX5 gene of Chlamydomonas reinhardtii is regulated by the Crr1 transcription factor. Eukaryot. Cell 2010, 9:1747-1754.
    • (2010) Eukaryot. Cell , vol.9 , pp. 1747-1754
    • Lambertz, C.1    Hemschemeier, A.2    Happe, T.3
  • 108
    • 2642606979 scopus 로고    scopus 로고
    • Biophysical, biochemical, and physiological characterization of Chlamydomonas reinhardtii mutants with amino acid substitutions at the Ala251 residue in the D1 protein that result in varying levels of photosynthetic competence
    • Lardans A., Förster B., Pràsil O., Falkowski P.G., Sobolev V., Edelman M., Osmond C.B., Gillham N.W., Boynton J.E. Biophysical, biochemical, and physiological characterization of Chlamydomonas reinhardtii mutants with amino acid substitutions at the Ala251 residue in the D1 protein that result in varying levels of photosynthetic competence. J. Biol. Chem. 1998, 273:11082-11091.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11082-11091
    • Lardans, A.1    Förster, B.2    Pràsil, O.3    Falkowski, P.G.4    Sobolev, V.5    Edelman, M.6    Osmond, C.B.7    Gillham, N.W.8    Boynton, J.E.9
  • 109
    • 35348839857 scopus 로고    scopus 로고
    • Transition to hydrogen economy in the United States: A 2006 status report
    • Lattin W.C., Utgikar V.P. Transition to hydrogen economy in the United States: A 2006 status report. Int. J. Hydrogen Energy 2007, 32:3230-3237.
    • (2007) Int. J. Hydrogen Energy , vol.32 , pp. 3230-3237
    • Lattin, W.C.1    Utgikar, V.P.2
  • 110
    • 4644293940 scopus 로고    scopus 로고
    • The effect of light intensity on hydrogen production by sulfur-deprived Chlamydomonas reinhardtii
    • Laurinavichene T., Tolstygina I., Tsygankov A. The effect of light intensity on hydrogen production by sulfur-deprived Chlamydomonas reinhardtii. J. Biotechnol. 2004, 114:143-151.
    • (2004) J. Biotechnol. , vol.114 , pp. 143-151
    • Laurinavichene, T.1    Tolstygina, I.2    Tsygankov, A.3
  • 111
    • 31944437818 scopus 로고    scopus 로고
    • Demonstration of sustained hydrogen photoproduction by immobilized, sulfur-deprived Chlamydomonas reinhardtii cells
    • Laurinavichene T.V., Fedorov A.S., Ghirardi M.L., Seibert M., Tsygankov A.A. Demonstration of sustained hydrogen photoproduction by immobilized, sulfur-deprived Chlamydomonas reinhardtii cells. Int. J. Hydrogen Energy 2006, 31:659-667.
    • (2006) Int. J. Hydrogen Energy , vol.31 , pp. 659-667
    • Laurinavichene, T.V.1    Fedorov, A.S.2    Ghirardi, M.L.3    Seibert, M.4    Tsygankov, A.A.5
  • 112
    • 0038078280 scopus 로고    scopus 로고
    • A new oxygen sensitivity and its potential application in photosynthetic H2 production
    • Lee J., Greenbaum E. A new oxygen sensitivity and its potential application in photosynthetic H2 production. Appl. Biochem. Biotechnol. 2003, 106:303-313.
    • (2003) Appl. Biochem. Biotechnol. , vol.106 , pp. 303-313
    • Lee, J.1    Greenbaum, E.2
  • 114
    • 78650244316 scopus 로고    scopus 로고
    • State transitions at the crossroad of thylakoid signalling pathways
    • Lemeille S., Rochaix J.-D. State transitions at the crossroad of thylakoid signalling pathways. Photosynth. Res. 2010, 106:33-46.
    • (2010) Photosynth. Res. , vol.106 , pp. 33-46
    • Lemeille, S.1    Rochaix, J.-D.2
  • 115
    • 33750458683 scopus 로고    scopus 로고
    • Powering the planet: Chemical challenges in solar energy utilization
    • Lewis N.S., Nocera D.G. Powering the planet: Chemical challenges in solar energy utilization. Proc. Natl. Acad. Sci. USA 2006, 103:15729-15735.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 15729-15735
    • Lewis, N.S.1    Nocera, D.G.2
  • 117
    • 56049085376 scopus 로고    scopus 로고
    • Brownian dynamics and molecular dynamics study of the association between hydrogenase and ferredoxin from Chlamydomonas reinhardtii
    • Long H., Chang C.H., King P.W., Ghirardi M.L., Kim K. Brownian dynamics and molecular dynamics study of the association between hydrogenase and ferredoxin from Chlamydomonas reinhardtii. Biophys. J. 2008, 95:3753-3766.
    • (2008) Biophys. J. , vol.95 , pp. 3753-3766
    • Long, H.1    Chang, C.H.2    King, P.W.3    Ghirardi, M.L.4    Kim, K.5
  • 118
    • 0036836353 scopus 로고    scopus 로고
    • A brief look at three decades of research on cyanobacterial hydrogen evolution
    • Lopes Pinto F.A., Troshina O., Lindblad P. A brief look at three decades of research on cyanobacterial hydrogen evolution. Int. J. Hydrogen Energy 2002, 27:1209-1215.
    • (2002) Int. J. Hydrogen Energy , vol.27 , pp. 1209-1215
    • Lopes Pinto, F.A.1    Troshina, O.2    Lindblad, P.3
  • 122
    • 77956877147 scopus 로고    scopus 로고
    • Hydrogen production by Chlamydomonas reinhardtii revisited: Rubisco as a biotechnological target
    • Marín-Navarro J., Esquivel M., Moreno J. Hydrogen production by Chlamydomonas reinhardtii revisited: Rubisco as a biotechnological target. World J. Microbiol. Biotechnol. 2010, 26:1785-1793.
    • (2010) World J. Microbiol. Biotechnol. , vol.26 , pp. 1785-1793
    • Marín-Navarro, J.1    Esquivel, M.2    Moreno, J.3
  • 125
    • 0025253920 scopus 로고
    • Stable nuclear transformation of Chlamydomonas reinhardtii by using a C. reinhardtii gene as the selectable marker
    • Mayfield S.P., Kindle K.L. Stable nuclear transformation of Chlamydomonas reinhardtii by using a C. reinhardtii gene as the selectable marker. Proc. Natl. Acad. Sci. USA 1990, 87:2087-2091.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 2087-2091
    • Mayfield, S.P.1    Kindle, K.L.2
  • 126
    • 36549000191 scopus 로고    scopus 로고
    • Towards a sustainable hydrogen economy: A multi-criteria sustainability appraisal of competing hydrogen futures
    • McDowall W., Eames M. Towards a sustainable hydrogen economy: A multi-criteria sustainability appraisal of competing hydrogen futures. Int. J. Hydrogen Energy 2007, 32:4611-4626.
    • (2007) Int. J. Hydrogen Energy , vol.32 , pp. 4611-4626
    • McDowall, W.1    Eames, M.2
  • 128
    • 0036827174 scopus 로고    scopus 로고
    • Green alga hydrogen production: Progress, challenges and prospects
    • Melis A. Green alga hydrogen production: Progress, challenges and prospects. Int. J. Hydrogen Energy 2002, 27:1217-1228.
    • (2002) Int. J. Hydrogen Energy , vol.27 , pp. 1217-1228
    • Melis, A.1
  • 129
    • 34548528653 scopus 로고    scopus 로고
    • Photosynthetic H2 metabolism in Chlamydomonas reinhardtii (unicellular green algae)
    • Melis A. Photosynthetic H2 metabolism in Chlamydomonas reinhardtii (unicellular green algae). Planta 2007, 226:1075-1086.
    • (2007) Planta , vol.226 , pp. 1075-1086
    • Melis, A.1
  • 130
    • 67651115666 scopus 로고    scopus 로고
    • Solar energy conversion efficiencies in photosynthesis: Minimizing the chlorophyll antennae to maximize efficiency
    • Melis A. Solar energy conversion efficiencies in photosynthesis: Minimizing the chlorophyll antennae to maximize efficiency. Plant Sci. 2009, 177:272-280.
    • (2009) Plant Sci. , vol.177 , pp. 272-280
    • Melis, A.1
  • 131
    • 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 J. Dunaliella salina (Chlorophyta) with small chlorophyll antenna sizes exhibit higher photosynthetic productivities and photon use efficiencies than normally pigmented cells. J. Appl. Phycol. 1998, 10:515-525.
    • (1998) J. Appl. Phycol. , vol.10 , pp. 515-525
    • Melis, A.1    Neidhardt, J.2    Benemann, J.3
  • 132
    • 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 M.L., Seibert M. Sustained photobiological hydrogen gas production upon reversible inactivation of oxygen evolution in the green alga Chlamydomonas reinhardtii. Plant Physiol. 2000, 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
  • 135
    • 0142152465 scopus 로고    scopus 로고
    • Arabidopsis genes encoding mitochondrial type II NAD(P)H dehydrogenases have different evolutionary origin and show distinct responses to light
    • Michalecka A.M., Svensson A.S., Johansson F.I., Agius S.C., Johanson U., Brennicke A., Binder S., Rasmusson A.G. Arabidopsis genes encoding mitochondrial type II NAD(P)H dehydrogenases have different evolutionary origin and show distinct responses to light. Plant Physiol. 2003, 133:642-652.
    • (2003) Plant Physiol. , vol.133 , pp. 642-652
    • Michalecka, A.M.1    Svensson, A.S.2    Johansson, F.I.3    Agius, S.C.4    Johanson, U.5    Brennicke, A.6    Binder, S.7    Rasmusson, A.G.8
  • 136
    • 76049111244 scopus 로고    scopus 로고
    • Genetic and biochemical analysis of the TLA1 gene in Chlamydomonas reinhardtii
    • Mitra M., Melis A. Genetic and biochemical analysis of the TLA1 gene in Chlamydomonas reinhardtii. Planta 2010, 231:729-740.
    • (2010) Planta , vol.231 , pp. 729-740
    • Mitra, M.1    Melis, A.2
  • 140
    • 77955560889 scopus 로고    scopus 로고
    • Developments and perspectives of photobioreactors for biofuel production
    • Morweiser M., Kruse O., Hankamer B., Posten C. Developments and perspectives of photobioreactors for biofuel production. Appl. Microbiol. Biotechnol. 2010, 87:1291-1301.
    • (2010) Appl. Microbiol. Biotechnol. , vol.87 , pp. 1291-1301
    • Morweiser, M.1    Kruse, O.2    Hankamer, B.3    Posten, C.4
  • 142
    • 0037047381 scopus 로고    scopus 로고
    • PGR5 is involved in cyclic electron flow around photosystem I and is essential for photoprotection in Arabidopsis
    • Munekage Y., Hojo M., Meurer J., Endo T., Tasaka M., Shikanai T. PGR5 is involved in cyclic electron flow around photosystem I and is essential for photoprotection in Arabidopsis. Cell 2002, 110:361-371.
    • (2002) Cell , vol.110 , pp. 361-371
    • Munekage, Y.1    Hojo, M.2    Meurer, J.3    Endo, T.4    Tasaka, M.5    Shikanai, T.6
  • 143
    • 34548489862 scopus 로고    scopus 로고
    • Anaerobic acclimation in Chlamydomonas reinhardtii: Anoxic gene expression, hydrogenase induction, and metabolic pathways
    • Mus F., Dubini A., Seibert M., Posewitz M.C., Grossman A.R. Anaerobic acclimation in Chlamydomonas reinhardtii: Anoxic gene expression, hydrogenase induction, and metabolic pathways. J. Biol. Chem. 2007, 282:25475-25486.
    • (2007) J. Biol. Chem. , vol.282 , pp. 25475-25486
    • Mus, F.1    Dubini, A.2    Seibert, M.3    Posewitz, M.C.4    Grossman, A.R.5
  • 145
    • 77957332953 scopus 로고    scopus 로고
    • Microalgae as substrates for fermentative biogas production in a combined biorefinery concept
    • Mussgnug J.H., Klassen V., Schlüter A., Kruse O. Microalgae as substrates for fermentative biogas production in a combined biorefinery concept. J. Biotechnol. 2010, 150:51-56.
    • (2010) J. Biotechnol. , vol.150 , pp. 51-56
    • Mussgnug, J.H.1    Klassen, V.2    Schlüter, A.3    Kruse, O.4
  • 148
    • 34848843479 scopus 로고    scopus 로고
    • The role of PGR5 in the redox poising of photosynthetic electron transport
    • Nandha B., Finazzi G., Joliot P., Hald S., Johnson G.N. The role of PGR5 in the redox poising of photosynthetic electron transport. Biochim. Biophys. Acta 2007, 1767:1252-1259.
    • (2007) Biochim. Biophys. Acta , vol.1767 , pp. 1252-1259
    • Nandha, B.1    Finazzi, G.2    Joliot, P.3    Hald, S.4    Johnson, G.N.5
  • 149
    • 6944228870 scopus 로고    scopus 로고
    • Improvement of fermentative hydrogen production: Various approaches
    • Nath K., Das D. Improvement of fermentative hydrogen production: Various approaches. Appl. Microbiol. Biotechnol. 2004, 65:520-529.
    • (2004) Appl. Microbiol. Biotechnol. , vol.65 , pp. 520-529
    • Nath, K.1    Das, D.2
  • 152
    • 77956375190 scopus 로고    scopus 로고
    • Recent advances in understanding the assembly and repair of photosystem II
    • Nixon P.J., Michoux F., Yu J., Boehm M., Komenda J. Recent advances in understanding the assembly and repair of photosystem II. Ann. Bot. 2010, 106:1-16.
    • (2010) Ann. Bot. , vol.106 , pp. 1-16
    • Nixon, P.J.1    Michoux, F.2    Yu, J.3    Boehm, M.4    Komenda, J.5
  • 153
    • 0030940253 scopus 로고    scopus 로고
    • Expression of the arylsulphatase reporter gene under the control of the nit1 promoter in Chlamydomonas reinhardtii
    • Ohresser M., Matagne R.F., Loppes R. Expression of the arylsulphatase reporter gene under the control of the nit1 promoter in Chlamydomonas reinhardtii. Curr. Genet. 1997, 31:264-271.
    • (1997) Curr. Genet. , vol.31 , pp. 264-271
    • Ohresser, M.1    Matagne, R.F.2    Loppes, R.3
  • 154
    • 79451470159 scopus 로고    scopus 로고
    • Effect of light intensity and the light: Dark cycles on the long term hydrogen production of Chlamydomonas reinhardtii by batch cultures
    • Oncel S., Sukan F.V. Effect of light intensity and the light: Dark cycles on the long term hydrogen production of Chlamydomonas reinhardtii by batch cultures. Biomass Bioenergy 2011, 35:1066-1074.
    • (2011) Biomass Bioenergy , vol.35 , pp. 1066-1074
    • Oncel, S.1    Sukan, F.V.2
  • 155
    • 4544329387 scopus 로고    scopus 로고
    • A biomimetic pathway for hydrogen evolution from a model of the iron hydrogenase active site
    • Ott S., Kritikos M., Åkermark B., Sun L., Lomoth R. A biomimetic pathway for hydrogen evolution from a model of the iron hydrogenase active site. Angew. Chem. Int. Ed. 2004, 43:1006-1009.
    • (2004) Angew. Chem. Int. Ed. , vol.43 , pp. 1006-1009
    • Ott, S.1    Kritikos, M.2    Åkermark, B.3    Sun, L.4    Lomoth, R.5
  • 156
    • 78650242669 scopus 로고    scopus 로고
    • Auxiliary electron transport pathways in chloroplasts of microalgae
    • Peltier G., Tolleter D., Billon E., Cournac L. Auxiliary electron transport pathways in chloroplasts of microalgae. Photosynth. Res. 2010, 1-13.
    • (2010) Photosynth. Res. , pp. 1-13
    • Peltier, G.1    Tolleter, D.2    Billon, E.3    Cournac, L.4
  • 157
    • 0032804337 scopus 로고    scopus 로고
    • Structure and mechanism of iron-only hydrogenases
    • Peters J.W. Structure and mechanism of iron-only hydrogenases. Curr. Opin. Struct. Biol. 1999, 9:670-676.
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 670-676
    • Peters, J.W.1
  • 158
    • 0032483966 scopus 로고    scopus 로고
    • X-ray crystal structure of the Fe-only hydrogenase (CpI) from Clostridium pasteurianum to 1.8 angstrom resolution
    • Peters J.W., Lanzilotta W.N., Lemon B.J., Seefeldt L.C. X-ray crystal structure of the Fe-only hydrogenase (CpI) from Clostridium pasteurianum to 1.8 angstrom resolution. Science 1998, 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
  • 159
    • 70450227314 scopus 로고    scopus 로고
    • PGRL1 participates in iron-induced remodeling of the photosynthetic apparatus and in energy metabolism in Chlamydomonas reinhardtii
    • Petroutsos D., Terauchi A.M., Busch A., Hirschmann I., Merchant S.S., Finazzi G., Hippler M. PGRL1 participates in iron-induced remodeling of the photosynthetic apparatus and in energy metabolism in Chlamydomonas reinhardtii. J. Biol. Chem. 2009, 284:32770-32781.
    • (2009) J. Biol. Chem. , vol.284 , pp. 32770-32781
    • Petroutsos, D.1    Terauchi, A.M.2    Busch, A.3    Hirschmann, I.4    Merchant, S.S.5    Finazzi, G.6    Hippler, M.7
  • 160
    • 79955044664 scopus 로고    scopus 로고
    • A pyruvate formate lyase (PFL1) deficient Chlamydomonas reinhardtii strain provides evidence for a link between fermentation and hydrogen evolution in green algae
    • Philipps G., Krawietz D., Hemschemeier A., Happe T. A pyruvate formate lyase (PFL1) deficient Chlamydomonas reinhardtii strain provides evidence for a link between fermentation and hydrogen evolution in green algae. Plant J. 2011, 66:330-340.
    • (2011) Plant J. , vol.66 , pp. 330-340
    • Philipps, G.1    Krawietz, D.2    Hemschemeier, A.3    Happe, T.4
  • 161
    • 0036827176 scopus 로고    scopus 로고
    • Truncated chlorophyll antenna size of the photosystems-A practical method to improve microalgal productivity and hydrogen production in mass culture
    • Polle J.E.W., Kanakagiri S., Jin E., Masuda T., Melis A. Truncated chlorophyll antenna size of the photosystems-A practical method to improve microalgal productivity and hydrogen production in mass culture. Int. J. Hydrogen Energy 2002, 27:1257-1264.
    • (2002) Int. J. Hydrogen Energy , vol.27 , pp. 1257-1264
    • Polle, J.E.W.1    Kanakagiri, S.2    Jin, E.3    Masuda, T.4    Melis, A.5
  • 162
    • 0037596752 scopus 로고    scopus 로고
    • Tla1 DNA insertional transformant of the green alga Chlamydomonas reinhardtii with a truncated light-harvesting chlorophyll antenna size
    • Polle J.E.W., Kanakagiri S.-D., Melis A. tla1 DNA insertional transformant of the green alga Chlamydomonas reinhardtii with a truncated light-harvesting chlorophyll antenna size. Planta 2003, 217:49-59.
    • (2003) Planta , vol.217 , pp. 49-59
    • Polle, J.E.W.1    Kanakagiri, S.-D.2    Melis, A.3
  • 163
    • 77955679170 scopus 로고    scopus 로고
    • Identification and regulation of plasma membrane sulfate transporters in Chlamydomonas
    • Pootakham W., Gonzalez-Ballester D., Grossman A.R. Identification and regulation of plasma membrane sulfate transporters in Chlamydomonas. Plant Physiol. 2010, 153:1653-1668.
    • (2010) Plant Physiol. , vol.153 , pp. 1653-1668
    • Pootakham, W.1    Gonzalez-Ballester, D.2    Grossman, A.R.3
  • 164
    • 2942586665 scopus 로고    scopus 로고
    • Discovery of two novel radical S-adenosylmethionine proteins required for the assembly of an active [Fe] hydrogenase
    • Posewitz M.C., King P.W., Smolinski S.L., Zhang L., Seibert M., Ghirardi M.L. Discovery of two novel radical S-adenosylmethionine proteins required for the assembly of an active [Fe] hydrogenase. J. Biol. Chem. 2004, 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.4    Seibert, M.5    Ghirardi, M.L.6
  • 166
    • 69949190933 scopus 로고    scopus 로고
    • Design principles of photo-bioreactors for cultivation of microalgae
    • Posten C. Design principles of photo-bioreactors for cultivation of microalgae. Eng. Life Sci. 2009, 9:165-177.
    • (2009) Eng. Life Sci. , vol.9 , pp. 165-177
    • Posten, C.1
  • 167
    • 0034793942 scopus 로고    scopus 로고
    • Photobioreactors: Production systems for phototrophic microorganisms
    • Pulz
    • Photobioreactors: Production systems for phototrophic microorganisms. Appl. Microbiol. Biotechnol. 2001, 57:287-293. Pulz.
    • (2001) Appl. Microbiol. Biotechnol. , vol.57 , pp. 287-293
  • 168
    • 0031721060 scopus 로고    scopus 로고
    • Copper-responsive gene expression during adaptation to copper deficiency
    • Academic Press, San Diego, California, USA
    • Quinn J.M., Merchant S., Lee M. Copper-responsive gene expression during adaptation to copper deficiency. Methods in Enzymology 1998, 263-279. Academic Press, San Diego, California, USA.
    • (1998) Methods in Enzymology , pp. 263-279
    • Quinn, J.M.1    Merchant, S.2    Lee, M.3
  • 169
    • 0142184944 scopus 로고    scopus 로고
    • Copper response element and Crr1-dependent Ni2+-responsive promoter for induced. Reversible gene expression in Chlamydomonas reinhardtii
    • Quinn J.M., Kropat J., Merchant S. Copper response element and Crr1-dependent Ni2+-responsive promoter for induced. Reversible gene expression in Chlamydomonas reinhardtii. Eukaryot. Cell 2003, 2:995-1002.
    • (2003) Eukaryot. Cell , vol.2 , pp. 995-1002
    • Quinn, J.M.1    Kropat, J.2    Merchant, S.3
  • 170
    • 0027389081 scopus 로고
    • Further characterization of the respiratory deficient dum-1 mutation of Chlamydomonas reinhardtii and its use as a recipient for mitochondrial transformation
    • Randolph-Anderson B.L., Boynton J.E., Gillham N.W., Harris E.H., Johnson A.M., Dorthu M.P., Matagne R.F. Further characterization of the respiratory deficient dum-1 mutation of Chlamydomonas reinhardtii and its use as a recipient for mitochondrial transformation. Mol. Gen. Genet. 1993, 236:235-244.
    • (1993) Mol. Gen. Genet. , vol.236 , pp. 235-244
    • Randolph-Anderson, B.L.1    Boynton, J.E.2    Gillham, N.W.3    Harris, E.H.4    Johnson, A.M.5    Dorthu, M.P.6    Matagne, R.F.7
  • 172
    • 0028110631 scopus 로고
    • The cyclic electron pathways around photosystem I in Chlamydomonas reinhardtii as determined in vivo by photoacoustic measurements of energy storage
    • Ravenel J., Peltier G., Havaux M. The cyclic electron pathways around photosystem I in Chlamydomonas reinhardtii as determined in vivo by photoacoustic measurements of energy storage. Planta 1994, 193:251-259.
    • (1994) Planta , vol.193 , pp. 251-259
    • Ravenel, J.1    Peltier, G.2    Havaux, M.3
  • 173
    • 73249146231 scopus 로고    scopus 로고
    • Visible light-driven H2 production by hydrogenases attached to dye-sensitized TiO2 nanoparticles
    • Reisner E., Powell D.J., Cavazza C., Fontecilla-Camps J.C., Armstrong F.A. Visible light-driven H2 production by hydrogenases attached to dye-sensitized TiO2 nanoparticles. J. Am. Chem. Soc. 2009, 131:18457-18466.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 18457-18466
    • Reisner, E.1    Powell, D.J.2    Cavazza, C.3    Fontecilla-Camps, J.C.4    Armstrong, F.A.5
  • 174
    • 79651469425 scopus 로고    scopus 로고
    • Regulation of photosynthetic electron transport
    • Rochaix J.-D. Regulation of photosynthetic electron transport. Biochim. Biophys. Acta Bioenergy 2011, 1807:375-383.
    • (2011) Biochim. Biophys. Acta Bioenergy , vol.1807 , pp. 375-383
    • Rochaix, J.-D.1
  • 175
    • 8444222059 scopus 로고    scopus 로고
    • Tandem inverted repeat system for selection of effective transgenic RNAi strains in Chlamydomonas
    • Rohr J., Sarkar N., Balenger S., Jeong B., Cerutti H. Tandem inverted repeat system for selection of effective transgenic RNAi strains in Chlamydomonas. Plant J. 2004, 40:611-621.
    • (2004) Plant J. , vol.40 , pp. 611-621
    • Rohr, J.1    Sarkar, N.2    Balenger, S.3    Jeong, B.4    Cerutti, H.5
  • 176
    • 57849125414 scopus 로고    scopus 로고
    • D1-arginine257 mutants (R257E, K, and Q) of Chlamydomonas reinhardtii have a lowered QB redox potential: Analysis of thermoluminescence and fluorescence measurements
    • Rose S., Minagawa J., Seufferheld M., Padden S., Svensson B., Kolling D., Crofts A., Govindjee D1-arginine257 mutants (R257E, K, and Q) of Chlamydomonas reinhardtii have a lowered QB redox potential: Analysis of thermoluminescence and fluorescence measurements. Photosynth. Res. 2008, 98:449-468.
    • (2008) Photosynth. Res. , vol.98 , pp. 449-468
    • Rose, S.1    Minagawa, J.2    Seufferheld, M.3    Padden, S.4    Svensson, B.5    Kolling, D.6    Crofts, A.7    Govindjee8
  • 177
    • 24144494192 scopus 로고    scopus 로고
    • Biochemical characterization of the HydE and HydG iron-only hydrogenase maturation enzymes from Thermatoga maritima
    • Rubach J.K., Brazzolotto X., Gaillard J., Fontecave M. Biochemical characterization of the HydE and HydG iron-only hydrogenase maturation enzymes from Thermatoga maritima. FEBS Lett. 2005, 579:5055-5060.
    • (2005) FEBS Lett. , vol.579 , pp. 5055-5060
    • Rubach, J.K.1    Brazzolotto, X.2    Gaillard, J.3    Fontecave, M.4
  • 178
    • 55149105865 scopus 로고    scopus 로고
    • A novel screening protocol for the isolation of hydrogen producing Chlamydomonas reinhardtii strains
    • Ruhle T., Hemschemeier A., Melis A., Happe T. A novel screening protocol for the isolation of hydrogen producing Chlamydomonas reinhardtii strains. BMC Plant Biol. 2008, 8:107.
    • (2008) BMC Plant Biol. , vol.8 , pp. 107
    • Ruhle, T.1    Hemschemeier, A.2    Melis, A.3    Happe, T.4
  • 179
    • 34547546173 scopus 로고    scopus 로고
    • Chlororespiration and cyclic electron flow around PSI during photosynthesis and plant stress response
    • Rumeau D., Peltier G., Cournac L. Chlororespiration and cyclic electron flow around PSI during photosynthesis and plant stress response. Plant Cell Environ. 2007, 30:1041-1051.
    • (2007) Plant Cell Environ. , vol.30 , pp. 1041-1051
    • Rumeau, D.1    Peltier, G.2    Cournac, L.3
  • 181
    • 34247610894 scopus 로고    scopus 로고
    • Promoting R&D in photobiological hydrogen production utilizing mariculture-raised cyanobacteria
    • Sakurai H., Masukawa H. Promoting R&D in photobiological hydrogen production utilizing mariculture-raised cyanobacteria. Mar. Biotechnol. 2007, 9:128-145.
    • (2007) Mar. Biotechnol. , vol.9 , pp. 128-145
    • Sakurai, H.1    Masukawa, H.2
  • 182
    • 1842790680 scopus 로고    scopus 로고
    • Substitutions at the Asp-473 latch residue of Chlamydomonas ribulosebisphosphate carboxylase/oxygenase cause decreases in carboxylation efficiency and CO2/O2 specificity
    • Satagopan S., Spreitzer R.J. Substitutions at the Asp-473 latch residue of Chlamydomonas ribulosebisphosphate carboxylase/oxygenase cause decreases in carboxylation efficiency and CO2/O2 specificity. J. Biol. Chem. 2004, 279:14240-14244.
    • (2004) J. Biol. Chem. , vol.279 , pp. 14240-14244
    • Satagopan, S.1    Spreitzer, R.J.2
  • 183
    • 77956182394 scopus 로고    scopus 로고
    • An inducible artificial microRNA system for Chlamydomonas reinhardtii confirms a key role for heat shock factor 1 in regulating thermotolerance
    • Schmollinger S., Strenkert D., Schroda M. An inducible artificial microRNA system for Chlamydomonas reinhardtii confirms a key role for heat shock factor 1 in regulating thermotolerance. Curr. Genet. 2010, 56:383-389.
    • (2010) Curr. Genet. , vol.56 , pp. 383-389
    • Schmollinger, S.1    Strenkert, D.2    Schroda, M.3
  • 184
    • 0342680049 scopus 로고    scopus 로고
    • The HSP70A promoter as a tool for the improved expression of transgenes in Chlamydomonas
    • Schroda M., Blöcker D., Beck C.F. The HSP70A promoter as a tool for the improved expression of transgenes in Chlamydomonas. Plant J. 2000, 21:121-131.
    • (2000) Plant J. , vol.21 , pp. 121-131
    • Schroda, M.1    Blöcker, D.2    Beck, C.F.3
  • 187
    • 0031893765 scopus 로고    scopus 로고
    • High-efficiency transformation of Chlamydomonas reinhardtii by electroporation
    • Shimogawara K., Fujiwara S., Grossman A., Usuda H. High-efficiency transformation of Chlamydomonas reinhardtii by electroporation. Genetics 1998, 148:1821-1828.
    • (1998) Genetics , vol.148 , pp. 1821-1828
    • Shimogawara, K.1    Fujiwara, S.2    Grossman, A.3    Usuda, H.4
  • 189
    • 38849118423 scopus 로고    scopus 로고
    • H2 production from marine and freshwater species of green algae during sulfur deprivation and considerations for bioreactor design
    • Skjånes K., Knutsen G., Källqvist T., Lindblad P. H2 production from marine and freshwater species of green algae during sulfur deprivation and considerations for bioreactor design. Int. J. Hydrogen Energy 2008, 33:511-521.
    • (2008) Int. J. Hydrogen Energy , vol.33 , pp. 511-521
    • Skjånes, K.1    Knutsen, G.2    Källqvist, T.3    Lindblad, P.4
  • 190
    • 0035282866 scopus 로고    scopus 로고
    • Radical SAM, a novel protein superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms: Functional characterization using new analysis and information visualization methods
    • Sofia H.J., Chen G., Hetzler B.G., Reyes-Spindola J.F., Miller N.E. Radical SAM, a novel protein superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms: Functional characterization using new analysis and information visualization methods. Nucleic Acids Res. 2001, 29:1097-1106.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 1097-1106
    • Sofia, H.J.1    Chen, G.2    Hetzler, B.G.3    Reyes-Spindola, J.F.4    Miller, N.E.5
  • 191
    • 44649143352 scopus 로고    scopus 로고
    • Microalgal carbon-dioxide-concentrating mechanisms: Chlamydomonas inorganic carbon transporters
    • Spalding M.H. Microalgal carbon-dioxide-concentrating mechanisms: Chlamydomonas inorganic carbon transporters. J. Exp. Bot. 2008, 59:1463-1473.
    • (2008) J. Exp. Bot. , vol.59 , pp. 1463-1473
    • Spalding, M.H.1
  • 193
    • 77956418571 scopus 로고    scopus 로고
    • A cell-free microtiter plate screen for improved [FeFe] hydrogenases
    • Stapleton J.A., Swartz J.R. A cell-free microtiter plate screen for improved [FeFe] hydrogenases. PLoS ONE 2010, 5:e10554.
    • (2010) PLoS ONE , vol.5
    • Stapleton, J.A.1    Swartz, J.R.2
  • 196
    • 66649106058 scopus 로고    scopus 로고
    • The structure of the active site H-cluster of [FeFe] hydrogenase from the green alga Chlamydomonas reinhardtii studied by X-ray absorption spectroscopy
    • Stripp S., Sanganas O., Happe T., Haumann M. The structure of the active site H-cluster of [FeFe] hydrogenase from the green alga Chlamydomonas reinhardtii studied by X-ray absorption spectroscopy. Biochemistry 2009, 48:5042-5049.
    • (2009) Biochemistry , vol.48 , pp. 5042-5049
    • Stripp, S.1    Sanganas, O.2    Happe, T.3    Haumann, M.4
  • 198
    • 0001649666 scopus 로고
    • The mechanism of hydrogen photoproduction by several algae
    • Stuart T.S., Gaffron H. The mechanism of hydrogen photoproduction by several algae. Planta 1972, 106:101-112.
    • (1972) Planta , vol.106 , pp. 101-112
    • Stuart, T.S.1    Gaffron, H.2
  • 199
    • 36849055926 scopus 로고    scopus 로고
    • Potential for hydrogen production with inducible chloroplast gene expression in Chlamydomonas
    • Surzycki R., Cournac L., Peltier G., Rochaix J.-D. Potential for hydrogen production with inducible chloroplast gene expression in Chlamydomonas. Proc. Natl. Acad. Sci. USA 2007, 104:17548-17553.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 17548-17553
    • Surzycki, R.1    Cournac, L.2    Peltier, G.3    Rochaix, J.-D.4
  • 201
    • 77952825427 scopus 로고    scopus 로고
    • Characterizing the anaerobic response of Chlamydomonas reinhardtii by quantitative proteomics
    • Terashima M., Specht M., Naumann B., Hippler M. Characterizing the anaerobic response of Chlamydomonas reinhardtii by quantitative proteomics. Mol. Cell. Proteomics 2010, 9:1514-1532.
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 1514-1532
    • Terashima, M.1    Specht, M.2    Naumann, B.3    Hippler, M.4
  • 205
    • 60549098776 scopus 로고    scopus 로고
    • Hydrogen production by photoautotrophic sulfur-deprived Chlamydomonas reinhardtii pre-grown and incubated under high light
    • Tolstygina I.V., Antal T.K., Kosourov S.N., Krendeleva T.E., Rubin A.B., Tsygankov A.A. Hydrogen production by photoautotrophic sulfur-deprived Chlamydomonas reinhardtii pre-grown and incubated under high light. Biotechnol. Bioeng. 2009, 102:1055-1061.
    • (2009) Biotechnol. Bioeng. , vol.102 , pp. 1055-1061
    • Tolstygina, I.V.1    Antal, T.K.2    Kosourov, S.N.3    Krendeleva, T.E.4    Rubin, A.B.5    Tsygankov, A.A.6
  • 206
    • 65949117066 scopus 로고    scopus 로고
    • Increased hydrogen photoproduction by means of a sulfur-deprived Chlamydomonas reinhardtii D1 protein mutant
    • Torzillo G., Scoma A., Faraloni C., Ena A., Johanningmeier U. Increased hydrogen photoproduction by means of a sulfur-deprived Chlamydomonas reinhardtii D1 protein mutant. Int. J. Hydrogen Energy 2009, 34:4529-4536.
    • (2009) Int. J. Hydrogen Energy , vol.34 , pp. 4529-4536
    • Torzillo, G.1    Scoma, A.2    Faraloni, C.3    Ena, A.4    Johanningmeier, U.5
  • 207
    • 23044529283 scopus 로고    scopus 로고
    • Laboratory scale photobioreactors
    • Tsygankov A.A. Laboratory scale photobioreactors. Appl. Biochem. Microbiol. 2001, 37:333-341.
    • (2001) Appl. Biochem. Microbiol. , vol.37 , pp. 333-341
    • Tsygankov, A.A.1
  • 208
    • 0036836413 scopus 로고    scopus 로고
    • Hydrogen photoproduction under continuous illumination by sulfur-deprived, synchronous Chlamydomonas reinhardtii cultures
    • Tsygankov A.A., Kosourov S., Seibert M., Ghirardi M.L. Hydrogen photoproduction under continuous illumination by sulfur-deprived, synchronous Chlamydomonas reinhardtii cultures. Int. J. Hydrogen Energy 2002, 27:1239-1244.
    • (2002) Int. J. Hydrogen Energy , vol.27 , pp. 1239-1244
    • Tsygankov, A.A.1    Kosourov, S.2    Seibert, M.3    Ghirardi, M.L.4
  • 210
    • 40849088189 scopus 로고    scopus 로고
    • Photobioreactors for mass cultivation of algae
    • Ugwu C.U., Aoyagi H., Uchiyama H. Photobioreactors for mass cultivation of algae. Biores. Technol. 2008, 99:4021-4028.
    • (2008) Biores. Technol. , vol.99 , pp. 4021-4028
    • Ugwu, C.U.1    Aoyagi, H.2    Uchiyama, H.3
  • 211
    • 36549058637 scopus 로고    scopus 로고
    • Effect of light intensity, wavelength and illumination protocol on hydrogen production in photobioreactors
    • Uyar B., Eroglu I., Yücel M., Gündüz U., Türker L. Effect of light intensity, wavelength and illumination protocol on hydrogen production in photobioreactors. Int. J. Hydrogen Energy 2007, 32:4670-4677.
    • (2007) Int. J. Hydrogen Energy , vol.32 , pp. 4670-4677
    • Uyar, B.1    Eroglu, I.2    Yücel, M.3    Gündüz, U.4    Türker, L.5
  • 212
    • 0027359351 scopus 로고
    • Mitochondrial DNA of Chlamydomonas reinhardtii: The structure of the ends of the linear 15.8-kb genome suggests mechanisms for DNA replication
    • Vahrenholz C., Riemen G., Pratje E., Dujon B., Michaelis G. Mitochondrial DNA of Chlamydomonas reinhardtii: The structure of the ends of the linear 15.8-kb genome suggests mechanisms for DNA replication. Curr. Genet. 1993, 24:241-247.
    • (1993) Curr. Genet. , vol.24 , pp. 241-247
    • Vahrenholz, C.1    Riemen, G.2    Pratje, E.3    Dujon, B.4    Michaelis, G.5
  • 215
    • 73649099860 scopus 로고    scopus 로고
    • Characterization of the key step for light-driven hydrogen evolution in green algae
    • Winkler M., Kuhlgert S., Hippler M., Happe T. Characterization of the key step for light-driven hydrogen evolution in green algae. J. Biol. Chem. 2009, 284:36620-36627.
    • (2009) J. Biol. Chem. , vol.284 , pp. 36620-36627
    • Winkler, M.1    Kuhlgert, S.2    Hippler, M.3    Happe, T.4
  • 216
    • 78149415409 scopus 로고    scopus 로고
    • Multiple ferredoxin isoforms in Chlamydomonas reinhardtii-Their role under stress conditions and biotechnological implications
    • Winkler M., Hemschemeier A., Jacobs J., Stripp S., Happe T. Multiple ferredoxin isoforms in Chlamydomonas reinhardtii-Their role under stress conditions and biotechnological implications. Eur. J. Cell Biol. 2010, 89:998-1004.
    • (2010) Eur. J. Cell Biol. , vol.89 , pp. 998-1004
    • Winkler, M.1    Hemschemeier, A.2    Jacobs, J.3    Stripp, S.4    Happe, T.5
  • 217
    • 77953956191 scopus 로고    scopus 로고
    • Improved hydrogen production with expression of hemH and lba genes in chloroplast of Chlamydomonas reinhardtii
    • Wu S., Huang R., Xu L., Yan G., Wang Q. Improved hydrogen production with expression of hemH and lba genes in chloroplast of Chlamydomonas reinhardtii. J. Biotechnol. 2010, 146:120-125.
    • (2010) J. Biotechnol. , vol.146 , pp. 120-125
    • Wu, S.1    Huang, R.2    Xu, L.3    Yan, G.4    Wang, Q.5
  • 218
    • 78650844008 scopus 로고    scopus 로고
    • Improved biohydrogen production with an expression of codon-optimized hemH and lba genes in the chloroplast of Chlamydomonas reinhardtii
    • Wu S., Xu L., Huang R., Wang Q. Improved biohydrogen production with an expression of codon-optimized hemH and lba genes in the chloroplast of Chlamydomonas reinhardtii. Biores. Technol. 2011, 102:2610-2616.
    • (2011) Biores. Technol. , vol.102 , pp. 2610-2616
    • Wu, S.1    Xu, L.2    Huang, R.3    Wang, Q.4
  • 219
    • 0032068061 scopus 로고    scopus 로고
    • The regulation of photosynthetic electron transport during nutrient deprivation in Chlamydomonas reinhardtii
    • Wykoff D.D., Davies J.P., Melis A., Grossman A.R. The regulation of photosynthetic electron transport during nutrient deprivation in Chlamydomonas reinhardtii. Plant Physiol. 1998, 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
  • 220
    • 0036735535 scopus 로고    scopus 로고
    • Comparison of photobioreactors for cultivation of Undaria pinnatifida gametophytes
    • Xu Z., Dapeng L., Yiping Z., Xiaoyan Z., Zhaoling C., Wei C., Fan O. Comparison of photobioreactors for cultivation of Undaria pinnatifida gametophytes. Biotechnol. Lett. 2002, 24:1499-1503.
    • (2002) Biotechnol. Lett. , vol.24 , pp. 1499-1503
    • Xu, Z.1    Dapeng, L.2    Yiping, Z.3    Xiaoyan, Z.4    Zhaoling, C.5    Wei, C.6    Fan, O.7
  • 221
    • 18644374880 scopus 로고    scopus 로고
    • Probing green algal hydrogen production
    • Zhang L., Melis A. Probing green algal hydrogen production. Phil. Trans. R. Soc. Lond. B 2002, 357:1499-1511.
    • (2002) Phil. Trans. R. Soc. Lond. B , vol.357 , pp. 1499-1511
    • Zhang, L.1    Melis, A.2
  • 222
    • 0036481398 scopus 로고    scopus 로고
    • Biochemical and morphological characterization of sulfur-deprived and H2 producing Chlamydomonas reinhardtii (green alga)
    • Zhang L., Happe T., Melis A. Biochemical and morphological characterization of sulfur-deprived and H2 producing Chlamydomonas reinhardtii (green alga). Planta 2002, 214:552-561.
    • (2002) Planta , vol.214 , pp. 552-561
    • Zhang, L.1    Happe, T.2    Melis, A.3
  • 223
    • 63349106223 scopus 로고    scopus 로고
    • Gene silencing by artificial microRNAs in Chlamydomonas
    • Zhao T., Wang W., Bai X., Qi Y. Gene silencing by artificial microRNAs in Chlamydomonas. Plant J. 2009, 58:157-164.
    • (2009) Plant J. , vol.58 , pp. 157-164
    • Zhao, T.1    Wang, W.2    Bai, X.3    Qi, Y.4
  • 224
    • 58549107608 scopus 로고    scopus 로고
    • Nuclear gene targeting in Chlamydomonas as exemplified by disruption of the PHOT gene
    • Zorin B., Lu Y., Sizova I., Hegemann P. Nuclear gene targeting in Chlamydomonas as exemplified by disruption of the PHOT gene. Gene 2009, 432:91-96.
    • (2009) Gene , vol.432 , pp. 91-96
    • Zorin, B.1    Lu, Y.2    Sizova, I.3    Hegemann, P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.