메뉴 건너뛰기




Volumn 38, Issue 4, 2013, Pages 1826-1836

A novel screening method for hydrogenase-deficient mutants in Chlamydomonas reinhardtii based on in vivo chlorophyll fluorescence and photosystem II quantum yield

Author keywords

Anaerobic photosynthesis; Chlamydomonas reinhardtii; Chlorophyll fluorescence; Hydrogen photoproduction; Hydrogenase; Microalgae

Indexed keywords

CHLAMYDOMONAS REINHARDTII; CHLOROPHYLL FLUORESCENCE; HYDROGEN PHOTOPRODUCTION; HYDROGENASES; MICRO-ALGAE;

EID: 84872615427     PISSN: 03603199     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ijhydene.2012.11.081     Document Type: Article
Times cited : (15)

References (67)
  • 2
    • 33747025752 scopus 로고    scopus 로고
    • A green hydrogen economy
    • W.C. Woodrow, and J. Rifkin A green hydrogen economy Energy Policy 34 2006 2630 2639
    • (2006) Energy Policy , vol.34 , pp. 2630-2639
    • Woodrow, W.C.1    Rifkin, J.2
  • 3
    • 84941787599 scopus 로고
    • Fermentative and photochemical production of hydrogen in algae
    • H. Gaffron, and J. Rubin Fermentative and photochemical production of hydrogen in algae J Gen Physiol 26 1942 219 240
    • (1942) J Gen Physiol , vol.26 , pp. 219-240
    • Gaffron, H.1    Rubin, J.2
  • 4
    • 0024657127 scopus 로고
    • Hydrogen production by eukaryotic algae
    • J.J. Brand, J.N. Wright, and S. Lien Hydrogen production by eukaryotic algae Biotechnol Bioeng 33 1989 1482 1488
    • (1989) Biotechnol Bioeng , vol.33 , pp. 1482-1488
    • Brand, J.J.1    Wright, J.N.2    Lien, S.3
  • 5
    • 0035197070 scopus 로고    scopus 로고
    • Hydrogen production. Green algae as a source of energy
    • A. Melis, and T. Happe Hydrogen production. Green algae as a source of energy Plant Physiol 127 2001 740 748
    • (2001) Plant Physiol , vol.127 , pp. 740-748
    • Melis, A.1    Happe, T.2
  • 7
    • 0000398649 scopus 로고
    • The mechanism of hydrogen evolution by Chlamydomonas moewusii
    • F.P. Healey The mechanism of hydrogen evolution by Chlamydomonas moewusii Plant Physiol 45 1970 153 159
    • (1970) Plant Physiol , vol.45 , pp. 153-159
    • Healey, F.P.1
  • 8
    • 0034886919 scopus 로고    scopus 로고
    • Classification and phylogeny of hydrogenases
    • P.M. Vignais, B. Billoud, and J. Meyer Classification and phylogeny of hydrogenases FEMS Microbiol Rev 25 2001 455 501
    • (2001) FEMS Microbiol Rev , vol.25 , pp. 455-501
    • Vignais, P.M.1    Billoud, B.2    Meyer, J.3
  • 9
    • 0032483966 scopus 로고    scopus 로고
    • X-ray crystal structure of the Fe-only hydrogenase (CpI) from Clostridium pasteurianum to 1.8 angstrom resolution
    • J.W. Peters, W.N. Lanzilotta, B.J. Lemon, and L.C. Seefeldt X-ray crystal structure of the Fe-only hydrogenase (CpI) from Clostridium pasteurianum to 1.8 angstrom resolution Science 282 1998 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
  • 10
    • 0033556301 scopus 로고    scopus 로고
    • Desulfovibrio desulfuricans iron hydrogenase: The structure shows unusual coordination to an active site Fe binuclear center
    • Y. Nicolet, C. Piras, P. Legrand, C.E. Hatchikian, and J.C. Fontecilla-Camps Desulfovibrio desulfuricans iron hydrogenase: the structure shows unusual coordination to an active site Fe binuclear center Structure 7 1999 13 23
    • (1999) Structure , vol.7 , pp. 13-23
    • Nicolet, Y.1    Piras, C.2    Legrand, P.3    Hatchikian, C.E.4    Fontecilla-Camps, J.C.5
  • 11
    • 0032804337 scopus 로고    scopus 로고
    • Structure and mechanism of iron-only hydrogenases
    • J.W. Peters Structure and mechanism of iron-only hydrogenases Curr Opin Struct Biol 9 1999 670 676
    • (1999) Curr Opin Struct Biol , vol.9 , pp. 670-676
    • Peters, J.W.1
  • 12
    • 0035961483 scopus 로고    scopus 로고
    • Crystallographic and FTIR spectroscopic evidence of changes in Fe coordination upon reduction of the active site of the Fe-only hydrogenase from Desulfovibrio desulfuricans
    • Y. Nicolet, A.L. de Lacey, X. Vernede, V.M. Fernandez, E.C. Hatchikian, and J.C. Fontecilla-Camps Crystallographic and FTIR spectroscopic evidence of changes in Fe coordination upon reduction of the active site of the Fe-only hydrogenase from Desulfovibrio desulfuricans J Am Chem Soc 123 2001 1596 1601
    • (2001) J Am Chem Soc , vol.123 , pp. 1596-1601
    • Nicolet, Y.1    De Lacey, A.L.2    Vernede, X.3    Fernandez, V.M.4    Hatchikian, E.C.5    Fontecilla-Camps, J.C.6
  • 13
    • 0001543350 scopus 로고
    • Cell-free hydrogenase from Chlamydomonas
    • F.B. Abeles Cell-free hydrogenase from Chlamydomonas Plant Physiol 39 1964 169 176
    • (1964) Plant Physiol , vol.39 , pp. 169-176
    • Abeles, F.B.1
  • 14
    • 0000892538 scopus 로고
    • Inactivation of hydrogenase in cell-free extracts and whole cells of Chlamydomonas reinhardi by oxygen
    • D.L. Erbes, D. King, and M. Gibbs Inactivation of hydrogenase in cell-free extracts and whole cells of Chlamydomonas reinhardi by oxygen Plant Physiol 63 1979 1138 1142
    • (1979) Plant Physiol , vol.63 , pp. 1138-1142
    • Erbes, D.L.1    King, D.2    Gibbs, M.3
  • 16
    • 14644432462 scopus 로고    scopus 로고
    • Molecular dynamics and experimental investigation of H(2) and O(2) diffusion in [Fe]-hydrogenase
    • J. Cohen, K. Kim, M. Posewitz, M.L. Ghirardi, K. Schulten, and M. Seibert Molecular dynamics and experimental investigation of H(2) and O(2) diffusion in [Fe]-hydrogenase Biochem Soc Trans 33 2005 80 82
    • (2005) Biochem Soc Trans , vol.33 , pp. 80-82
    • Cohen, J.1    Kim, K.2    Posewitz, M.3    Ghirardi, M.L.4    Schulten, K.5    Seibert, M.6
  • 17
    • 33644850541 scopus 로고    scopus 로고
    • Functional studies of [FeFe] hydrogenase maturation in an Escherichia coli biosynthetic system
    • P.W. King, M.C. Posewitz, M.L. Ghirardi, and M. Seibert Functional studies of [FeFe] hydrogenase maturation in an Escherichia coli biosynthetic system J Bacteriol 188 2006 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
  • 18
    • 0036186921 scopus 로고    scopus 로고
    • Differential regulation of the Fe-hydrogenase during anaerobic adaptation in the green alga Chlamydomonas reinhardtii
    • T. Happe, and A. Kaminski Differential regulation of the Fe-hydrogenase during anaerobic adaptation in the green alga Chlamydomonas reinhardtii Eur J Biochem 269 2002 1022 1032
    • (2002) Eur J Biochem , vol.269 , pp. 1022-1032
    • Happe, T.1    Kaminski, A.2
  • 19
    • 0037715163 scopus 로고    scopus 로고
    • Expression of two [Fe]-hydrogenases in Chlamydomonas reinhardtii under anaerobic conditions
    • M. Forestier, P. King, L. Zhang, M. Posewitz, S. Schwarzer, and T. Happe Expression of two [Fe]-hydrogenases in Chlamydomonas reinhardtii under anaerobic conditions Eur J Biochem 270 2003 2750 2758
    • (2003) Eur J Biochem , vol.270 , pp. 2750-2758
    • Forestier, M.1    King, P.2    Zhang, L.3    Posewitz, M.4    Schwarzer, S.5    Happe, T.6
  • 20
    • 78049255865 scopus 로고    scopus 로고
    • RNA silencing of hydrogenase(-like) genes and investigation of their physiological roles in the green alga Chlamydomonas reinhardtii
    • J.E. Godman, A. Molnar, D.C. Baulcombe, and J. Balk RNA silencing of hydrogenase(-like) genes and investigation of their physiological roles in the green alga Chlamydomonas reinhardtii Biochem J 431 2010 345 351
    • (2010) Biochem J , vol.431 , pp. 345-351
    • Godman, J.E.1    Molnar, A.2    Baulcombe, D.C.3    Balk, J.4
  • 21
    • 84855835711 scopus 로고    scopus 로고
    • Genetic disruption of both Chlamydomonas reinhardtii [FeFe]-hydrogenases: Insight into the role of HYDA2 in H(2) production
    • J.E. Meuser, S. D'Adamo, R.E. Jinkerson, F. Mus, W. Yang, and M.L. Ghirardi Genetic disruption of both Chlamydomonas reinhardtii [FeFe]-hydrogenases: insight into the role of HYDA2 in H(2) production Biochem Biophys Res Commun 417 2012 704 709
    • (2012) Biochem Biophys Res Commun , vol.417 , pp. 704-709
    • Meuser, J.E.1    D'Adamo, S.2    Jinkerson, R.E.3    Mus, F.4    Yang, W.5    Ghirardi, M.L.6
  • 22
    • 77952428962 scopus 로고    scopus 로고
    • Stepwise [FeFe]-hydrogenase H-cluster assembly revealed in the structure of HydA(DeltaEFG)
    • D.W. Mulder, E.S. Boyd, R. Sarma, R.K. Lange, J.A. Endrizzi, and J.B. Broderick Stepwise [FeFe]-hydrogenase H-cluster assembly revealed in the structure of HydA(DeltaEFG) Nature 465 2010 248 251
    • (2010) Nature , vol.465 , pp. 248-251
    • Mulder, D.W.1    Boyd, E.S.2    Sarma, R.3    Lange, R.K.4    Endrizzi, J.A.5    Broderick, J.B.6
  • 25
    • 4043114949 scopus 로고    scopus 로고
    • Hydrogen photoproduction is attenuated by disruption of an isoamylase gene in Chlamydomonas reinhardtii
    • M.C. Posewitz, S.L. Smolinski, S. Kanakagiri, A. Melis, M. Seibert, and M.L. Ghirardi Hydrogen photoproduction is attenuated by disruption of an isoamylase gene in Chlamydomonas reinhardtii Plant Cell 16 2004 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
  • 26
    • 84864645925 scopus 로고    scopus 로고
    • Differential expression of the Chlamydomonas [FeFe]-hydrogenase encoding HYDA1 gene is regulated by the copper response regulator 1
    • M. Pape, C. Lambertz, T. Happe, and A. Hemschemeier Differential expression of the Chlamydomonas [FeFe]-hydrogenase encoding HYDA1 gene is regulated by the copper response regulator 1 Plant Physiol 159 2012 1700 1712
    • (2012) Plant Physiol , vol.159 , pp. 1700-1712
    • Pape, M.1    Lambertz, C.2    Happe, T.3    Hemschemeier, A.4
  • 27
    • 79955044664 scopus 로고    scopus 로고
    • A pyruvate formate lyase-deficient Chlamydomonas reinhardtii strain provides evidence for a link between fermentation and hydrogen production in green algae
    • G. Philipps, D. Krawietz, A. Hemschemeier, and T. Happe A pyruvate formate lyase-deficient Chlamydomonas reinhardtii strain provides evidence for a link between fermentation and hydrogen production in green algae Plant J 66 2011 330 340
    • (2011) Plant J , vol.66 , pp. 330-340
    • Philipps, G.1    Krawietz, D.2    Hemschemeier, A.3    Happe, T.4
  • 28
    • 58149483399 scopus 로고    scopus 로고
    • A type II NAD(P)H dehydrogenase mediates light-independent plastoquinone reduction in the chloroplast of Chlamydomonas
    • F. Jans, E. Mignolet, P.A. Houyoux, P. Cardol, B. Ghysels, and S. Cuine A type II NAD(P)H dehydrogenase mediates light-independent plastoquinone reduction in the chloroplast of Chlamydomonas Proc Natl Acad Sci U S A 105 2008 20546 20551
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 20546-20551
    • Jans, F.1    Mignolet, E.2    Houyoux, P.A.3    Cardol, P.4    Ghysels, B.5    Cuine, S.6
  • 29
    • 79960895878 scopus 로고    scopus 로고
    • Functional analysis of hydrogen photoproduction in respiratory-deficient mutants of Chlamydomonas reinhardtii
    • R. Lecler, D. Godaux, H. Vigeolas, S. Hiligsmann, P. Thonart, and F. Franck Functional analysis of hydrogen photoproduction in respiratory-deficient mutants of Chlamydomonas reinhardtii Int J Hydrogen Energy 36 2011 9562 9570
    • (2011) Int J Hydrogen Energy , vol.36 , pp. 9562-9570
    • Lecler, R.1    Godaux, D.2    Vigeolas, H.3    Hiligsmann, S.4    Thonart, P.5    Franck, F.6
  • 31
    • 55149105865 scopus 로고    scopus 로고
    • A novel screening protocol for the isolation of hydrogen producing Chlamydomonas reinhardtii strains
    • T. Ruhle, A. Hemschemeier, A. Melis, and T. Happe A novel screening protocol for the isolation of hydrogen producing Chlamydomonas reinhardtii strains BMC Plant Biol 8 2008 107
    • (2008) BMC Plant Biol , vol.8 , pp. 107
    • Ruhle, T.1    Hemschemeier, A.2    Melis, A.3    Happe, T.4
  • 33
    • 80051938286 scopus 로고    scopus 로고
    • Control of hydrogen photoproduction by the proton gradient generated by cyclic electron flow in Chlamydomonas reinhardtii
    • D. Tolleter, B. Ghysels, J. Alric, D. Petroutsos, I. Tolstygina, and D. Krawietz Control of hydrogen photoproduction by the proton gradient generated by cyclic electron flow in Chlamydomonas reinhardtii Plant Cell 23 2011 2619 2630
    • (2011) Plant Cell , vol.23 , pp. 2619-2630
    • Tolleter, D.1    Ghysels, B.2    Alric, J.3    Petroutsos, D.4    Tolstygina, I.5    Krawietz, D.6
  • 35
    • 0016651535 scopus 로고
    • Quenching of chlorophyll fluorescence and primary photochemistry in chloroplasts by dibromothymoquinone
    • M. Kitajima, and W.L. Butler Quenching of chlorophyll fluorescence and primary photochemistry in chloroplasts by dibromothymoquinone Biochim Biophys Acta (BBA)-Bioenerg 376 1975 105 115
    • (1975) Biochim Biophys Acta (BBA)-Bioenerg , vol.376 , pp. 105-115
    • Kitajima, M.1    Butler, W.L.2
  • 36
    • 85023704649 scopus 로고
    • The relationship between the quantum yield of photosynthetic electron transport and quenching of chlorophyll fluorescence
    • B. Genty, J.-M. Briantais, and N.R. Baker The relationship between the quantum yield of photosynthetic electron transport and quenching of chlorophyll fluorescence Biochim Biophys Acta (BBA) 990 1989 87 92
    • (1989) Biochim Biophys Acta (BBA) , vol.990 , pp. 87-92
    • Genty, B.1    Briantais, J.-M.2    Baker, N.R.3
  • 37
    • 0001231299 scopus 로고
    • Stoichiometry of system i and system II reaction centers and of plastoquinone in different photosynthetic membranes
    • A. Melis, and J.S. Brown Stoichiometry of system I and system II reaction centers and of plastoquinone in different photosynthetic membranes Proc Natl Acad Sci U S A 77 1980 4712 4716
    • (1980) Proc Natl Acad Sci U S A , vol.77 , pp. 4712-4716
    • Melis, A.1    Brown, J.S.2
  • 38
    • 70349468044 scopus 로고    scopus 로고
    • Impaired respiration discloses the physiological significance of state transitions in Chlamydomonas
    • P. Cardol, J. Alric, J. Girard-Bascou, F. Franck, F.A. Wollman, and G. Finazzi Impaired respiration discloses the physiological significance of state transitions in Chlamydomonas Proc Natl Acad Sci U S A 106 2009 15979 15984
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 15979-15984
    • Cardol, P.1    Alric, J.2    Girard-Bascou, J.3    Franck, F.4    Wollman, F.A.5    Finazzi, G.6
  • 39
    • 0031893765 scopus 로고    scopus 로고
    • High-efficiency transformation of Chlamydomonas reinhardtii by electroporation
    • K. Shimogawara, S. Fujiwara, A. Grossman, and H. Usuda High-efficiency transformation of Chlamydomonas reinhardtii by electroporation Genetics 148 1998 1821 1828
    • (1998) Genetics , vol.148 , pp. 1821-1828
    • Shimogawara, K.1    Fujiwara, S.2    Grossman, A.3    Usuda, H.4
  • 40
    • 0036967786 scopus 로고    scopus 로고
    • An engineered Streptomyces hygroscopicus aph 7″ gene mediates dominant resistance against hygromycin B in Chlamydomonas reinhardtii
    • P. Berthold, R. Schmitt, and W. Mages An engineered Streptomyces hygroscopicus aph 7″ gene mediates dominant resistance against hygromycin B in Chlamydomonas reinhardtii Protist 153 2002 401 412
    • (2002) Protist , vol.153 , pp. 401-412
    • Berthold, P.1    Schmitt, R.2    Mages, W.3
  • 42
    • 19044380672 scopus 로고    scopus 로고
    • Functional genomics of eukaryotic photosynthesis using insertional mutagenesis of Chlamydomonas reinhardtii
    • R.M. Dent, C.M. Haglund, B.L. Chin, M.C. Kobayashi, and K. Niyogi Functional genomics of eukaryotic photosynthesis using insertional mutagenesis of Chlamydomonas reinhardtii Plant Physiol 137 2005 545 556
    • (2005) Plant Physiol , vol.137 , pp. 545-556
    • Dent, R.M.1    Haglund, C.M.2    Chin, B.L.3    Kobayashi, M.C.4    Niyogi, K.5
  • 43
    • 79958188929 scopus 로고    scopus 로고
    • A forward genetic screen identifies mutants deficient for mitochondrial complex i assembly in Chlamydomonas reinhardtii
    • M.R. Barbieri, V. Larosa, C. Nouet, N. Subrahmanian, C. Remacle, and P.P. Hamel A forward genetic screen identifies mutants deficient for mitochondrial complex I assembly in Chlamydomonas reinhardtii Genetics 188 2011 349 358
    • (2011) Genetics , vol.188 , pp. 349-358
    • Barbieri, M.R.1    Larosa, V.2    Nouet, C.3    Subrahmanian, N.4    Remacle, C.5    Hamel, P.P.6
  • 44
    • 0024746937 scopus 로고
    • Antibiotic resistance mutations in the chloroplast 16S and 23S rRNA genes of Chlamydomonas reinhardtii: Correlation of genetic and physical maps of the chloroplast genome
    • E.H. Harris, B.D. Burkhart, N.W. Gillham, and J.E. Boynton Antibiotic resistance mutations in the chloroplast 16S and 23S rRNA genes of Chlamydomonas reinhardtii: correlation of genetic and physical maps of the chloroplast genome Genetics 123 1989 281 292
    • (1989) Genetics , vol.123 , pp. 281-292
    • Harris, E.H.1    Burkhart, B.D.2    Gillham, N.W.3    Boynton, J.E.4
  • 45
    • 30044440683 scopus 로고    scopus 로고
    • The polyphasic chlorophyll a fluorescence rise measured under high intensity of exciting light
    • D. Lazar The polyphasic chlorophyll a fluorescence rise measured under high intensity of exciting light Funct Plant Biol 33 2006 9 30
    • (2006) Funct Plant Biol , vol.33 , pp. 9-30
    • Lazar, D.1
  • 46
    • 84857955106 scopus 로고    scopus 로고
    • Altered fermentative metabolism in Chlamydomonas reinhardtii mutants lacking pyruvate formate lyase and both pyruvate formate lyase and alcohol dehydrogenase
    • C. Catalanotti, A. Dubini, V. Subramanian, W. Yang, L. Magneschi, and F. Mus Altered fermentative metabolism in Chlamydomonas reinhardtii mutants lacking pyruvate formate lyase and both pyruvate formate lyase and alcohol dehydrogenase Plant Cell 24 2012 692 707
    • (2012) Plant Cell , vol.24 , pp. 692-707
    • Catalanotti, C.1    Dubini, A.2    Subramanian, V.3    Yang, W.4    Magneschi, L.5    Mus, F.6
  • 47
    • 84863230146 scopus 로고    scopus 로고
    • A mutant in the ADH1 gene of Chlamydomonas reinhardtii elicits metabolic restructuring during anaerobiosis
    • L. Magneschi, C. Catalanotti, V. Subramanian, A. Dubini, W. Yang, and F. Mus A mutant in the ADH1 gene of Chlamydomonas reinhardtii elicits metabolic restructuring during anaerobiosis Plant Physiol 158 2012 1293 1305
    • (2012) Plant Physiol , vol.158 , pp. 1293-1305
    • Magneschi, L.1    Catalanotti, C.2    Subramanian, V.3    Dubini, A.4    Yang, W.5    Mus, F.6
  • 48
    • 0035898532 scopus 로고    scopus 로고
    • State transitions reveal the dynamics and flexibility of the photosynthetic apparatus
    • F.A. Wollman State transitions reveal the dynamics and flexibility of the photosynthetic apparatus EMBO J 20 2001 3623 3630
    • (2001) EMBO J , vol.20 , pp. 3623-3630
    • Wollman, F.A.1
  • 49
    • 0032472375 scopus 로고    scopus 로고
    • A systematic survey of conserved histidines in the core subunits of photosystem i by site-directed mutagenesis reveals the likely axial ligands of P700
    • K. Redding, F. MacMillan, W. Leibl, K. Brettel, J. Hanley, and A.W. Rutherford A systematic survey of conserved histidines in the core subunits of photosystem I by site-directed mutagenesis reveals the likely axial ligands of P700 EMBO J 17 1998 50 60
    • (1998) EMBO J , vol.17 , pp. 50-60
    • Redding, K.1    MacMillan, F.2    Leibl, W.3    Brettel, K.4    Hanley, J.5    Rutherford, A.W.6
  • 50
    • 0028178516 scopus 로고
    • The assembly of cytochrome b6/f complexes: An approach using genetic transformation of the green alga Chlamydomonas reinhardtii
    • R. Kuras, and F.A. Wollman The assembly of cytochrome b6/f complexes: an approach using genetic transformation of the green alga Chlamydomonas reinhardtii EMBO J 13 1994 1019 1027
    • (1994) EMBO J , vol.13 , pp. 1019-1027
    • Kuras, R.1    Wollman, F.A.2
  • 51
    • 84855500513 scopus 로고    scopus 로고
    • Plastid terminal oxidase 2 (PTOX2) is the major oxidase involved in chlororespiration in Chlamydomonas
    • L. Houille-Vernes, F. Rappaport, F.A. Wollman, J. Alric, and X. Johnson Plastid terminal oxidase 2 (PTOX2) is the major oxidase involved in chlororespiration in Chlamydomonas Proc Natl Acad Sci U S A 108 2011 20820 20825
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 20820-20825
    • Houille-Vernes, L.1    Rappaport, F.2    Wollman, F.A.3    Alric, J.4    Johnson, X.5
  • 52
    • 1442295800 scopus 로고
    • Characterization of a photosynthetic mutant strain of Chlamydomonas reinhardtii deficient in phosphoribulokinase activity
    • B. Moll, and R.P. Levine Characterization of a photosynthetic mutant strain of Chlamydomonas reinhardtii deficient in phosphoribulokinase activity Plant Physiol 46 1970 576 580
    • (1970) Plant Physiol , vol.46 , pp. 576-580
    • Moll, B.1    Levine, R.P.2
  • 53
    • 0016279053 scopus 로고
    • Chlorophyll fluorescence induction in anaerobic Scenedesmus obliquus
    • U. Schreiber, and W. Vidaver Chlorophyll fluorescence induction in anaerobic Scenedesmus obliquus Biochim Biophys Acta 368 1974 97 112
    • (1974) Biochim Biophys Acta , vol.368 , pp. 97-112
    • Schreiber, U.1    Vidaver, W.2
  • 54
    • 84872618031 scopus 로고
    • Dissertation: RWTH Aachen. Germany
    • Schreiber U. Dissertation: RWTH Aachen. Germany: 1971.
    • (1971)
    • Schreiber, U.1
  • 56
    • 0015810074 scopus 로고
    • Effect of anaerobiosis on photosynthetic reactions and nitrogen metabolism of algae with and without hydrogenase
    • E. Kessler Effect of anaerobiosis on photosynthetic reactions and nitrogen metabolism of algae with and without hydrogenase Arch Mikrobiol 93 1973 91 100
    • (1973) Arch Mikrobiol , vol.93 , pp. 91-100
    • Kessler, E.1
  • 57
    • 44949110144 scopus 로고    scopus 로고
    • Chlorophyll fluorescence: A probe of photosynthesis in vivo
    • N.R. Baker Chlorophyll fluorescence: a probe of photosynthesis in vivo Annu Rev Plant Biol 59 2008 89 113
    • (2008) Annu Rev Plant Biol , vol.59 , pp. 89-113
    • Baker, N.R.1
  • 58
    • 2642672010 scopus 로고    scopus 로고
    • Chlamydomonas xantophyll cycle mutants identified by video imaging of chlorophyll fluorescence quenching
    • K. Niyogi, O. Bjorkman, and A. Grossman Chlamydomonas xantophyll cycle mutants identified by video imaging of chlorophyll fluorescence quenching Plant Cell 9 1997 1369 1380
    • (1997) Plant Cell , vol.9 , pp. 1369-1380
    • Niyogi, K.1    Bjorkman, O.2    Grossman, A.3
  • 59
    • 0001618669 scopus 로고
    • Detecting mutants that have impaired photosynthesis by their increased level of fluorescence
    • P. Bennoun, and R.P. Levine Detecting mutants that have impaired photosynthesis by their increased level of fluorescence Plant Physiol 42 1967 1284 1287
    • (1967) Plant Physiol , vol.42 , pp. 1284-1287
    • Bennoun, P.1    Levine, R.P.2
  • 60
    • 76149124197 scopus 로고    scopus 로고
    • Analytical approaches to photobiological hydrogen production in unicellular green algae
    • A. Hemschemeier, A. Melis, and T. Happe Analytical approaches to photobiological hydrogen production in unicellular green algae Photosyn Res 102 2009 523 540
    • (2009) Photosyn Res , vol.102 , pp. 523-540
    • Hemschemeier, A.1    Melis, A.2    Happe, T.3
  • 61
    • 70349647741 scopus 로고    scopus 로고
    • Hydrogen production in Chlamydomonas: Photosystem II-dependent and -independent pathways differ in their requirement for starch metabolism
    • V. Chochois, D. Dauvillee, A. Beyly, D. Tolleter, S. Cuine, and H. Timpano Hydrogen production in Chlamydomonas: photosystem II-dependent and -independent pathways differ in their requirement for starch metabolism Plant Physiol 151 2009 631 640
    • (2009) Plant Physiol , vol.151 , pp. 631-640
    • Chochois, V.1    Dauvillee, D.2    Beyly, A.3    Tolleter, D.4    Cuine, S.5    Timpano, H.6
  • 62
    • 0347052748 scopus 로고    scopus 로고
    • Photosynthesis and state transitions in mitochondrial mutants of Chlamydomonas reinhardtii affected in respiration
    • P. Cardol, G. Gloire, M. Havaux, C. Remacle, R. Matagne, and F. Franck Photosynthesis and state transitions in mitochondrial mutants of Chlamydomonas reinhardtii affected in respiration Plant Physiol 133 2003 2010 2020
    • (2003) Plant Physiol , vol.133 , pp. 2010-2020
    • Cardol, P.1    Gloire, G.2    Havaux, M.3    Remacle, C.4    Matagne, R.5    Franck, F.6
  • 63
    • 0000709041 scopus 로고
    • Photosynthesis-deficient mutants of Chlamydomonas reinhardii with associated light-sensitive phenotypes
    • R.J. Spreitzer, and L. Mets Photosynthesis-deficient mutants of Chlamydomonas reinhardii with associated light-sensitive phenotypes Plant Physiol 67 1981 565 569
    • (1981) Plant Physiol , vol.67 , pp. 565-569
    • Spreitzer, R.J.1    Mets, L.2
  • 64
    • 77950366107 scopus 로고    scopus 로고
    • Gene hunting by complementation of pooled Chlamydomonas reinhardtii mutants
    • X. Johnson, R. Kuras, F.A. Wollman, and O. Vallon Gene hunting by complementation of pooled Chlamydomonas reinhardtii mutants Photosynthesis 17 2008 1093 1097
    • (2008) Photosynthesis , vol.17 , pp. 1093-1097
    • Johnson, X.1    Kuras, R.2    Wollman, F.A.3    Vallon, O.4
  • 65
    • 0026810791 scopus 로고
    • Biochemical, genetic and molecular characterization of new respiratory-deficient mutants in Chlamydomonas reinhardtii
    • M.P. Dorthu, S. Remy, M.R. Michel-Wolwertz, L. Colleaux, D. Breyer, and M.C. Beckers Biochemical, genetic and molecular characterization of new respiratory-deficient mutants in Chlamydomonas reinhardtii Plant Mol Biol 18 1992 759 772
    • (1992) Plant Mol Biol , vol.18 , pp. 759-772
    • Dorthu, M.P.1    Remy, S.2    Michel-Wolwertz, M.R.3    Colleaux, L.4    Breyer, D.5    Beckers, M.C.6
  • 66
    • 0034872370 scopus 로고    scopus 로고
    • Mutations inactivating mitochondrial genes in Chlamydomonas reinhardtii
    • C. Remacle, F. Duby, P. Cardol, and R.F. Matagne Mutations inactivating mitochondrial genes in Chlamydomonas reinhardtii Biochem Soc Trans 29 2001 442 446
    • (2001) Biochem Soc Trans , vol.29 , pp. 442-446
    • Remacle, C.1    Duby, F.2    Cardol, P.3    Matagne, R.F.4
  • 67
    • 0036304765 scopus 로고    scopus 로고
    • Impact of mutations affecting ND mitochondria-encoded subunits on the activity and assembly of complex i in Chlamydomonas. Implication for the structural organization of the enzyme
    • P. Cardol, R.F. Matagne, and C. Remacle Impact of mutations affecting ND mitochondria-encoded subunits on the activity and assembly of complex I in Chlamydomonas. Implication for the structural organization of the enzyme J Mol Biol 319 2002 1211 1221
    • (2002) J Mol Biol , vol.319 , pp. 1211-1221
    • Cardol, P.1    Matagne, R.F.2    Remacle, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.