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Volumn 583, Issue 2, 2009, Pages 325-329

A novel, anaerobically induced ferredoxin in Chlamydomonas reinhardtii

Author keywords

Anaerobiosis; Ferredoxin; Green alga; Hydrogen metabolism

Indexed keywords

FERREDOXIN; FERREDOXIN NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE REDUCTASE; HYDROGENASE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; PROTEIN FDX5; PROTEIN HYDA1; PROTEIN PETF; UNCLASSIFIED DRUG;

EID: 58249096361     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2008.12.018     Document Type: Article
Times cited : (57)

References (32)
  • 1
    • 0002166923 scopus 로고
    • Structure and evolution of chloroplast- and bacterial-type ferredoxin
    • Sigman D.S., and Brazier H.A.B. (Eds), Academic Press, NY, USA
    • Matsubara H., Hase T., Wakabayashi S., and Wada K. Structure and evolution of chloroplast- and bacterial-type ferredoxin. In: Sigman D.S., and Brazier H.A.B. (Eds). The Evolution of Protein Structure and Function (1980), Academic Press, NY, USA 245-266
    • (1980) The Evolution of Protein Structure and Function , pp. 245-266
    • Matsubara, H.1    Hase, T.2    Wakabayashi, S.3    Wada, K.4
  • 2
    • 0001038547 scopus 로고    scopus 로고
    • Ferredoxin and ferredoxin dependent enzymes
    • Ort D.R., and Yocum C.F. (Eds), Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Knaff D.B. Ferredoxin and ferredoxin dependent enzymes. In: Ort D.R., and Yocum C.F. (Eds). Oxygenic Photosynthesis: The Light Reactions (1996), Kluwer Academic Publishers, Dordrecht, The Netherlands 333-361
    • (1996) Oxygenic Photosynthesis: The Light Reactions , pp. 333-361
    • Knaff, D.B.1
  • 3
    • 0023858197 scopus 로고
    • The discovery of ferredoxin: the photosynthetic path
    • Arnon D.I. The discovery of ferredoxin: the photosynthetic path. Trends Biochem. Sci. 13 (1989) 30-33
    • (1989) Trends Biochem. Sci. , vol.13 , pp. 30-33
    • Arnon, D.I.1
  • 4
    • 0036140264 scopus 로고    scopus 로고
    • Browsing gene banks for Fe2S2 ferredoxins and structural modelling of 88 planttype sequences: an analysis of fold and function
    • Bertini I., Luchinat C., Provenzani A., Rosato A., and Vasos P.R. Browsing gene banks for Fe2S2 ferredoxins and structural modelling of 88 planttype sequences: an analysis of fold and function. Proteins 46 (2002) 110-127
    • (2002) Proteins , vol.46 , pp. 110-127
    • Bertini, I.1    Luchinat, C.2    Provenzani, A.3    Rosato, A.4    Vasos, P.R.5
  • 5
    • 0001454446 scopus 로고
    • Expression of maize ferredoxin cDNA in Escherichia coli
    • Hase T., Mizutani S., and Mukohata Y. Expression of maize ferredoxin cDNA in Escherichia coli. Plant Physiol. 97 (1991) 1395-1401
    • (1991) Plant Physiol. , vol.97 , pp. 1395-1401
    • Hase, T.1    Mizutani, S.2    Mukohata, Y.3
  • 8
    • 0027153213 scopus 로고
    • Isolation, characterization and N-terminal amino acid sequence of hydrogenase from the green alga Chlamydomonas reinhardtii
    • Happe T., and Naber J.D. Isolation, characterization and N-terminal amino acid sequence of hydrogenase from the green alga Chlamydomonas reinhardtii. Eur. J. Biochem. 214 (1993) 475-481
    • (1993) Eur. J. Biochem. , vol.214 , pp. 475-481
    • Happe, T.1    Naber, J.D.2
  • 10
    • 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., and 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 7 (2008) 518-526
    • (2008) Eukaryot. Cell , vol.7 , pp. 518-526
    • Hemschemeier, A.1    Jacobs, J.2    Happe, T.3
  • 11
    • 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., and Seibert M. Sustained photobiological hydrogen gas production upon reversible inactivation of oxygen evolution in the green alga Chlamydomonas reinhardtii. Plant Physiol. 122 (2000) 127-135
    • (2000) Plant Physiol. , vol.122 , pp. 127-135
    • Melis, A.1    Zhang, L.2    Forestier, M.3    Ghirardi, M.L.4    Seibert, M.5
  • 12
    • 0036827189 scopus 로고    scopus 로고
    • [Fe]-hydrogenases in green algae: photo-fermentation and hydrogen evolution under sulfur-deprivation
    • Winkler M., Hemschemeier A., Gotor C., Melis A., and Happe T. [Fe]-hydrogenases in green algae: photo-fermentation and hydrogen evolution under sulfur-deprivation. Int. J. Hydrogen Energy 27 (2002) 1431-1439
    • (2002) Int. J. Hydrogen Energy , vol.27 , pp. 1431-1439
    • Winkler, M.1    Hemschemeier, A.2    Gotor, C.3    Melis, A.4    Happe, T.5
  • 14
    • 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., and Happe T. Hydrogen production by Chlamydomonas reinhardtii: an elaborate interplay of electron sources and sinks. Planta 227 (2008) 397-407
    • (2008) Planta , vol.227 , pp. 397-407
    • Hemschemeier, A.1    Fouchard, S.2    Cournac, L.3    Peltier, G.4    Happe, T.5
  • 16
    • 0031953257 scopus 로고    scopus 로고
    • Low density membranes are associated with RNA-binding proteins and thylakoids in the chloroplast of Chlamydomonas reinhardtii
    • Zerges W., and Rochaix J.-D. Low density membranes are associated with RNA-binding proteins and thylakoids in the chloroplast of Chlamydomonas reinhardtii. J. Cell Biol. 140 (1998) 101-110
    • (1998) J. Cell Biol. , vol.140 , pp. 101-110
    • Zerges, W.1    Rochaix, J.-D.2
  • 17
    • 0029110550 scopus 로고
    • Isolation, purification, and characterization of mitochondria from Chlamydomonas reinhardtii
    • Erikkson M., Gardeström P., and Samuelsson G. Isolation, purification, and characterization of mitochondria from Chlamydomonas reinhardtii. Plant Physiol. 107 (1995) 479-483
    • (1995) Plant Physiol. , vol.107 , pp. 479-483
    • Erikkson, M.1    Gardeström, P.2    Samuelsson, G.3
  • 18
    • 34249789854 scopus 로고    scopus 로고
    • Structural response of Photosystem 2 to iron deficiency: Characterization of a new Photosystem 2-IdiA complex from the cyanobacterium Thermosynechococcus elongatus BP-1
    • Lax J., Arteni A., Boekema E., Pistorius E., Michel K.-P., and Rögner M. Structural response of Photosystem 2 to iron deficiency: Characterization of a new Photosystem 2-IdiA complex from the cyanobacterium Thermosynechococcus elongatus BP-1. Biochim. Biophys. Acta 1767 (2007) 528-534
    • (2007) Biochim. Biophys. Acta , vol.1767 , pp. 528-534
    • Lax, J.1    Arteni, A.2    Boekema, E.3    Pistorius, E.4    Michel, K.-P.5    Rögner, M.6
  • 19
    • 0028285551 scopus 로고
    • Induction, localization and metal content of hydrogenase in the green alga Chlamydomonas reinhardtii
    • Happe T., Mosler B., and Naber J.D. Induction, localization and metal content of hydrogenase in the green alga Chlamydomonas reinhardtii. Eur. J. Biochem. 222 (1994) 769-774
    • (1994) Eur. J. Biochem. , vol.222 , pp. 769-774
    • Happe, T.1    Mosler, B.2    Naber, J.D.3
  • 20
    • 0001842885 scopus 로고
    • Physiological bases for detecting and predicting photoinhibition of aquatic photosynthesis by PAR and UV radiation
    • Current Topics in Plant Physiology. Yamamoto H.J., and Smith C.M. (Eds), American Society of Plant Physiologists, Rockville, MD, USA
    • Neale P.J., Cullen J.J., Lesser M.P., and Melis A. Physiological bases for detecting and predicting photoinhibition of aquatic photosynthesis by PAR and UV radiation. In: Yamamoto H.J., and Smith C.M. (Eds). Current Topics in Plant Physiology. Photosynthetic responses to the environment Vol. 8 (1993), American Society of Plant Physiologists, Rockville, MD, USA 61-77
    • (1993) Photosynthetic responses to the environment , vol.8 , pp. 61-77
    • Neale, P.J.1    Cullen, J.J.2    Lesser, M.P.3    Melis, A.4
  • 21
    • 0017578884 scopus 로고
    • +-reductase in cyclic electron transport of spinach chloroplasts
    • +-reductase in cyclic electron transport of spinach chloroplasts. Eur. J. Biochem. 72 (1977) 283-289
    • (1977) Eur. J. Biochem. , vol.72 , pp. 283-289
    • Böhme, H.1
  • 22
    • 0025135468 scopus 로고
    • A conserved cleavage-site motif in chloroplast transit peptides
    • Gavel Y., and von Heijne G. A conserved cleavage-site motif in chloroplast transit peptides. FEBS Lett. 261 (1990) 455-458
    • (1990) FEBS Lett. , vol.261 , pp. 455-458
    • Gavel, Y.1    von Heijne, G.2
  • 23
    • 1542364538 scopus 로고    scopus 로고
    • Mechanism of oxygen sensing by the bacterial transcription factor fumarate-nitrate reduction (FNR)
    • Crack J., Green J., and Thomson A.J. Mechanism of oxygen sensing by the bacterial transcription factor fumarate-nitrate reduction (FNR). J. Biol. Chem. 279 (2004) 9278-9286
    • (2004) J. Biol. Chem. , vol.279 , pp. 9278-9286
    • Crack, J.1    Green, J.2    Thomson, A.J.3
  • 24
    • 0035119660 scopus 로고    scopus 로고
    • Valine 77 of heterocystous ferredoxin FdxH2 in Anabaena variabilis strain ATCC 29413 is critical for its oxygen sensitivity
    • Singh B.B., Curdt I., Shomburg D., Bisen P.S., and Böhme H. Valine 77 of heterocystous ferredoxin FdxH2 in Anabaena variabilis strain ATCC 29413 is critical for its oxygen sensitivity. Mol. Cell Biochem. 217 (2001) 137-142
    • (2001) Mol. Cell Biochem. , vol.217 , pp. 137-142
    • Singh, B.B.1    Curdt, I.2    Shomburg, D.3    Bisen, P.S.4    Böhme, H.5
  • 25
    • 0142184944 scopus 로고    scopus 로고
    • 2+-responsive promoter for induced, reversible gene expression in Chlamydomonas reinhardtii
    • 2+-responsive promoter for induced, reversible gene expression in Chlamydomonas reinhardtii. Eukaryot. Cell 2 (2003) 995-1002
    • (2003) Eukaryot. Cell , vol.2 , pp. 995-1002
    • Quinn, J.M.1    Kropat, J.2    Merchant, S.3
  • 26
    • 45149135688 scopus 로고
    • Chloroplast transit peptides from the green alga Chlamydomonas reinhardtii share features with both mitochondrial and higher plant chloroplast presequences
    • Franzen G., Rochaix J.D., and von Heijne G. Chloroplast transit peptides from the green alga Chlamydomonas reinhardtii share features with both mitochondrial and higher plant chloroplast presequences. FEBS Lett. 260 (1989) 165-168
    • (1989) FEBS Lett. , vol.260 , pp. 165-168
    • Franzen, G.1    Rochaix, J.D.2    von Heijne, G.3
  • 27
    • 0023899855 scopus 로고
    • Rapid colorimetric micromethod for the quantitation of complexed iron in biological samples
    • Fish W.W. Rapid colorimetric micromethod for the quantitation of complexed iron in biological samples. Meth. Enzymol. 158 (1988) 357-364
    • (1988) Meth. Enzymol. , vol.158 , pp. 357-364
    • Fish, W.W.1
  • 28
    • 0006880881 scopus 로고
    • Physicochemical properties of ferredoxin from Chlamydomonas reinhardii
    • Galvan F., Marquez A.J., and Fernandez E. Physicochemical properties of ferredoxin from Chlamydomonas reinhardii. Z. Naturforsch. 40c (1985) 373-378
    • (1985) Z. Naturforsch. , vol.40 c , pp. 373-378
    • Galvan, F.1    Marquez, A.J.2    Fernandez, E.3
  • 29
    • 18744388311 scopus 로고    scopus 로고
    • Release of oxidized plastocyanin from photosystem I limits electron transfer between photosystem I and cytochrome b6f complex in vivo
    • Finazzi G., Sommer F., and Hippler M. Release of oxidized plastocyanin from photosystem I limits electron transfer between photosystem I and cytochrome b6f complex in vivo. Proc. Natl. Acad. Sci. USA 102 (2005) 7031-7036
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 7031-7036
    • Finazzi, G.1    Sommer, F.2    Hippler, M.3
  • 30
    • 0038575234 scopus 로고    scopus 로고
    • S-Adenosylmethionine: a wolf in sheep's clothing, or a rich man's Adenosylcobalamin?
    • Frey P.A., and Magnusson O.T. S-Adenosylmethionine: a wolf in sheep's clothing, or a rich man's Adenosylcobalamin?. Chem. Rev. 103 (2003) 2129-2148
    • (2003) Chem. Rev. , vol.103 , pp. 2129-2148
    • Frey, P.A.1    Magnusson, O.T.2
  • 31
    • 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., and Seibert M. 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
  • 32
    • 0033911508 scopus 로고    scopus 로고
    • Differential interaction of maize root ferredoxin:NADP(+) oxidoreductase with photosynthetic and non-photosynthetic ferredoxin isoproteins
    • Onda Y., Matsumura T., Kimata-Ariga Y., Sakakibara H., Sugiyama T., and Hase T. Differential interaction of maize root ferredoxin:NADP(+) oxidoreductase with photosynthetic and non-photosynthetic ferredoxin isoproteins. Plant Physiol. 123 (2000) 1037-1045
    • (2000) Plant Physiol. , vol.123 , pp. 1037-1045
    • Onda, Y.1    Matsumura, T.2    Kimata-Ariga, Y.3    Sakakibara, H.4    Sugiyama, T.5    Hase, T.6


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