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Volumn 134, Issue 1, 2004, Pages 255-264

A Post Genomic Characterization of Arabidopsis Ferredoxins

Author keywords

[No Author keywords available]

Indexed keywords

GENES; GENETIC ENGINEERING; IMMUNOLOGY; METABOLISM; PHOTOSYNTHESIS; PHYSIOLOGY; PROTEINS;

EID: 0842264043     PISSN: 00320889     EISSN: None     Source Type: Journal    
DOI: 10.1104/pp.103.032755     Document Type: Article
Times cited : (124)

References (31)
  • 1
    • 0032829695 scopus 로고    scopus 로고
    • Comparison of the electrostatic binding sites on the surface of ferredoxin for two ferredoxin-dependent enzymes, ferredoxin-NADP(+) reductase and sulfite reductase
    • Akashi T, Matsumura T, Ideguchi T, Iwakiri K, Kawakatsu T, Taniguchi I, Hase T (1999) Comparison of the electrostatic binding sites on the surface of ferredoxin for two ferredoxin-dependent enzymes, ferredoxin-NADP(+) reductase and sulfite reductase. J Biol Chem 274: 29399-29405
    • (1999) J Biol Chem , vol.274 , pp. 29399-29405
    • Akashi, T.1    Matsumura, T.2    Ideguchi, T.3    Iwakiri, K.4    Kawakatsu, T.5    Taniguchi, I.6    Hase, T.7
  • 3
    • 0029051294 scopus 로고
    • Direct electrochemistry and EPR spectroscopy of spinach ferredoxin mutants with modified electron transfer properties
    • Aliverti A, Hagen WR, Zanetti G (1995) Direct electrochemistry and EPR spectroscopy of spinach ferredoxin mutants with modified electron transfer properties. FEBS Lett 368: 220-224
    • (1995) FEBS Lett , vol.368 , pp. 220-224
    • Aliverti, A.1    Hagen, W.R.2    Zanetti, G.3
  • 4
    • 0001155586 scopus 로고    scopus 로고
    • Photosynthetic and heterotrophic ferredoxin isoproteins are colocalized in fruit plastids of tomato
    • Aoki K, Yamamoto M, Wada K (1998) Photosynthetic and heterotrophic ferredoxin isoproteins are colocalized in fruit plastids of tomato. Plant Physiol 118: 439-449
    • (1998) Plant Physiol , vol.118 , pp. 439-449
    • Aoki, K.1    Yamamoto, M.2    Wada, K.3
  • 5
    • 0034649566 scopus 로고    scopus 로고
    • Analysis of the genome sequence of the flowering plant Arabidopsis thaliana
    • Arabidopsis Genome Initiative (2000) Analysis of the genome sequence of the flowering plant Arabidopsis thaliana. Nature 408: 796-815
    • (2000) Nature , vol.408 , pp. 796-815
  • 6
    • 0023858197 scopus 로고
    • The discovery of ferredoxin: The photosynthetic path
    • Arnon DI (1989) The discovery of ferredoxin: the photosynthetic path. Trends Biochem Sci 13: 30-33
    • (1989) Trends Biochem Sci , vol.13 , pp. 30-33
    • Arnon, D.I.1
  • 7
    • 0036140264 scopus 로고    scopus 로고
    • 2 ferredoxins and structural modelling of 88 plant-type sequences: An analysis of fold and function
    • 2 ferredoxins and structural modelling of 88 plant-type sequences: an analysis of fold and function. Proteins 46: 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
  • 9
    • 0003022798 scopus 로고
    • Molecular cloning and differential expression of the maize ferredoxin family
    • Hase T, Kimata Y, Matsumura T, Sakakibara H (1991a) Molecular cloning and differential expression of the maize ferredoxin family. Plant Physiol 96: 77-83
    • (1991) Plant Physiol , vol.96 , pp. 77-83
    • Hase, T.1    Kimata, Y.2    Matsumura, T.3    Sakakibara, H.4
  • 10
    • 0001454446 scopus 로고
    • Expression of maize ferredoxin cDNA in Escherichia coli: Comparison of photosynthetic and nonphotosynthetic ferredoxin isoproteins and their chimeric molecule
    • Hase T, Mizutani S, Mukohata Y (1991b) Expression of maize ferredoxin cDNA in Escherichia coli: comparison of photosynthetic and nonphotosynthetic ferredoxin isoproteins and their chimeric molecule. Plant Physiol 97: 1395-1401
    • (1991) Plant Physiol , vol.97 , pp. 1395-1401
    • Hase, T.1    Mizutani, S.2    Mukohata, Y.3
  • 11
    • 0020827651 scopus 로고
    • Reduction potential and thermodynamic parameters of adrenodoxin by the use of an anaerobic thin-layer electrode
    • Huang YY, Kimura T (1983) Reduction potential and thermodynamic parameters of adrenodoxin by the use of an anaerobic thin-layer electrode. Anal Biochem 133: 385-393
    • (1983) Anal Biochem , vol.133 , pp. 385-393
    • Huang, Y.Y.1    Kimura, T.2
  • 12
    • 0017814013 scopus 로고
    • In vitro synthesis of chloroplast ferredoxin as a high molecular weight precursor in a cell-free protein synthesizing system from wheat germs
    • Huisman JG, Moorman AF, Verkley FN (1978) In vitro synthesis of chloroplast ferredoxin as a high molecular weight precursor in a cell-free protein synthesizing system from wheat germs. Biochem Biophys Res Commun 82: 1121-1131
    • (1978) Biochem Biophys Res Commun , vol.82 , pp. 1121-1131
    • Huisman, J.G.1    Moorman, A.F.2    Verkley, F.N.3
  • 14
    • 0000145187 scopus 로고
    • Localization of ferredoxin isoproteins in mesophyll and bundle sheath cells in maize leaf
    • Kimata Y, Hase T (1989) Localization of ferredoxin isoproteins in mesophyll and bundle sheath cells in maize leaf. Plant Physiol 89: 1193-1197
    • (1989) Plant Physiol , vol.89 , pp. 1193-1197
    • Kimata, Y.1    Hase, T.2
  • 16
    • 0001038547 scopus 로고    scopus 로고
    • Ferredoxin and ferredoxin dependent enzymes
    • DR Ort, CF Yocum, eds, Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Knaff DB (1996) Ferredoxin and ferredoxin dependent enzymes. In DR Ort, CF Yocum, eds, Oxygenic Photosynthesis: The Light Reactions. Kluwer Academic Publishers, Dordrecht, The Netherlands, pp 333-361
    • (1996) Oxygenic Photosynthesis: The Light Reactions , pp. 333-361
    • Knaff, D.B.1
  • 18
    • 0015581286 scopus 로고
    • Cytochrome c: A thermodynamic study of the relationships among oxidation state, ion-binding and structural parameters: 1. The effects of temperature, pH and electrostatic media on the standard redox potential of cytochrome
    • Margalit R, Schejter A (1973) Cytochrome c: a thermodynamic study of the relationships among oxidation state, ion-binding and structural parameters: 1. The effects of temperature, pH and electrostatic media on the standard redox potential of cytochrome. Eur J Biochem 32: 492-499
    • (1973) Eur J Biochem , vol.32 , pp. 492-499
    • Margalit, R.1    Schejter, A.2
  • 20
    • 0031153934 scopus 로고    scopus 로고
    • A nitrate-inducible ferredoxin in maize roots: Genomic organization and differential expression of two nonphotosynthetic ferredoxin isoproteins
    • Matsumura T, Sakakibara H, Nakano R, Kimata Y, Sugiyama T, Hase T (1997) A nitrate-inducible ferredoxin in maize roots: genomic organization and differential expression of two nonphotosynthetic ferredoxin isoproteins. Plant Physiol 114: 653-660
    • (1997) Plant Physiol , vol.114 , pp. 653-660
    • Matsumura, T.1    Sakakibara, H.2    Nakano, R.3    Kimata, Y.4    Sugiyama, T.5    Hase, T.6
  • 22
    • 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, Hase T (2000) Differential interaction of maize root ferredoxin:NADP(+) oxidoreductase with photosynthetic and non-photosynthetic ferredoxin isoproteins. Plant Physiol 123: 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
  • 23
    • 0037255010 scopus 로고    scopus 로고
    • Differential response of genes for ferredoxin and ferredoxin:NADP+ oxidoreductase to nitrate and light in maize leaves
    • Sakakibara H (2003) Differential response of genes for ferredoxin and ferredoxin:NADP+ oxidoreductase to nitrate and light in maize leaves. J Plant Physiol 160: 65-70
    • (2003) J Plant Physiol , vol.160 , pp. 65-70
    • Sakakibara, H.1
  • 24
    • 0001695169 scopus 로고
    • Isolation and characterization of a ferredoxin gene from Arabidopsis thaliana
    • Somers DE, Caspar T, Quail PH (1990) Isolation and characterization of a ferredoxin gene from Arabidopsis thaliana. Plant Physiol 93: 572-577
    • (1990) Plant Physiol , vol.93 , pp. 572-577
    • Somers, D.E.1    Caspar, T.2    Quail, P.H.3
  • 25
    • 0010227852 scopus 로고
    • An electron transport system in maize roots for reaction of glutamate synthase and nitrite reductase
    • Suzuki A, Oaks A, Jacquot JP, Vidai J, Gadal P (1985) An electron transport system in maize roots for reaction of glutamate synthase and nitrite reductase. Plant Physiol 78: 374-378
    • (1985) Plant Physiol , vol.78 , pp. 374-378
    • Suzuki, A.1    Oaks, A.2    Jacquot, J.P.3    Vidai, J.4    Gadal, P.5
  • 26
    • 0014400751 scopus 로고
    • Oxidation-reduction potentials and stoichiomerry of electron transfer in ferredoxins
    • Tagawa Y, Arnon DI (1968) Oxidation-reduction potentials and stoichiomerry of electron transfer in ferredoxins. Biochim Biophys Acta 153: 602-613
    • (1968) Biochim Biophys Acta , vol.153 , pp. 602-613
    • Tagawa, Y.1    Arnon, D.I.2
  • 27
    • 0040350299 scopus 로고    scopus 로고
    • Electrochemical study of biological functions of particular evolutionary conserved amino acid residues using mutated molecules of maize ferredoxin
    • Taniguchi I, Miyahara A, Iwakiri K, Hirakawa Y, Hayashi Y, Nishiyama K, Akashi T, Hase T (1997) Electrochemical study of biological functions of particular evolutionary conserved amino acid residues using mutated molecules of maize ferredoxin. Chem Lett 1977: 929-930
    • (1997) Chem Lett , vol.1977 , pp. 929-930
    • Taniguchi, I.1    Miyahara, A.2    Iwakiri, K.3    Hirakawa, Y.4    Hayashi, Y.5    Nishiyama, K.6    Akashi, T.7    Hase, T.8
  • 28
    • 0033777345 scopus 로고    scopus 로고
    • Analysis of reductant supply systems for ferredoxin-dependent sulfite reductase in photosynthetic and nonphotosynthetic organs of maize
    • Yonekura-Sakakibara K, Onda Y, Ashikari T, Tanaka Y, Kusumi T, Hase T (2000) Analysis of reductant supply systems for ferredoxin-dependent sulfite reductase in photosynthetic and nonphotosynthetic organs of maize. Plant Physiol 122: 887-894
    • (2000) Plant Physiol , vol.122 , pp. 887-894
    • Yonekura-Sakakibara, K.1    Onda, Y.2    Ashikari, T.3    Tanaka, Y.4    Kusumi, T.5    Hase, T.6
  • 29
    • 0027613997 scopus 로고
    • Light-regulated expression of the Arabidopsis thaliana ferredoxin a gene involves both transcriptional and post-transcriptional processes
    • Vorst O, van Dam F, Weisbeek P, Smeekens S (1993) Light-regulated expression of the Arabidopsis thaliana ferredoxin A gene involves both transcriptional and post-transcriptional processes. Plant J 3: 793-803
    • (1993) Plant J , vol.3 , pp. 793-803
    • Vorst, O.1    Van Dam, F.2    Weisbeek, P.3    Smeekens, S.4
  • 30
    • 0001044278 scopus 로고
    • Ferredoxin isolated from plant non-photosynthetic tissues: Purification and characterization
    • Wada K, Onda M, Matsubara H (1986) Ferredoxin isolated from plant non-photosynthetic tissues: purification and characterization. Plant Cell Physiol 27: 407-415
    • (1986) Plant Cell Physiol , vol.27 , pp. 407-415
    • Wada, K.1    Onda, M.2    Matsubara, H.3
  • 31
    • 0033831570 scopus 로고    scopus 로고
    • Genomic analysis of a nutrient response in Arabidopsis reveals diverse expression patterns and novel metabolic and potential regulatory genes induced by nitrate
    • Wang R, Guegler K, LaBrie ST, Crawford NM (2000) Genomic analysis of a nutrient response in Arabidopsis reveals diverse expression patterns and novel metabolic and potential regulatory genes induced by nitrate. Plant Cell 12: 1491-1509
    • (2000) Plant Cell , vol.12 , pp. 1491-1509
    • Wang, R.1    Guegler, K.2    LaBrie, S.T.3    Crawford, N.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.