메뉴 건너뛰기




Volumn 176, Issue 6, 2009, Pages 709-714

Iron uptake mechanisms in plants: Functions of the FRO family of ferric reductases

Author keywords

Ferric chelate reductase; Iron; Iron transport mechanisms

Indexed keywords

ARABIDOPSIS;

EID: 63749124124     PISSN: 01689452     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.plantsci.2009.02.011     Document Type: Review
Times cited : (213)

References (68)
  • 1
    • 0026740508 scopus 로고
    • Biologically relevant metal ion-dependent hydroxyl radical generation
    • Halliwell B., and Gutteridge J.M.C. Biologically relevant metal ion-dependent hydroxyl radical generation. FEBS Lett. 307 (1992) 108-112
    • (1992) FEBS Lett. , vol.307 , pp. 108-112
    • Halliwell, B.1    Gutteridge, J.M.C.2
  • 3
    • 51649126661 scopus 로고    scopus 로고
    • Time to pump iron: iron-deficiency-signaling mechanisms of higher plants
    • Walker E.L., and Connolly E.L. Time to pump iron: iron-deficiency-signaling mechanisms of higher plants. Curr. Opin. Plant Biol. 11 (2008) 530-535
    • (2008) Curr. Opin. Plant Biol. , vol.11 , pp. 530-535
    • Walker, E.L.1    Connolly, E.L.2
  • 4
    • 0000527867 scopus 로고
    • Different strategies for iron acquisition in higher plants
    • Romheld V. Different strategies for iron acquisition in higher plants. Physiol. Plant 70 (1987) 231-234
    • (1987) Physiol. Plant , vol.70 , pp. 231-234
    • Romheld, V.1
  • 5
    • 17844402729 scopus 로고    scopus 로고
    • Two plasma membrane H+-ATPase genes are differentially expressed in iron-deficient cucumber plants
    • Santi S., Cesco S., and Pinton V.Z.R. Two plasma membrane H+-ATPase genes are differentially expressed in iron-deficient cucumber plants. Plant Physiol. Biochem. 43 (2005) 287-292
    • (2005) Plant Physiol. Biochem. , vol.43 , pp. 287-292
    • Santi, S.1    Cesco, S.2    Pinton, V.Z.R.3
  • 6
    • 43149086850 scopus 로고    scopus 로고
    • Laser microdissection-assisted analysis of the functional fate of iron deficiency-induced root hairs in cucumber
    • Santi S., and Schmidt W. Laser microdissection-assisted analysis of the functional fate of iron deficiency-induced root hairs in cucumber. J. Exp. Bot. 59 (2008) 697-704
    • (2008) J. Exp. Bot. , vol.59 , pp. 697-704
    • Santi, S.1    Schmidt, W.2
  • 7
    • 18444408674 scopus 로고    scopus 로고
    • The essential basic helix-loop-helix protein FIT1 is required for the iron deficiency response
    • Colangelo E.P., and Guerinot M.L. The essential basic helix-loop-helix protein FIT1 is required for the iron deficiency response. Plant Cell 16 (2004) 3400-3412
    • (2004) Plant Cell , vol.16 , pp. 3400-3412
    • Colangelo, E.P.1    Guerinot, M.L.2
  • 8
    • 8844234980 scopus 로고    scopus 로고
    • FRU (BHLH029) is required for induction of iron mobilization genes in Arabidopsis thaliana
    • Jakoby M., Wang H.Y., Reidt W., Weisshaar B., and Bauer P. FRU (BHLH029) is required for induction of iron mobilization genes in Arabidopsis thaliana. FEBS Lett. 577 (2004) 528-534
    • (2004) FEBS Lett. , vol.577 , pp. 528-534
    • Jakoby, M.1    Wang, H.Y.2    Reidt, W.3    Weisshaar, B.4    Bauer, P.5
  • 9
    • 27944446929 scopus 로고    scopus 로고
    • AtbHLH29 of Arabidopsis thaliana is a functional ortholog of tomato FER involved in controlling iron acquisition in strategy I plants
    • Yuan Y.X., Zhang J., Wang D.W., and Ling H.Q. AtbHLH29 of Arabidopsis thaliana is a functional ortholog of tomato FER involved in controlling iron acquisition in strategy I plants. Cell Res. 15 (2005) 613-621
    • (2005) Cell Res. , vol.15 , pp. 613-621
    • Yuan, Y.X.1    Zhang, J.2    Wang, D.W.3    Ling, H.Q.4
  • 11
    • 0030295014 scopus 로고    scopus 로고
    • Genetic evidence that induction of root Fe(III) chelate reductase activity is necessary for iron uptake under iron deficiency
    • Yi Y., and Guerinot M.L. Genetic evidence that induction of root Fe(III) chelate reductase activity is necessary for iron uptake under iron deficiency. Plant J. 10 (1996) 835-844
    • (1996) Plant J. , vol.10 , pp. 835-844
    • Yi, Y.1    Guerinot, M.L.2
  • 13
    • 0036735024 scopus 로고    scopus 로고
    • The metal ion transporter IRT1 is necessary for iron homeostasis and efficient photosynthesis in Arabidopsis thaliana
    • Varotto C., Maiwald D., Pesaresi P., Jahns P., Francesco S., and Leister D. The metal ion transporter IRT1 is necessary for iron homeostasis and efficient photosynthesis in Arabidopsis thaliana. Plant J. 31 (2002) 589-599
    • (2002) Plant J. , vol.31 , pp. 589-599
    • Varotto, C.1    Maiwald, D.2    Pesaresi, P.3    Jahns, P.4    Francesco, S.5    Leister, D.6
  • 14
    • 0036836922 scopus 로고    scopus 로고
    • Knock-out of Arabidopsis metal transporter gene IRT1 results in iron deficiency accompanied by cell differentiation defects
    • Henriques R., Jasik J., Klein M., Martinoia E., Feller U., Schell J., Pais M.S., and Koncz C. Knock-out of Arabidopsis metal transporter gene IRT1 results in iron deficiency accompanied by cell differentiation defects. Plant Mol. Biol. 50 (2002) 587-597
    • (2002) Plant Mol. Biol. , vol.50 , pp. 587-597
    • Henriques, R.1    Jasik, J.2    Klein, M.3    Martinoia, E.4    Feller, U.5    Schell, J.6    Pais, M.S.7    Koncz, C.8
  • 15
    • 0029891827 scopus 로고    scopus 로고
    • A novel iron-regulated metal transporter from plants identified by functional expression in yeast
    • Eide D., Broderius M., Fett J., and Guerinot M.L. A novel iron-regulated metal transporter from plants identified by functional expression in yeast. Proc. Natl. Acad. Sci. U.S.A. 93 (1996) 5624-5628
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 5624-5628
    • Eide, D.1    Broderius, M.2    Fett, J.3    Guerinot, M.L.4
  • 16
    • 0030785552 scopus 로고    scopus 로고
    • The froh gene family from Arabidopsis thaliana: putative iron-chelate reductases
    • Robinson N.J., Sadjuga, and Groom Q.J. The froh gene family from Arabidopsis thaliana: putative iron-chelate reductases. Plant Soil 196 (1997) 245-248
    • (1997) Plant Soil , vol.196 , pp. 245-248
    • Robinson, N.J.1    Sadjuga2    Groom, Q.J.3
  • 20
    • 33748555572 scopus 로고    scopus 로고
    • Transmembrane topology of FRO2, a ferric chelate reductase from Arabidopsis thaliana
    • Schagerlof U., Wilson G., Herbert H., Al-Karadaghi S., and Hagerhall C. Transmembrane topology of FRO2, a ferric chelate reductase from Arabidopsis thaliana. Plant Mol. Biol. 62 (2006) 215-221
    • (2006) Plant Mol. Biol. , vol.62 , pp. 215-221
    • Schagerlof, U.1    Wilson, G.2    Herbert, H.3    Al-Karadaghi, S.4    Hagerhall, C.5
  • 21
    • 0345392723 scopus 로고    scopus 로고
    • Overexpression of the FRO2 iron reductase confers tolerance to growth on low iron and uncovers post-transcriptional control
    • Connolly E.L., Campbell N., Grotz N., Prichard C.L., and Guerinot M.L. Overexpression of the FRO2 iron reductase confers tolerance to growth on low iron and uncovers post-transcriptional control. Plant Physiol. 133 (2003) 1102-1110
    • (2003) Plant Physiol. , vol.133 , pp. 1102-1110
    • Connolly, E.L.1    Campbell, N.2    Grotz, N.3    Prichard, C.L.4    Guerinot, M.L.5
  • 22
    • 11944267416 scopus 로고
    • Does iron deficiency in Pisum sativum enhance the activity of the root plasmalemma iron transport protein?
    • Grusak M.A., Welch R.M., and Kochian L.V. Does iron deficiency in Pisum sativum enhance the activity of the root plasmalemma iron transport protein?. Plant Physiol. 94 (1990) 1353-1357
    • (1990) Plant Physiol. , vol.94 , pp. 1353-1357
    • Grusak, M.A.1    Welch, R.M.2    Kochian, L.V.3
  • 23
    • 33748950648 scopus 로고    scopus 로고
    • Molecular and phenotypic characterization of transgenic soybean expressing the Arabidopsis ferric chelate reductase gene, FRO2
    • Vasconcelos M., Eckert H., Arahana V., Graef G., Grusak M.A., and Clemente T. Molecular and phenotypic characterization of transgenic soybean expressing the Arabidopsis ferric chelate reductase gene, FRO2. Planta 224 (2006) 1116-1128
    • (2006) Planta , vol.224 , pp. 1116-1128
    • Vasconcelos, M.1    Eckert, H.2    Arahana, V.3    Graef, G.4    Grusak, M.A.5    Clemente, T.6
  • 24
    • 0036000016 scopus 로고    scopus 로고
    • Characterization of FRO1, a pea ferric-chelate reductase involved in root iron acquisition
    • Waters B.M., Blevins D.G., and Eide D.J. Characterization of FRO1, a pea ferric-chelate reductase involved in root iron acquisition. Plant Physiol. 129 (2002) 85-94
    • (2002) Plant Physiol. , vol.129 , pp. 85-94
    • Waters, B.M.1    Blevins, D.G.2    Eide, D.J.3
  • 25
    • 3442888061 scopus 로고    scopus 로고
    • Isolation and characterization of Fe(III)-chelate reductase gene LeFRO1 in tomato
    • Li L., Cheng X., and Ling H.Q. Isolation and characterization of Fe(III)-chelate reductase gene LeFRO1 in tomato. Plant Mol. Biol. 54 (2004) 125-136
    • (2004) Plant Mol. Biol. , vol.54 , pp. 125-136
    • Li, L.1    Cheng, X.2    Ling, H.Q.3
  • 26
    • 34249945129 scopus 로고    scopus 로고
    • Ethylene involvement in the regulation of the H(+)-ATPase CsHA1 gene and of the new isolated ferric reductase CsFRO1 and iron transporter CsIRT1 genes in cucumber plants
    • Waters B.M., Lucena C., Romera F.J., Jester G.G., Wynn A.N., Rojas C.L., Alcantara E., and Perez-Vincente R. Ethylene involvement in the regulation of the H(+)-ATPase CsHA1 gene and of the new isolated ferric reductase CsFRO1 and iron transporter CsIRT1 genes in cucumber plants. Plant Physiol. Biochem. 45 (2007) 293-301
    • (2007) Plant Physiol. Biochem. , vol.45 , pp. 293-301
    • Waters, B.M.1    Lucena, C.2    Romera, F.J.3    Jester, G.G.4    Wynn, A.N.5    Rojas, C.L.6    Alcantara, E.7    Perez-Vincente, R.8
  • 27
    • 33646410449 scopus 로고    scopus 로고
    • Expression profiling of the Arabidopsis ferric chelate reductase (FRO) gene family reveals differential regulation by iron and copper
    • Mukherjee I., Campbell N.H., Ash J.S., and Connolly E.L. Expression profiling of the Arabidopsis ferric chelate reductase (FRO) gene family reveals differential regulation by iron and copper. Planta 223 (2006) 1178-1190
    • (2006) Planta , vol.223 , pp. 1178-1190
    • Mukherjee, I.1    Campbell, N.H.2    Ash, J.S.3    Connolly, E.L.4
  • 28
    • 26444464710 scopus 로고    scopus 로고
    • Molecular and biochemical characterization of the Fe(III) chelate reductase gene family in Arabidopsis thaliana
    • Wu H., Lihua L., Du J., Yuan Y., Cheng X., and Ling H.Q. Molecular and biochemical characterization of the Fe(III) chelate reductase gene family in Arabidopsis thaliana. Plant Cell Physiol. 46 (2005) 1505-1514
    • (2005) Plant Cell Physiol. , vol.46 , pp. 1505-1514
    • Wu, H.1    Lihua, L.2    Du, J.3    Yuan, Y.4    Cheng, X.5    Ling, H.Q.6
  • 29
    • 11144299015 scopus 로고    scopus 로고
    • Analysis of sequence, map position and gene expression reveal conserved essential genes for iron uptake in Arabidopsis and tomato
    • Bauer P., Theil T., Klatte M., Bereczky Z., Brumbarova T., Hell R., and Grosse I. Analysis of sequence, map position and gene expression reveal conserved essential genes for iron uptake in Arabidopsis and tomato. Plant Physiol. 136 (2004) 4169-4183
    • (2004) Plant Physiol. , vol.136 , pp. 4169-4183
    • Bauer, P.1    Theil, T.2    Klatte, M.3    Bereczky, Z.4    Brumbarova, T.5    Hell, R.6    Grosse, I.7
  • 30
    • 33745445728 scopus 로고    scopus 로고
    • Light-regulated, tissue- and cell differentiation-specific expression of the Arabidopsis Fe(III)-chelate reductase gene AtFRO6
    • Feng H., An F., Zhang S., Ji Z., Ling H.-Q., and Zuo J. Light-regulated, tissue- and cell differentiation-specific expression of the Arabidopsis Fe(III)-chelate reductase gene AtFRO6. Plant Physiol. 140 (2006) 1345-1354
    • (2006) Plant Physiol. , vol.140 , pp. 1345-1354
    • Feng, H.1    An, F.2    Zhang, S.3    Ji, Z.4    Ling, H.-Q.5    Zuo, J.6
  • 32
    • 0001262364 scopus 로고
    • Iron translocation: plant culture, exudate sampling, iron citrate analysis
    • Tiffin L.O. Iron translocation: plant culture, exudate sampling, iron citrate analysis. Plant Physiol. 45 (1966) 280-283
    • (1966) Plant Physiol. , vol.45 , pp. 280-283
    • Tiffin, L.O.1
  • 33
    • 0038047698 scopus 로고    scopus 로고
    • Iron uptake, trafficking and homeostasis in plants
    • Hell R., and Stephan U.W. Iron uptake, trafficking and homeostasis in plants. Planta 216 (2003) 541-551
    • (2003) Planta , vol.216 , pp. 541-551
    • Hell, R.1    Stephan, U.W.2
  • 34
    • 0001753508 scopus 로고    scopus 로고
    • Ferric chelate reduction by sunflower (Helianthus annuus L.) leaves: influence of light, oxygen, iron-deficiency and leaf age
    • de la Guardia M.D., and Alcantara E. Ferric chelate reduction by sunflower (Helianthus annuus L.) leaves: influence of light, oxygen, iron-deficiency and leaf age. J. Exp. Bot. 47 (1996) 669-675
    • (1996) J. Exp. Bot. , vol.47 , pp. 669-675
    • de la Guardia, M.D.1    Alcantara, E.2
  • 35
    • 0001690821 scopus 로고
    • Iron uptake by leaf mesophyll cells: the role of the plasma membrane-bound ferric-chelate reductase
    • Brüggemann W., Maas-Kantel K., and Moog P.R. Iron uptake by leaf mesophyll cells: the role of the plasma membrane-bound ferric-chelate reductase. Planta 190 (1993) 151-155
    • (1993) Planta , vol.190 , pp. 151-155
    • Brüggemann, W.1    Maas-Kantel, K.2    Moog, P.R.3
  • 36
    • 48749114297 scopus 로고    scopus 로고
    • Chloroplast Fe(III) chelate reductase activity is essential for seedling viability under iron limiting conditions
    • Jeong J., Cohu C., Kerkeb L., Pilon M., Connolly E.L., and Guerinot M.L. Chloroplast Fe(III) chelate reductase activity is essential for seedling viability under iron limiting conditions. Proc. Natl. Acad. Sci. U.S.A. 105 (2008) 10619-10624
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 10619-10624
    • Jeong, J.1    Cohu, C.2    Kerkeb, L.3    Pilon, M.4    Connolly, E.L.5    Guerinot, M.L.6
  • 37
    • 0035905794 scopus 로고    scopus 로고
    • Maize yellow stripe1 encodes a membrane protein directly involved in Fe(III) uptake
    • Curie C., Panaviene Z., Loulergue C., Dellaporta S.L., Briat J.-F., and Walker E.L. Maize yellow stripe1 encodes a membrane protein directly involved in Fe(III) uptake. Nature 409 (2001) 346-349
    • (2001) Nature , vol.409 , pp. 346-349
    • Curie, C.1    Panaviene, Z.2    Loulergue, C.3    Dellaporta, S.L.4    Briat, J.-F.5    Walker, E.L.6
  • 38
    • 1542305429 scopus 로고    scopus 로고
    • ZmYS1 functions as a proton-coupled symporter for phytosiderophore- and nicotianamine-chelated metals
    • Schaaf G., Ludewig U., Erenoglu B.E., Mori S., Kitahara T., and von Wiren N. ZmYS1 functions as a proton-coupled symporter for phytosiderophore- and nicotianamine-chelated metals. J. Biol. Chem. 279 (2004) 9091-9096
    • (2004) J. Biol. Chem. , vol.279 , pp. 9091-9096
    • Schaaf, G.1    Ludewig, U.2    Erenoglu, B.E.3    Mori, S.4    Kitahara, T.5    von Wiren, N.6
  • 39
    • 33646240063 scopus 로고    scopus 로고
    • A specific transporter for iron(III)-phytosiderophore in barley roots
    • Murata Y., Ma J.F., Yamaji N., Ueno D., Nomoto K., and Iwashita T. A specific transporter for iron(III)-phytosiderophore in barley roots. Plant J. 46 (2006) 563-572
    • (2006) Plant J. , vol.46 , pp. 563-572
    • Murata, Y.1    Ma, J.F.2    Yamaji, N.3    Ueno, D.4    Nomoto, K.5    Iwashita, T.6
  • 40
    • 34248157691 scopus 로고    scopus 로고
    • Mining iron: Iron uptake and transport in plants
    • Kim S.A., and Guerinot M.L. Mining iron: Iron uptake and transport in plants. FEBS Lett. 581 (2007) 2273-2280
    • (2007) FEBS Lett. , vol.581 , pp. 2273-2280
    • Kim, S.A.1    Guerinot, M.L.2
  • 42
    • 37249027651 scopus 로고    scopus 로고
    • Mutation in nicotianamine aminotransferase stimulated the Fe(II) acquisition system and led to iron accumulation in rice
    • Cheng L., Wang F., Shou H., Huang F., Zheng L., He F., Li J., Zhao F.-J., Ueno D., Ma J.F., and Wu P. Mutation in nicotianamine aminotransferase stimulated the Fe(II) acquisition system and led to iron accumulation in rice. Plant Physiol. 145 (2007) 1647-1657
    • (2007) Plant Physiol. , vol.145 , pp. 1647-1657
    • Cheng, L.1    Wang, F.2    Shou, H.3    Huang, F.4    Zheng, L.5    He, F.6    Li, J.7    Zhao, F.-J.8    Ueno, D.9    Ma, J.F.10    Wu, P.11
  • 45
    • 33947418045 scopus 로고    scopus 로고
    • Fractionation of stable iron isotopes in higher plants
    • Guelke M., and Von Blanckenburg F. Fractionation of stable iron isotopes in higher plants. Environ. Sci. Technol. 41 (2007) 1896-1901
    • (2007) Environ. Sci. Technol. , vol.41 , pp. 1896-1901
    • Guelke, M.1    Von Blanckenburg, F.2
  • 46
    • 0032508637 scopus 로고    scopus 로고
    • Metalloregulation of FRE1 and FRE2 homologs in Saccharomyces cerevisiae
    • Martins L.J., Jensen L.T., Simons J.R., Keller G.L., and Winge D.R. Metalloregulation of FRE1 and FRE2 homologs in Saccharomyces cerevisiae. J. Biol. Chem. 273 (1998) 23716-23721
    • (1998) J. Biol. Chem. , vol.273 , pp. 23716-23721
    • Martins, L.J.1    Jensen, L.T.2    Simons, J.R.3    Keller, G.L.4    Winge, D.R.5
  • 47
    • 34547557628 scopus 로고    scopus 로고
    • Identification of a vacuole-associated metalloreductase and its role in Ctr2-mediated intracellular copper mobilization
    • Rees E.M., and Thiele D.J. Identification of a vacuole-associated metalloreductase and its role in Ctr2-mediated intracellular copper mobilization. J. Biol. Chem. 282 (2007) 21629-21638
    • (2007) J. Biol. Chem. , vol.282 , pp. 21629-21638
    • Rees, E.M.1    Thiele, D.J.2
  • 48
    • 35348984430 scopus 로고    scopus 로고
    • The metalloreductase Fre6p in Fe-efflux from the yeast vacuole
    • Singh A., Kaur N., and Kosman D.J. The metalloreductase Fre6p in Fe-efflux from the yeast vacuole. J. Biol. Chem. 282 (2007) 28619-28626
    • (2007) J. Biol. Chem. , vol.282 , pp. 28619-28626
    • Singh, A.1    Kaur, N.2    Kosman, D.J.3
  • 52
    • 0036006057 scopus 로고    scopus 로고
    • Ferrous iron transport across chloroplast inner envelope membranes
    • Shingles R., North M., and McCarty R.E. Ferrous iron transport across chloroplast inner envelope membranes. Plant Physiol. 128 (2002) 1022-1030
    • (2002) Plant Physiol. , vol.128 , pp. 1022-1030
    • Shingles, R.1    North, M.2    McCarty, R.E.3
  • 53
    • 0035050681 scopus 로고    scopus 로고
    • Genes essential to iron transport in the cyanobacterium Synechocystis sp. strain PCC 6803
    • Katoh H., Hagino N., Grossman A.R., and Ogawa T. Genes essential to iron transport in the cyanobacterium Synechocystis sp. strain PCC 6803. J. Bacteriol. 183 (2001) 2779-2784
    • (2001) J. Bacteriol. , vol.183 , pp. 2779-2784
    • Katoh, H.1    Hagino, N.2    Grossman, A.R.3    Ogawa, T.4
  • 54
    • 34248146824 scopus 로고    scopus 로고
    • PIC1, an ancient permease in Arabidopsis chloroplasts, mediates iron transport
    • Duy D., Wanner G., Meda A.R., von Wiren N., Soll J., and Philippar K. PIC1, an ancient permease in Arabidopsis chloroplasts, mediates iron transport. Plant Cell 19 (2007) 986-1006
    • (2007) Plant Cell , vol.19 , pp. 986-1006
    • Duy, D.1    Wanner, G.2    Meda, A.R.3    von Wiren, N.4    Soll, J.5    Philippar, K.6
  • 55
    • 0842270043 scopus 로고    scopus 로고
    • Experimental analysis of the Arabidopsis mitochondrial proteome highlights signaling and regulatory components, provides assessment of targeting prediction programs, and indicates plant-specific mitochondrial proteins
    • Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J., and Millar A.H. Experimental analysis of the Arabidopsis mitochondrial proteome highlights signaling and regulatory components, provides assessment of targeting prediction programs, and indicates plant-specific mitochondrial proteins. The Plant Cell 16 (2004) 241-256
    • (2004) The Plant Cell , vol.16 , pp. 241-256
    • Heazlewood, J.L.1    Tonti-Filippini, J.S.2    Gout, A.M.3    Day, D.A.4    Whelan, J.5    Millar, A.H.6
  • 56
    • 13444264729 scopus 로고    scopus 로고
    • GENEVESTIGATOR. Arabidopsis microarray database and analysis toolbox
    • Zimmermann P., Hirsch-Hoffmann M., Hennig L., and Gruissem W. GENEVESTIGATOR. Arabidopsis microarray database and analysis toolbox. Plant Physiol. 136 (2004) 2621-2632
    • (2004) Plant Physiol. , vol.136 , pp. 2621-2632
    • Zimmermann, P.1    Hirsch-Hoffmann, M.2    Hennig, L.3    Gruissem, W.4
  • 60
    • 14944360174 scopus 로고    scopus 로고
    • Identification of an ascorbate-dependent cytochrome b of the tonoplast membrane sharing biochemical features with members of the cytochrome b561 family
    • Preger V., Scagliarini S., Pupillo P., and Trost P. Identification of an ascorbate-dependent cytochrome b of the tonoplast membrane sharing biochemical features with members of the cytochrome b561 family. Planta 220 (2005) 365-375
    • (2005) Planta , vol.220 , pp. 365-375
    • Preger, V.1    Scagliarini, S.2    Pupillo, P.3    Trost, P.4
  • 61
    • 33947422966 scopus 로고    scopus 로고
    • An Arabidopsis cytochrome b561 with trans-membrane ferrireductase capability
    • Bérczi A., Su D., and Asard H. An Arabidopsis cytochrome b561 with trans-membrane ferrireductase capability. FEBS Lett. 581 (2007) 1505-1508
    • (2007) FEBS Lett. , vol.581 , pp. 1505-1508
    • Bérczi, A.1    Su, D.2    Asard, H.3
  • 62
    • 33745851905 scopus 로고    scopus 로고
    • Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics
    • Reinders J., Zahedi R.P., Pfanner N., Meisinger C., and Sickmann A. Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics. J. Prot. Res. 5 (2006) 1543-1554
    • (2006) J. Prot. Res. , vol.5 , pp. 1543-1554
    • Reinders, J.1    Zahedi, R.P.2    Pfanner, N.3    Meisinger, C.4    Sickmann, A.5
  • 64
    • 34247371015 scopus 로고    scopus 로고
    • Transporters of ligands for essential metal ions in plants
    • Haydon M.J., and Cobbett C.S. Transporters of ligands for essential metal ions in plants. New Phytol. 174 (2007) 499-506
    • (2007) New Phytol. , vol.174 , pp. 499-506
    • Haydon, M.J.1    Cobbett, C.S.2
  • 65
    • 57649183232 scopus 로고    scopus 로고
    • The redox environment in the mitochondrial intermembrane space is maintained separately from the cytosol and matrix
    • Hu J., Dong L., and Outten C.E. The redox environment in the mitochondrial intermembrane space is maintained separately from the cytosol and matrix. J. Biol. Chem. 283 (2008) 29126-29134
    • (2008) J. Biol. Chem. , vol.283 , pp. 29126-29134
    • Hu, J.1    Dong, L.2    Outten, C.E.3
  • 68
    • 51749085365 scopus 로고    scopus 로고
    • The FRO2 ferric reductase is required for glycine betaine's effect on chilling tolerance in Arabidopsis root
    • Einset J., Winge P., Bones A.M., and Connolly E.L. The FRO2 ferric reductase is required for glycine betaine's effect on chilling tolerance in Arabidopsis root. Physiol. Plant 134 (2008) 334-341
    • (2008) Physiol. Plant , vol.134 , pp. 334-341
    • Einset, J.1    Winge, P.2    Bones, A.M.3    Connolly, E.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.