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Volumn 220, Issue 3, 2005, Pages 365-375

Identification of an ascorbate-dependent cytochrome b of the tonoplast membrane sharing biochemical features with members of the cytochrome b561 family

Author keywords

Ascorbate; Iron; Phaseolus; Plasma membrane; Redox; Vacuole

Indexed keywords

BIOLOGICAL MEMBRANES; CELLS; CHROMATOGRAPHIC ANALYSIS; CYTOLOGY; ENZYMES; ION EXCHANGE; NEGATIVE IONS; SOLUBILITY; SUGAR (SUCROSE);

EID: 14944360174     PISSN: 00320935     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00425-004-1360-0     Document Type: Article
Times cited : (37)

References (51)
  • 1
    • 0021773181 scopus 로고
    • Unusual redox behaviour of cytochrome b-561 from bovine chromaffin granule membranes
    • Apps DK, Boisclair MD, Gavine FS, Pettigrew GW (1984) Unusual redox behaviour of cytochrome b-561 from bovine chromaffin granule membranes. Biochim Biophys Acta 764:8-16
    • (1984) Biochim Biophys Acta , vol.764 , pp. 8-16
    • Apps, D.K.1    Boisclair, M.D.2    Gavine, F.S.3    Pettigrew, G.W.4
  • 2
    • 0002159383 scopus 로고
    • Duroquinone-stimulated NADH oxidase and b type cytochromes in the plasma membrane of cauliflower and mung beans
    • Asard H, Caubergs R, Renders D, De Greef JA (1987) Duroquinone-stimulated NADH oxidase and b type cytochromes in the plasma membrane of cauliflower and mung beans. Plant Sci 53:109-119
    • (1987) Plant Sci , vol.53 , pp. 109-119
    • Asard, H.1    Caubergs, R.2    Renders, D.3    De Greef, J.A.4
  • 4
    • 0026721187 scopus 로고
    • Transmembrane electron transport in ascorbate-loaded plasma membrane vesicles from higher plants involves a b-type cytochrome
    • Asard H, Horemans N, Caubergs RJ (1992) Transmembrane electron transport in ascorbate-loaded plasma membrane vesicles from higher plants involves a b-type cytochrome. FEBS Lett 306:143-146
    • (1992) FEBS Lett , vol.306 , pp. 143-146
    • Asard, H.1    Horemans, N.2    Caubergs, R.J.3
  • 7
    • 0001344391 scopus 로고
    • Cytochromes of plant plasma membranes: Characterization by absorbance difference spectroscopy and redox titration
    • Askerlund P, Larsson C, Widell S (1989) Cytochromes of plant plasma membranes: characterization by absorbance difference spectroscopy and redox titration. Physiol Plant 76:123-134
    • (1989) Physiol Plant , vol.76 , pp. 123-134
    • Askerlund, P.1    Larsson, C.2    Widell, S.3
  • 9
    • 0038348700 scopus 로고    scopus 로고
    • Structure prediction for di-heme cytochrome b-561 protein family
    • Bashtovyy D, Bérczi A, Asard H, Páli T (2003) Structure prediction for di-heme cytochrome b-561 protein family. Protoplasma 221:31-40
    • (2003) Protoplasma , vol.221 , pp. 31-40
    • Bashtovyy, D.1    Bérczi, A.2    Asard, H.3    Páli, T.4
  • 10
    • 0028938278 scopus 로고
    • Iron sequestration by the yeast vacuole. A study with vacuolar mutants of Saccharomyces cerevisiae
    • Bode HP, Dumschat M, Garotti S, Fuhrmann GF (1995) Iron sequestration by the yeast vacuole. A study with vacuolar mutants of Saccharomyces cerevisiae. Eur J Biochem 228:337-342
    • (1995) Eur J Biochem , vol.228 , pp. 337-342
    • Bode, H.P.1    Dumschat, M.2    Garotti, S.3    Fuhrmann, G.F.4
  • 11
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 12
    • 0033564656 scopus 로고    scopus 로고
    • Cellular and subcellular localization of the Nramp2 iron transporter in the intestinal brush border and regulation by dietary iron
    • Canonne-Hergaux F, Gruenheid S, Ponka P, Gros P (1999) Cellular and subcellular localization of the Nramp2 iron transporter in the intestinal brush border and regulation by dietary iron. Blood 93:4406-4417
    • (1999) Blood , vol.93 , pp. 4406-4417
    • Canonne-Hergaux, F.1    Gruenheid, S.2    Ponka, P.3    Gros, P.4
  • 13
    • 0028331764 scopus 로고
    • Mechanism of reduction of quinones by Trypanosoma congolense trypanothione reductase
    • Cenas NK, Arscott D, Williams CH Jr, Blanchard JS (1994) Mechanism of reduction of quinones by Trypanosoma congolense trypanothione reductase. Biochemistry 3:2509-2515
    • (1994) Biochemistry , vol.3 , pp. 2509-2515
    • Cenas, N.K.1    Arscott, D.2    Williams Jr., C.H.3    Blanchard, J.S.4
  • 14
  • 15
    • 1342308497 scopus 로고    scopus 로고
    • Localization of an ascorbate-reducible cytochrome b-561 in the plant tonoplast
    • Griesen D, Su D, Bérczi A, Asard H (2004) Localization of an ascorbate-reducible cytochrome b-561 in the plant tonoplast. Plant Physiol 134:726-734
    • (2004) Plant Physiol , vol.134 , pp. 726-734
    • Griesen, D.1    Su, D.2    Bérczi, A.3    Asard, H.4
  • 17
    • 0021304591 scopus 로고
    • Solubilization of functional membrane proteins
    • Hjelmeland LM, Chrambach A (1984) Solubilization of functional membrane proteins. Methods Enzymol 104:305-318
    • (1984) Methods Enzymol , vol.104 , pp. 305-318
    • Hjelmeland, L.M.1    Chrambach, A.2
  • 18
    • 0028080557 scopus 로고
    • The role of the ascorbate free radical as an electron acceptor to cytochrome b-mediated trans-plasma membrane electron transport in higher plants
    • Horemans N, Asard H, Caubergs R-J (1994) The role of the ascorbate free radical as an electron acceptor to cytochrome b-mediated trans-plasma membrane electron transport in higher plants. Plant Physiol 104:1455-1458
    • (1994) Plant Physiol , vol.104 , pp. 1455-1458
    • Horemans, N.1    Asard, H.2    Caubergs, R.-J.3
  • 19
    • 0018827418 scopus 로고
    • Subcellular distribution of ascorbate in bovine adrenal medulla. Evidence for accumulation in chromaffin granules against a concentration gradient
    • Ingebretsen OC, Terland O, Flatmark T (1980) Subcellular distribution of ascorbate in bovine adrenal medulla. Evidence for accumulation in chromaffin granules against a concentration gradient. Biochim Biophys Acta 628:182-189
    • (1980) Biochim Biophys Acta , vol.628 , pp. 182-189
    • Ingebretsen, O.C.1    Terland, O.2    Flatmark, T.3
  • 20
    • 0035936858 scopus 로고    scopus 로고
    • Chromaffin granule membranes contain at least three heme centers: Direct evidence from EPR and absorption spectroscopy
    • Kamensky YA, Palmer G (2001) Chromaffin granule membranes contain at least three heme centers: direct evidence from EPR and absorption spectroscopy. FEBS Lett 491:119-122
    • (2001) FEBS Lett , vol.491 , pp. 119-122
    • Kamensky, Y.A.1    Palmer, G.2
  • 21
    • 0037024551 scopus 로고    scopus 로고
    • Composition of the heme centers in chromaffin granule cytochrome b-561
    • Kamensky YA, Kulmacz R, Palmer G (2002) Composition of the heme centers in chromaffin granule cytochrome b-561. Ann N Y Acad Sci 971:450-453
    • (2002) Ann N Y Acad Sci , vol.971 , pp. 450-453
    • Kamensky, Y.A.1    Kulmacz, R.2    Palmer, G.3
  • 22
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 23
    • 0035800856 scopus 로고    scopus 로고
    • CCC1 is a transporter that mediates vacuolar iron storage in yeast
    • Li L, Chen OS, McVey Ward D, Kaplan J (2001) CCC1 is a transporter that mediates vacuolar iron storage in yeast. J Biol Chem 276:29515-29519
    • (2001) J Biol Chem , vol.276 , pp. 29515-29519
    • Li, L.1    Chen, O.S.2    McVey Ward, D.3    Kaplan, J.4
  • 24
    • 0025272761 scopus 로고
    • Purification of octyl β-D-glucopyranoside and re-estimation of its micellar size
    • Lorber B, Bishop JB, DeLucas LJ (1990) Purification of octyl β-D-glucopyranoside and re-estimation of its micellar size. Biochim Biophys Acta 1023:254-265
    • (1990) Biochim Biophys Acta , vol.1023 , pp. 254-265
    • Lorber, B.1    Bishop, J.B.2    DeLucas, L.J.3
  • 26
    • 0017632673 scopus 로고
    • Modification of histidyl residues in proteins by diethylpyrocarbonate
    • Miles EW (1977) Modification of histidyl residues in proteins by diethylpyrocarbonate. Methods Enzymol 47:431-442
    • (1977) Methods Enzymol , vol.47 , pp. 431-442
    • Miles, E.W.1
  • 27
    • 0021142747 scopus 로고
    • 2 staining is not specific for heme proteins separated by gel electrophoresis
    • 2 staining is not specific for heme proteins separated by gel electrophoresis. Anal Biochem 140:577-580
    • (1984) Anal Biochem , vol.140 , pp. 577-580
    • Miller, D.J.1    Nicholas, D.J.2
  • 29
    • 0032473867 scopus 로고    scopus 로고
    • Structural basis for the electron transfer across the chromaffin vesicle membranes catalyzed by cytochrome b-561: Analyses of DNA nucleotide sequences and visible absorption spectra
    • Okuyama E, Yamamoto R, Ichikawa Y, Tsubaki M (1998) Structural basis for the electron transfer across the chromaffin vesicle membranes catalyzed by cytochrome b-561: analyses of DNA nucleotide sequences and visible absorption spectra. Biochim Biophys Acta 1383:269-278
    • (1998) Biochim Biophys Acta , vol.1383 , pp. 269-278
    • Okuyama, E.1    Yamamoto, R.2    Ichikawa, Y.3    Tsubaki, M.4
  • 30
    • 0024077919 scopus 로고
    • The structure of cytochrome b561, a secretory vesicle-specific electron transport protein
    • Perin MS, Fried VA, Slaughter CA, Südhof TC (1988) The structure of cytochrome b561, a secretory vesicle-specific electron transport protein. EMBO J 7:2697-2703
    • (1988) EMBO J , vol.7 , pp. 2697-2703
    • Perin, M.S.1    Fried, V.A.2    Slaughter, C.A.3    Südhof, T.C.4
  • 31
    • 0034772773 scopus 로고    scopus 로고
    • Fe homeostasis in plant cells: Does nicotianamine play multiple roles in the regulation of cytoplasmic Fe concentration?
    • Pich A, Manteuffel R, Hillmer S (2001) Fe homeostasis in plant cells: does nicotianamine play multiple roles in the regulation of cytoplasmic Fe concentration? Planta 213:967-976
    • (2001) Planta , vol.213 , pp. 967-976
    • Pich, A.1    Manteuffel, R.2    Hillmer, S.3
  • 32
    • 0035880488 scopus 로고    scopus 로고
    • Domain homologues of dopamine β-hydroxylase and ferric reductase: Roles for iron metabolism in neurodegenerative disorders?
    • Ponting CP (2001) Domain homologues of dopamine β-hydroxylase and ferric reductase: roles for iron metabolism in neurodegenerative disorders? Hum Mol Genet 10:1853-1858
    • (2001) Hum Mol Genet , vol.10 , pp. 1853-1858
    • Ponting, C.P.1
  • 33
    • 0034953893 scopus 로고    scopus 로고
    • Ascorbate-independent electron transfer between cytochrome b-561 and a 27-kDa ascorbate peroxidase of bean hypocotyls
    • Preger V, Pesaresi A, Pupillo P, Trost P (2001) Ascorbate-independent electron transfer between cytochrome b-561 and a 27-kDa ascorbate peroxidase of bean hypocotyls. Protoplasma 217:137-145
    • (2001) Protoplasma , vol.217 , pp. 137-145
    • Preger, V.1    Pesaresi, A.2    Pupillo, P.3    Trost, P.4
  • 34
    • 0024284213 scopus 로고
    • Iron storage in Saccharomyces cerevisiae
    • Raguzzi F, Lesuisse E, Crichton RR (1988) Iron storage in Saccharomyces cerevisiae. FEBS Lett 231:253-258
    • (1988) FEBS Lett , vol.231 , pp. 253-258
    • Raguzzi, F.1    Lesuisse, E.2    Crichton, R.R.3
  • 35
    • 0028066076 scopus 로고
    • Transport of ascorbic and dehydroascorbic acids across protoplast and vacuole membranes isolated from barley (Hordeum vulgare L. cv Gerbel) leaves
    • Rautenkranz AAF, Li L, Mächler F, Martinoia E, Oertli JJ (1994) Transport of ascorbic and dehydroascorbic acids across protoplast and vacuole membranes isolated from barley (Hordeum vulgare L. cv Gerbel) leaves. Plant Physiol 106:187-193
    • (1994) Plant Physiol , vol.106 , pp. 187-193
    • Rautenkranz, A.A.F.1    Li, L.2    Mächler, F.3    Martinoia, E.4    Oertli, J.J.5
  • 36
    • 0032424619 scopus 로고    scopus 로고
    • Initial purification study of the cytochrome b-561 of bean hypocotyl plasma membrane
    • Scagliarini S, Rotino L, Bäurle I, Asard H, Pupillo P, Trost P (1998) Initial purification study of the cytochrome b-561 of bean hypocotyl plasma membrane. Protoplasma 205:66-73
    • (1998) Protoplasma , vol.205 , pp. 66-73
    • Scagliarini, S.1    Rotino, L.2    Bäurle, I.3    Asard, H.4    Pupillo, P.5    Trost, P.6
  • 37
    • 0033452469 scopus 로고    scopus 로고
    • Cloning and heterologous expression of NAD(P)H:quinone reductase of Arabidopsis thaliana, a functional homologue of animal DT-diaphorase
    • Sparla F, Tedeschi G, Pupillo P, Trost P (1999) Cloning and heterologous expression of NAD(P)H:quinone reductase of Arabidopsis thaliana, a functional homologue of animal DT-diaphorase. FEBS Lett 463:382-386
    • (1999) FEBS Lett , vol.463 , pp. 382-386
    • Sparla, F.1    Tedeschi, G.2    Pupillo, P.3    Trost, P.4
  • 38
    • 0002844767 scopus 로고    scopus 로고
    • Systematic analysis of peptide recoveries from in-gel digestions for protein identifications in proteome studies
    • Speicher KD, Kolbas OK, Haper S, Speicher DW (2000) Systematic analysis of peptide recoveries from in-gel digestions for protein identifications in proteome studies. J Biomol Tech 2000:74-86
    • (2000) J Biomol Tech , vol.2000 , pp. 74-86
    • Speicher, K.D.1    Kolbas, O.K.2    Haper, S.3    Speicher, D.W.4
  • 39
    • 0017170673 scopus 로고
    • An improved staining procedure for the detection of the peroxidase activity of cytochrome P-450 on sodium dodecyl sulfate polyacrylamide gels
    • Thomas PE, Ryan D, Levin W (1976) An improved staining procedure for the detection of the peroxidase activity of cytochrome P-450 on sodium dodecyl sulfate polyacrylamide gels. Anal Biochem 75:168-176
    • (1976) Anal Biochem , vol.75 , pp. 168-176
    • Thomas, P.E.1    Ryan, D.2    Levin, W.3
  • 40
    • 0038468540 scopus 로고    scopus 로고
    • AtNRAMP3, a multispecific vacuolar transporter involved in plant responses to iron deficiency
    • Thomine S, Lelièvre F, Debarbieux E, Schroeder JI, Barbier-Brygoo H (2003) AtNRAMP3, a multispecific vacuolar transporter involved in plant responses to iron deficiency. Plant J 34:685-695
    • (2003) Plant J , vol.34 , pp. 685-695
    • Thomine, S.1    Lelièvre, F.2    Debarbieux, E.3    Schroeder, J.I.4    Barbier-Brygoo, H.5
  • 41
    • 0031397296 scopus 로고    scopus 로고
    • Dissecting the diphenylene iodonium-sensitive NAD(P)H: Quinone oxidoreductase of Cucurbita plasma membrane
    • Trost P, Foscarini S, Preger V, Bonora P, Vitale L, Pupillo P (1997) Dissecting the diphenylene iodonium-sensitive NAD(P)H: quinone oxidoreductase of Cucurbita plasma membrane. Plant Physiol 114:737-746
    • (1997) Plant Physiol , vol.114 , pp. 737-746
    • Trost, P.1    Foscarini, S.2    Preger, V.3    Bonora, P.4    Vitale, L.5    Pupillo, P.6
  • 42
    • 0342844282 scopus 로고    scopus 로고
    • Purification of cytochrome b-561 from bean hypocotyls plasma membrane. Evidence for the presence of two heme centers
    • Trost P, Bérczi A, Sparla F, Sponza G, Marzadori B, Asard H, Pupillo P (2000) Purification of cytochrome b-561 from bean hypocotyls plasma membrane. Evidence for the presence of two heme centers. Biochim Biophys Acta 1468:1-5
    • (2000) Biochim Biophys Acta , vol.1468 , pp. 1-5
    • Trost, P.1    Bérczi, A.2    Sparla, F.3    Sponza, G.4    Marzadori, B.5    Asard, H.6    Pupillo, P.7
  • 43
    • 0030817141 scopus 로고    scopus 로고
    • 561 from bovine adrenal chromaffin vesicles as revealed by a new purification procedure and EPR spectroscopy
    • 561 from bovine adrenal chromaffin vesicles as revealed by a new purification procedure and EPR spectroscopy. J Biol Chem 272:23206-23210
    • (1997) J Biol Chem , vol.272 , pp. 23206-23210
    • Tsubaki, M.1    Nakayama, M.2    Okuyama, E.3    Ichikawa, Y.4    Hori, H.5
  • 44
    • 0034724254 scopus 로고    scopus 로고
    • Diethyl pyrocarbonate modification abolishes fast electron accepting ability of cytochrome b561 from ascorbate but does not influence electron donation to monodehydroascorbate radical: Identification of the modification sites by mass spectrometric analysis
    • Tsubaki M, Kobayashi K, Ichise T, Takeuchi F, Tagawa S (2000) Diethyl pyrocarbonate modification abolishes fast electron accepting ability of cytochrome b561 from ascorbate but does not influence electron donation to monodehydroascorbate radical: identification of the modification sites by mass spectrometric analysis. Biochemistry 39:3276-3284
    • (2000) Biochemistry , vol.39 , pp. 3276-3284
    • Tsubaki, M.1    Kobayashi, K.2    Ichise, T.3    Takeuchi, F.4    Tagawa, S.5
  • 45
    • 0011160214 scopus 로고
    • Increase of plasma membrane NADH-duroquinone reductase in tobacco leaves treated with protein-lipopolysaccharide complexes
    • Valenti V, Minardi P, Guerrini F, Mazzucchi U, Pupillo P (1989) Increase of plasma membrane NADH-duroquinone reductase in tobacco leaves treated with protein-lipopolysaccharide complexes. Plant Physiol Biochem 27:569-575
    • (1989) Plant Physiol Biochem , vol.27 , pp. 569-575
    • Valenti, V.1    Minardi, P.2    Guerrini, F.3    Mazzucchi, U.4    Pupillo, P.5
  • 47
    • 0037562593 scopus 로고    scopus 로고
    • A phylogenetic study of cytochrome b561 proteins
    • Verelst W, Asard H (2003) A phylogenetic study of cytochrome b561 proteins. Genome Biol 4:R38
    • (2003) Genome Biol , vol.4
    • Verelst, W.1    Asard, H.2
  • 48
    • 1442291188 scopus 로고    scopus 로고
    • Analysis of an Arabidopsis thaliana protein family, structurally related to cytochromes b561 and potentially involved in cathecolamine biochemistry in plants
    • Verelst W, Asard H (2004) Analysis of an Arabidopsis thaliana protein family, structurally related to cytochromes b561 and potentially involved in cathecolamine biochemistry in plants. J Plant Physiol 161:175-181
    • (2004) J Plant Physiol , vol.161 , pp. 175-181
    • Verelst, W.1    Asard, H.2
  • 49
    • 1642573177 scopus 로고    scopus 로고
    • Tissue-specific expression and developmental regulation of cytochrome b561 genes in Arabidopsis thaliana and Raphanus sativus
    • Verelst W, Kapila J, de Almeida Engler J, Stone JM, Caubergs R, Asard H (2004) Tissue-specific expression and developmental regulation of cytochrome b561 genes in Arabidopsis thaliana and Raphanus sativus. Physiol Plant 120:312-318
    • (2004) Physiol Plant , vol.120 , pp. 312-318
    • Verelst, W.1    Kapila, J.2    De Almeida Engler, J.3    Stone, J.M.4    Caubergs, R.5    Asard, H.6
  • 51
    • 0037378106 scopus 로고    scopus 로고
    • H-induced alteration and oxidative destruction of heme in purified chromaffin granule cytochrome b561: Implications for oxidative stress in catecholaminergic neurons
    • Wanduragala S, Wimalasena DS, Haines D, Kahol P, Wimalasena K (2003) pH-induced alteration and oxidative destruction of heme in purified chromaffin granule cytochrome b561: implications for oxidative stress in catecholaminergic neurons. Biochemistry 42:3617-3626
    • (2003) Biochemistry , vol.42 , pp. 3617-3626
    • Wanduragala, S.1    Wimalasena, D.S.2    Haines, D.3    Kahol, P.4    Wimalasena, K.5


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