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Volumn 71, Issue 1, 2010, Pages 21-26

Analysis of peroxidase activity of rice (Oryza sativa) recombinant hemoglobin 1: Implications for in vivo function of hexacoordinate non-symbiotic hemoglobins in plants

Author keywords

Function; Gramineae; Hemoglobin; Hydrogen peroxide; Non symbiotic; Oryza sativa; Peroxidase; Plants; Rice

Indexed keywords

CARBON MONOXIDE; GUAIACOL; HEMOGLOBIN; HORSERADISH PEROXIDASE; HYDROGEN PEROXIDE; NON SYMBIOTIC HEMOGLOBIN 1 PROTEIN, RICE; NON-SYMBIOTIC HEMOGLOBIN 1 PROTEIN, RICE; PEROXIDASE; RECOMBINANT PROTEIN; SCAVENGER; VEGETABLE PROTEIN;

EID: 72149101608     PISSN: 00319422     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.phytochem.2009.09.016     Document Type: Article
Times cited : (20)

References (43)
  • 1
    • 3242715114 scopus 로고    scopus 로고
    • Reactive oxygen species: metabolism, oxidative stress, and signal transduction
    • Apel K., and Hirt H. Reactive oxygen species: metabolism, oxidative stress, and signal transduction. Ann. Rev. Plant Biol. 55 (2004) 373-399
    • (2004) Ann. Rev. Plant Biol. , vol.55 , pp. 373-399
    • Apel, K.1    Hirt, H.2
  • 4
    • 0031277482 scopus 로고    scopus 로고
    • Rice hemoglobins: gene cloning, analysis and oxygen-binding kinetics of a recombinant protein synthesized in Escherichia coli
    • Arredondo-Peter R., Hargrove M.S., Sarath G., Moran J.F., Lohrman J., Olson J.S., and Klucas R.V. Rice hemoglobins: gene cloning, analysis and oxygen-binding kinetics of a recombinant protein synthesized in Escherichia coli. Plant Physiol. 115 (1997) 1259-1266
    • (1997) Plant Physiol. , vol.115 , pp. 1259-1266
    • Arredondo-Peter, R.1    Hargrove, M.S.2    Sarath, G.3    Moran, J.F.4    Lohrman, J.5    Olson, J.S.6    Klucas, R.V.7
  • 5
    • 0031153920 scopus 로고    scopus 로고
    • Molecular cloning of the cowpea (Vigna unguiculata) leghemoglobin II gene and expression of its cDNA in Escherichia coli; purification and characterization of the recombinant protein
    • Arredondo-Peter R., Moran J.F., Sarath G., Luan P., and Klucas R.V. Molecular cloning of the cowpea (Vigna unguiculata) leghemoglobin II gene and expression of its cDNA in Escherichia coli; purification and characterization of the recombinant protein. Plant Physiol. 114 (1997) 493-500
    • (1997) Plant Physiol. , vol.114 , pp. 493-500
    • Arredondo-Peter, R.1    Moran, J.F.2    Sarath, G.3    Luan, P.4    Klucas, R.V.5
  • 7
    • 0033180574 scopus 로고    scopus 로고
    • Role of active oxygen species and NO in plant defence responses
    • Bolwell G.P. Role of active oxygen species and NO in plant defence responses. Curr. Opin. Plant Biol. 2 (1999) 287-294
    • (1999) Curr. Opin. Plant Biol. , vol.2 , pp. 287-294
    • Bolwell, G.P.1
  • 8
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 9
    • 77957006400 scopus 로고
    • Assay of catalase and peroxidases
    • Chance B., and Maehley A.C. Assay of catalase and peroxidases. Meth. Enzymol. 2 (1955) 764-775
    • (1955) Meth. Enzymol. , vol.2 , pp. 764-775
    • Chance, B.1    Maehley, A.C.2
  • 10
  • 11
    • 0031571165 scopus 로고    scopus 로고
    • Identification of the colored guaiacol oxidation product produced by peroxidases
    • Doerge D.R., Divi R.L., and Churchwell M.I. Identification of the colored guaiacol oxidation product produced by peroxidases. Anal. Biochem. 250 (1997) 10-17
    • (1997) Anal. Biochem. , vol.250 , pp. 10-17
    • Doerge, D.R.1    Divi, R.L.2    Churchwell, M.I.3
  • 12
    • 0141678892 scopus 로고    scopus 로고
    • Expression of a stress-induced hemoglobin affects NO levels produced by alfalfa root cultures under hypoxic stress
    • Dordas C., Hasinoff B.B., Igamberdiev A.U., Manasćh N., Rivoal J., and Hill R.D. Expression of a stress-induced hemoglobin affects NO levels produced by alfalfa root cultures under hypoxic stress. Plant J. 35 (2003) 763-770
    • (2003) Plant J. , vol.35 , pp. 763-770
    • Dordas, C.1    Hasinoff, B.B.2    Igamberdiev, A.U.3    Manasćh, N.4    Rivoal, J.5    Hill, R.D.6
  • 13
    • 1842823269 scopus 로고    scopus 로고
    • Class-1 hemoglobins, nitrate and NO levels in anoxic maize cell-suspension cultures
    • Dordas C., Hasinoff B.B., Rivoal J., and Hill R.D. Class-1 hemoglobins, nitrate and NO levels in anoxic maize cell-suspension cultures. Planta 219 (2004) 66-72
    • (2004) Planta , vol.219 , pp. 66-72
    • Dordas, C.1    Hasinoff, B.B.2    Rivoal, J.3    Hill, R.D.4
  • 14
    • 0030811194 scopus 로고    scopus 로고
    • Expression, purification and properties of recombinant barley (Hordeum sp.) hemoglobin: optical spectra and reactions with gaseous ligands
    • Duff S.M.G., Wittenberg J.B., and Hill R.D. Expression, purification and properties of recombinant barley (Hordeum sp.) hemoglobin: optical spectra and reactions with gaseous ligands. J. Biol. Chem. 272 (1997) 16746-16752
    • (1997) J. Biol. Chem. , vol.272 , pp. 16746-16752
    • Duff, S.M.G.1    Wittenberg, J.B.2    Hill, R.D.3
  • 15
    • 0034623171 scopus 로고    scopus 로고
    • Enhanced peroxidase activity in rice leaves in response to excess iron, copper and zinc
    • Fang W.C., and Kao C.H. Enhanced peroxidase activity in rice leaves in response to excess iron, copper and zinc. Plant Sci. 158 (2000) 71-76
    • (2000) Plant Sci. , vol.158 , pp. 71-76
    • Fang, W.C.1    Kao, C.H.2
  • 16
    • 0033046052 scopus 로고    scopus 로고
    • Signal transduction by reactive oxygen species in non-phagocytic cells
    • Finkel T. Signal transduction by reactive oxygen species in non-phagocytic cells. J. Leukoc. Biol. 65 (1999) 337-340
    • (1999) J. Leukoc. Biol. , vol.65 , pp. 337-340
    • Finkel, T.1
  • 17
    • 33745654570 scopus 로고    scopus 로고
    • Control of plant development by reactive oxygen species
    • Gapper C., and Dolan L. Control of plant development by reactive oxygen species. Plant Physiol. 141 (2006) 341-345
    • (2006) Plant Physiol. , vol.141 , pp. 341-345
    • Gapper, C.1    Dolan, L.2
  • 21
    • 0019023707 scopus 로고
    • Kinetic studies of the reaction of ferric soybean leghemoglobins with hydrogen peroxide, cyanide and nicotinic acid
    • Job D., Zeba B., Puppo A., and Rigaud J. Kinetic studies of the reaction of ferric soybean leghemoglobins with hydrogen peroxide, cyanide and nicotinic acid. Eur. J. Biochem. 107 (1980) 491-500
    • (1980) Eur. J. Biochem. , vol.107 , pp. 491-500
    • Job, D.1    Zeba, B.2    Puppo, A.3    Rigaud, J.4
  • 22
    • 0034960311 scopus 로고    scopus 로고
    • Role of auxin-induced reactive oxygen species in root gravitropism
    • Joo J.H., Bae Y.S., and Lee J.S. Role of auxin-induced reactive oxygen species in root gravitropism. Plant Physiol. 126 (2001) 1055-1060
    • (2001) Plant Physiol. , vol.126 , pp. 1055-1060
    • Joo, J.H.1    Bae, Y.S.2    Lee, J.S.3
  • 23
    • 34147115160 scopus 로고    scopus 로고
    • An investigation of the peroxidase activity of Vitreoscilla hemoglobin
    • Kvist M., Ryabova E.S., and Leif-Bülow E.N. An investigation of the peroxidase activity of Vitreoscilla hemoglobin. J. Biol. Inorg. Chem. 12 (2007) 324-334
    • (2007) J. Biol. Inorg. Chem. , vol.12 , pp. 324-334
    • Kvist, M.1    Ryabova, E.S.2    Leif-Bülow, E.N.3
  • 24
    • 33745678065 scopus 로고    scopus 로고
    • The role of reactive oxygen species in hormonal responses
    • Kwak J.M., Nguyen V., and Schroeder J.I. The role of reactive oxygen species in hormonal responses. Plant Physiol. 141 (2006) 323-329
    • (2006) Plant Physiol. , vol.141 , pp. 323-329
    • Kwak, J.M.1    Nguyen, V.2    Schroeder, J.I.3
  • 25
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assemble of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assemble of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 26
    • 0034903839 scopus 로고    scopus 로고
    • Synthesis of hemoglobins in rice (Oryza sativa var. Jackson) plants growing in normal and stress conditions
    • Lira-Ruan V., Sarath G., Klucas R.V., and Arredondo-Peter R. Synthesis of hemoglobins in rice (Oryza sativa var. Jackson) plants growing in normal and stress conditions. Plant Sci. 161 (2001) 279-287
    • (2001) Plant Sci. , vol.161 , pp. 279-287
    • Lira-Ruan, V.1    Sarath, G.2    Klucas, R.V.3    Arredondo-Peter, R.4
  • 27
    • 15744399426 scopus 로고    scopus 로고
    • Induction of class-1 non-symbiotic hemoglobin genes by nitrate, nitrite and nitric oxide in cultured rice cells
    • Ohwaki Y., Kawagishi-Kobayashi M., Wakasa K., Fujihara S., and Yoneyama T. Induction of class-1 non-symbiotic hemoglobin genes by nitrate, nitrite and nitric oxide in cultured rice cells. Plant Cell Physiol. 46 (2005) 324-331
    • (2005) Plant Cell Physiol. , vol.46 , pp. 324-331
    • Ohwaki, Y.1    Kawagishi-Kobayashi, M.2    Wakasa, K.3    Fujihara, S.4    Yoneyama, T.5
  • 28
    • 34147154024 scopus 로고    scopus 로고
    • Reaction of Mycobacterium tuberculosis truncated hemoglobin O with hydrogen peroxide: evidence for peroxidatic activity and formation of protein-based radicals
    • Ouellet H., Ranguelova K., LaBarre M., Wittenberg J.B., Wittenberg B.A., Magliozzo R.S., and Guertin M. Reaction of Mycobacterium tuberculosis truncated hemoglobin O with hydrogen peroxide: evidence for peroxidatic activity and formation of protein-based radicals. J. Biol. Chem. 282 (2007) 7491-7503
    • (2007) J. Biol. Chem. , vol.282 , pp. 7491-7503
    • Ouellet, H.1    Ranguelova, K.2    LaBarre, M.3    Wittenberg, J.B.4    Wittenberg, B.A.5    Magliozzo, R.S.6    Guertin, M.7
  • 29
    • 0037008194 scopus 로고    scopus 로고
    • Reactive oxygen species in the elongation zone of maize leaves are necessary for leaf extension
    • Rodriguez A.A., Grunberg K.A., and Taleisnik E.L. Reactive oxygen species in the elongation zone of maize leaves are necessary for leaf extension. Plant Physiol. 129 (2002) 1627-1632
    • (2002) Plant Physiol. , vol.129 , pp. 1627-1632
    • Rodriguez, A.A.1    Grunberg, K.A.2    Taleisnik, E.L.3
  • 31
    • 13244272406 scopus 로고    scopus 로고
    • Modeling the tertiary structure of a maize (Zea mays ssp. mays) non-symbiotic hemoglobin
    • Saenz-Rivera J., Sarath G., and Arredondo-Peter R. Modeling the tertiary structure of a maize (Zea mays ssp. mays) non-symbiotic hemoglobin. Plant Physiol. Biochem. 42 (2004) 891-897
    • (2004) Plant Physiol. Biochem. , vol.42 , pp. 891-897
    • Saenz-Rivera, J.1    Sarath, G.2    Arredondo-Peter, R.3
  • 32
    • 4143085079 scopus 로고    scopus 로고
    • Three distinct Arabidopsis hemoglobins exhibit peroxidase-like activity and differentially mediate nitrite-dependent protein nitration
    • Sakamoto A., Sakurao S., Fukunaga K., Matsubara T., Ueda-Hashimoto M., Takahashi M., and Morikawa H. Three distinct Arabidopsis hemoglobins exhibit peroxidase-like activity and differentially mediate nitrite-dependent protein nitration. FEBS Lett. 572 (2004) 27-32
    • (2004) FEBS Lett. , vol.572 , pp. 27-32
    • Sakamoto, A.1    Sakurao, S.2    Fukunaga, K.3    Matsubara, T.4    Ueda-Hashimoto, M.5    Takahashi, M.6    Morikawa, H.7
  • 35
    • 0032544075 scopus 로고    scopus 로고
    • Altering hemoglobin levels changes energy status in maize cells under hypoxia
    • Sowa A.W., Duff S.M.G., Guy P.A., and Hill R.D. Altering hemoglobin levels changes energy status in maize cells under hypoxia. Proc. Natl. Acad. Sci. USA 95 (1998) 10317-10321
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 10317-10321
    • Sowa, A.W.1    Duff, S.M.G.2    Guy, P.A.3    Hill, R.D.4
  • 36
    • 0028384684 scopus 로고
    • A cereal haemoglobin gene is expressed in seed and root tissues under anaerobic conditions
    • Taylor E.R., Nie X.Z., MacGregor A.W., and Hill R.D. A cereal haemoglobin gene is expressed in seed and root tissues under anaerobic conditions. Plant Mol. Biol. 24 (1994) 853-862
    • (1994) Plant Mol. Biol. , vol.24 , pp. 853-862
    • Taylor, E.R.1    Nie, X.Z.2    MacGregor, A.W.3    Hill, R.D.4
  • 37
    • 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 P.E., Ryan D., and Levin W. An improved staining procedure for the detection of the peroxidase activity of cytochrome P-450 on sodium dodecyl sulfate polyacrylamide gels. Anal. Biochem. 75 (1976) 168-176
    • (1976) Anal. Biochem. , vol.75 , pp. 168-176
    • Thomas, P.E.1    Ryan, D.2    Levin, W.3
  • 38
    • 0035918528 scopus 로고    scopus 로고
    • A model for ligand binding to hexacoordinate hemoglobins
    • TrentIII J.T., Hvitved A.N., and Hargrove M.S. A model for ligand binding to hexacoordinate hemoglobins. Biochemistry 40 (2001) 6155-6163
    • (2001) Biochemistry , vol.40 , pp. 6155-6163
    • TrentIII, J.T.1    Hvitved, A.N.2    Hargrove, M.S.3
  • 40
    • 0742324902 scopus 로고    scopus 로고
    • Horseradish peroxidase: a modern view of a classic enzyme
    • Veitch N.C. Horseradish peroxidase: a modern view of a classic enzyme. Phytochemistry 65 (2004) 249-259
    • (2004) Phytochemistry , vol.65 , pp. 249-259
    • Veitch, N.C.1
  • 41
  • 42
    • 0037853210 scopus 로고    scopus 로고
    • Two tomato non-symbiotic haemoglobin genes are differentially expressed in response to diverse changes in mineral nutrient status
    • Wang Y.H., Kochian L.V., Doyle J.J., and Garvin D.F. Two tomato non-symbiotic haemoglobin genes are differentially expressed in response to diverse changes in mineral nutrient status. Plant Cell Environ. 26 (2003) 673-680
    • (2003) Plant Cell Environ. , vol.26 , pp. 673-680
    • Wang, Y.H.1    Kochian, L.V.2    Doyle, J.J.3    Garvin, D.F.4
  • 43
    • 24044440978 scopus 로고    scopus 로고
    • AtGLB1 enhances the tolerance of Arabidopsis to hydrogen peroxide stress
    • Yang L.X., Wang R.Y., Ren F., Liu J., Cheng J., and Lu Y.T. AtGLB1 enhances the tolerance of Arabidopsis to hydrogen peroxide stress. Plant Cell Physiol. 46 (2005) 1309-1316
    • (2005) Plant Cell Physiol. , vol.46 , pp. 1309-1316
    • Yang, L.X.1    Wang, R.Y.2    Ren, F.3    Liu, J.4    Cheng, J.5    Lu, Y.T.6


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