메뉴 건너뛰기




Volumn 1797, Issue 5, 2010, Pages 531-542

Horseradish peroxidase-catalyzed oxidation of chlorophyll a with hydrogen peroxide Characterization of the products and mechanism of the reaction

Author keywords

Allomerization; Chlorophyll; Enzyme; Free radical; Oxidation; Peroxidase

Indexed keywords

CHLOROPHYLL A; FREE RADICAL; HORSERADISH PEROXIDASE; HYDROGEN PEROXIDE; PHEOPHYTIN; PHEOPHYTIN A; TRITON X 100; UNCLASSIFIED DRUG;

EID: 77950367547     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2010.01.017     Document Type: Article
Times cited : (40)

References (95)
  • 2
    • 0002154654 scopus 로고
    • Horseradish peroxidase: structure and kinetic properties
    • CRC Press, Boca Raton, FL
    • Dunford H.B. Horseradish peroxidase: structure and kinetic properties. Peroxidases in Chemistry and Biology 1991, vol. 2:1-24. CRC Press, Boca Raton, FL.
    • (1991) Peroxidases in Chemistry and Biology , vol.2 , pp. 1-24
    • Dunford, H.B.1
  • 6
    • 0002037932 scopus 로고
    • Structure and evolution of peroxidases
    • University of Geneva, Geneva, K.G. Welinder, S.K. Rasmussen, C. Penel, H. Greppin (Eds.)
    • Welinder K.G., Gajhede M. Structure and evolution of peroxidases. Plant Peroxidases: Biochemistry and Physiology 1993, 35-42. University of Geneva, Geneva. K.G. Welinder, S.K. Rasmussen, C. Penel, H. Greppin (Eds.).
    • (1993) Plant Peroxidases: Biochemistry and Physiology , pp. 35-42
    • Welinder, K.G.1    Gajhede, M.2
  • 9
    • 12944305786 scopus 로고
    • Superfamily of plant, fungal and bacterial peroxidases
    • Welinder K.G. Superfamily of plant, fungal and bacterial peroxidases. Curr. Opin. Struct. Biol. 1992, 2:388-393.
    • (1992) Curr. Opin. Struct. Biol. , vol.2 , pp. 388-393
    • Welinder, K.G.1
  • 10
    • 0032042908 scopus 로고    scopus 로고
    • Substrate binding and catalysis in heme peroxidases
    • Smith A.T., Veitch N.C. Substrate binding and catalysis in heme peroxidases. Curr. Opin. Chem. Biol. 1998, 2:269-278.
    • (1998) Curr. Opin. Chem. Biol. , vol.2 , pp. 269-278
    • Smith, A.T.1    Veitch, N.C.2
  • 12
    • 23944527027 scopus 로고    scopus 로고
    • Structural determinants of plant peroxidase function
    • Veitch N.C. Structural determinants of plant peroxidase function. Phytochem. Rev. 2004, 3:3-18.
    • (2004) Phytochem. Rev. , vol.3 , pp. 3-18
    • Veitch, N.C.1
  • 13
    • 0000805517 scopus 로고
    • On the function and mechanism of action of peroxidases
    • Dunford H.B., Stillman J.S. On the function and mechanism of action of peroxidases. Coord. Chem. Rev. 1976, 19:187-251.
    • (1976) Coord. Chem. Rev. , vol.19 , pp. 187-251
    • Dunford, H.B.1    Stillman, J.S.2
  • 14
    • 77950367647 scopus 로고    scopus 로고
    • PROMISE mirror
    • PROMISE mirror: http://metallo.scripps.edu/promise/FPBPEROXIDASES.html.
  • 15
    • 4744347907 scopus 로고    scopus 로고
    • Purification and physical-chemical characterization of the three hydroperoxidases from the symbiotic bacterium Sinorhizobium meliloti
    • Ardissone S., Frendo P., Laurenti E., Jantschko W., Obinger C., Puppo A., Ferrari R.P. Purification and physical-chemical characterization of the three hydroperoxidases from the symbiotic bacterium Sinorhizobium meliloti. Biochemistry 2004, 43:12692-12699.
    • (2004) Biochemistry , vol.43 , pp. 12692-12699
    • Ardissone, S.1    Frendo, P.2    Laurenti, E.3    Jantschko, W.4    Obinger, C.5    Puppo, A.6    Ferrari, R.P.7
  • 16
    • 11944266861 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis KatG(S315T) catalase-peroxidase retains all active site properties for proper catalytic function
    • Kapetanaki S.M., Chouchane S., Yu S., Zhao X., Magliozzo R., Schelvis P.M. Mycobacterium tuberculosis KatG(S315T) catalase-peroxidase retains all active site properties for proper catalytic function. Biochemistry 2005, 44:243-252.
    • (2005) Biochemistry , vol.44 , pp. 243-252
    • Kapetanaki, S.M.1    Chouchane, S.2    Yu, S.3    Zhao, X.4    Magliozzo, R.5    Schelvis, P.M.6
  • 18
    • 0030754289 scopus 로고    scopus 로고
    • Formation of chlorins by oxidation of deuteroporphyrin with horseradish peroxidase
    • Pont F., Jacobs N.J., Montforts N.F.-P. Formation of chlorins by oxidation of deuteroporphyrin with horseradish peroxidase. Tetrahedron Lett. 1997, 38:6383-6384.
    • (1997) Tetrahedron Lett. , vol.38 , pp. 6383-6384
    • Pont, F.1    Jacobs, N.J.2    Montforts, N.F.-P.3
  • 20
    • 0037185609 scopus 로고    scopus 로고
    • Benzylic biooxidation of various toluenes to aldehydes by peroxidase
    • Russ R., Zelinski T., Anke T. Benzylic biooxidation of various toluenes to aldehydes by peroxidase. Tetrahedron Lett. 2002, 43:791-793.
    • (2002) Tetrahedron Lett. , vol.43 , pp. 791-793
    • Russ, R.1    Zelinski, T.2    Anke, T.3
  • 21
    • 0037033220 scopus 로고    scopus 로고
    • Chloroperoxidase-catalyzed oxidation of conjugated dienoic esters
    • Bougioukou D.J., Smonou I. Chloroperoxidase-catalyzed oxidation of conjugated dienoic esters. Tetrahedron Lett. 2002, 43:339-342.
    • (2002) Tetrahedron Lett. , vol.43 , pp. 339-342
    • Bougioukou, D.J.1    Smonou, I.2
  • 22
    • 0002204018 scopus 로고
    • Purification of horseradish peroxidase and comparison of its properties with those of catalase and methaemoglobin
    • Keilin D., Hartree E.F. Purification of horseradish peroxidase and comparison of its properties with those of catalase and methaemoglobin. Biochem. J. 1951, 49:88-104.
    • (1951) Biochem. J. , vol.49 , pp. 88-104
    • Keilin, D.1    Hartree, E.F.2
  • 24
    • 0017129482 scopus 로고
    • Substituent effect on the oxidation of phenols and aromatic amines by horseradish peroxidase compound I
    • Job D., Dunford H.B. Substituent effect on the oxidation of phenols and aromatic amines by horseradish peroxidase compound I. Eur. J. Biochem. 1976, 66:607-614.
    • (1976) Eur. J. Biochem. , vol.66 , pp. 607-614
    • Job, D.1    Dunford, H.B.2
  • 25
    • 0030742880 scopus 로고    scopus 로고
    • Catalytic activities and structural properties of horseradish peroxidase distal His42→Gln mutant
    • Tanaka M., Ishimori K., Mukai M., Kitagawa T., Morishima I. Catalytic activities and structural properties of horseradish peroxidase distal His42→Gln mutant. Biochemistry 1997, 36:9889-9898.
    • (1997) Biochemistry , vol.36 , pp. 9889-9898
    • Tanaka, M.1    Ishimori, K.2    Mukai, M.3    Kitagawa, T.4    Morishima, I.5
  • 27
  • 31
    • 0019876656 scopus 로고
    • Electron-nuclear double resonance of horseradish peroxidase compound I
    • Roberts J.E., Hoffman B.M., Rutter R., Hager L.P. Electron-nuclear double resonance of horseradish peroxidase compound I. J. Biol. Chem. 1981, 256:2118-2121.
    • (1981) J. Biol. Chem. , vol.256 , pp. 2118-2121
    • Roberts, J.E.1    Hoffman, B.M.2    Rutter, R.3    Hager, L.P.4
  • 32
    • 0021113923 scopus 로고
    • Chemical nature of porphyrin Π-cation radical in horseradish peroxidase compound I
    • Rutter R., Valentine M., Hendrish M.P., Hager L.P., Debrunner P.G. Chemical nature of porphyrin Π-cation radical in horseradish peroxidase compound I. Biochemistry 1983, 22:4769-4774.
    • (1983) Biochemistry , vol.22 , pp. 4769-4774
    • Rutter, R.1    Valentine, M.2    Hendrish, M.P.3    Hager, L.P.4    Debrunner, P.G.5
  • 35
    • 0003926186 scopus 로고
    • Catabolism of chlorophyll: involvement of a peroxidase?
    • Matile P. Catabolism of chlorophyll: involvement of a peroxidase?. Zeitschr. Pflanzenphysiol. 1980, 99:475-478.
    • (1980) Zeitschr. Pflanzenphysiol. , vol.99 , pp. 475-478
    • Matile, P.1
  • 36
    • 0001055726 scopus 로고
    • Peroxidase-catalyzed oxidation of chlorophyll by hydrogen peroxide
    • Huff A. Peroxidase-catalyzed oxidation of chlorophyll by hydrogen peroxide. Phytochemistry 1982, 21:261-265.
    • (1982) Phytochemistry , vol.21 , pp. 261-265
    • Huff, A.1
  • 37
    • 0001591904 scopus 로고
    • Catabolism of chlorophyll: demonstration of chloroplast-localized peroxidative and oxidative activities
    • Martinoia E., Dalling M.J., Matile P. Catabolism of chlorophyll: demonstration of chloroplast-localized peroxidative and oxidative activities. Zeitschr. Pflanzenphysiol. 1982, 107:269-279.
    • (1982) Zeitschr. Pflanzenphysiol. , vol.107 , pp. 269-279
    • Martinoia, E.1    Dalling, M.J.2    Matile, P.3
  • 38
    • 0000413455 scopus 로고
    • Chlorophyll metabolism in higher plants. VI. Involvement of peroxidase in chlorophyll degradation
    • Kato M., Shimizu S. Chlorophyll metabolism in higher plants. VI. Involvement of peroxidase in chlorophyll degradation. Plant Cell Physiol. 1985, 26:1291-1301.
    • (1985) Plant Cell Physiol. , vol.26 , pp. 1291-1301
    • Kato, M.1    Shimizu, S.2
  • 39
    • 0000296470 scopus 로고
    • Chlorophyll metabolism in higher plants. VII. Chlorophyll degradation in senescing tobacco leaves: phenolic-dependent peroxidative degradation
    • Kato M., Shimizu S. Chlorophyll metabolism in higher plants. VII. Chlorophyll degradation in senescing tobacco leaves: phenolic-dependent peroxidative degradation. Can. J. Bot. 1987, 65:729-735.
    • (1987) Can. J. Bot. , vol.65 , pp. 729-735
    • Kato, M.1    Shimizu, S.2
  • 40
    • 0038814772 scopus 로고    scopus 로고
    • Effect of ethylene and 1-methylcyclopropene on chlorophyll catabolism of broccoli florets
    • Gong Y., Mattheis J.P. Effect of ethylene and 1-methylcyclopropene on chlorophyll catabolism of broccoli florets. Plant Growth Regul. 2003, 40:33-38.
    • (2003) Plant Growth Regul. , vol.40 , pp. 33-38
    • Gong, Y.1    Mattheis, J.P.2
  • 41
    • 0040397176 scopus 로고
    • Thylakoid-associated chlorophyll oxidase - distinction fom lipoxygenase
    • Lüthy B., Martinoia E., Matile P. Thylakoid-associated chlorophyll oxidase - distinction fom lipoxygenase. Zeitschr. Pflanzenphysiol. 1984, 113:423-434.
    • (1984) Zeitschr. Pflanzenphysiol. , vol.113 , pp. 423-434
    • Lüthy, B.1    Martinoia, E.2    Matile, P.3
  • 42
    • 0000034875 scopus 로고
    • Properties of linolenic acid-dependent chlorophyll oxidation in thylakoid membranes
    • Lüthy B., Matile P., Thomas H. Properties of linolenic acid-dependent chlorophyll oxidation in thylakoid membranes. J. Plant Physiol. 1986, 132:169-180.
    • (1986) J. Plant Physiol. , vol.132 , pp. 169-180
    • Lüthy, B.1    Matile, P.2    Thomas, H.3
  • 43
    • 85025532754 scopus 로고
    • Linolenic acid-dependent chlorophyll oxidase activity: a property of photosystem I and II
    • Lüthy B., Thomas H., Matile P. Linolenic acid-dependent chlorophyll oxidase activity: a property of photosystem I and II. J. Plant Physiol. 1986, 123:203-209.
    • (1986) J. Plant Physiol. , vol.123 , pp. 203-209
    • Lüthy, B.1    Thomas, H.2    Matile, P.3
  • 44
    • 0011525264 scopus 로고
    • Leaf senescence in a non-yellowing mutant of Festuca pratensis Huds
    • Thomas H., Lüthy B., Matile P. Leaf senescence in a non-yellowing mutant of Festuca pratensis Huds. Planta 1985, 164:400-405.
    • (1985) Planta , vol.164 , pp. 400-405
    • Thomas, H.1    Lüthy, B.2    Matile, P.3
  • 45
    • 0007625783 scopus 로고
    • The role of unsaturated fatty acids in senescence
    • Thomas H. The role of unsaturated fatty acids in senescence. J. Plant Physiol. 1986, 123:97-105.
    • (1986) J. Plant Physiol. , vol.123 , pp. 97-105
    • Thomas, H.1
  • 46
    • 0002028028 scopus 로고
    • 2-Hydroxychlorophyll a, the first product in the reaction of chlorophyll oxidase
    • 2-Hydroxychlorophyll a, the first product in the reaction of chlorophyll oxidase. J. Plant Physiol. 1984, 115:85-89.
    • (1984) J. Plant Physiol. , vol.115 , pp. 85-89
    • Schoch, S.1    Rüdiger, W.2    Lüthy, B.3    Matile, P.4
  • 47
    • 0005732849 scopus 로고
    • Chlorophyll bleaching by legume seeds - lipoxidase activity of leaves
    • Holden M. Chlorophyll bleaching by legume seeds - lipoxidase activity of leaves. Phytochemistry 1970, 9:507-512.
    • (1970) Phytochemistry , vol.9 , pp. 507-512
    • Holden, M.1
  • 48
    • 85032080326 scopus 로고
    • The degradation of chlorophyll - a biological enigma
    • Hendry G.A.F., Houghton J.D., Brown S.B. The degradation of chlorophyll - a biological enigma. New Phytol. 1987, 107:255-302.
    • (1987) New Phytol. , vol.107 , pp. 255-302
    • Hendry, G.A.F.1    Houghton, J.D.2    Brown, S.B.3
  • 49
    • 0002487607 scopus 로고
    • Chlorophyll breakdown
    • CRC Press, Boca Raton, FL, H. Scheer (Ed.)
    • Brown S.B., Houghton J.D., Hendry G.A.F. Chlorophyll breakdown. Chlorophylls 1991, 465-489. CRC Press, Boca Raton, FL. H. Scheer (Ed.).
    • (1991) Chlorophylls , pp. 465-489
    • Brown, S.B.1    Houghton, J.D.2    Hendry, G.A.F.3
  • 50
    • 23944436084 scopus 로고    scopus 로고
    • Peroxidase-mediated chlorophyll degradation in horticultural crops
    • Yamauchi N., Funamoto Y., Shigyo M. Peroxidase-mediated chlorophyll degradation in horticultural crops. Phytochem. Rev. 2004, 3:221-228.
    • (2004) Phytochem. Rev. , vol.3 , pp. 221-228
    • Yamauchi, N.1    Funamoto, Y.2    Shigyo, M.3
  • 51
    • 0032876883 scopus 로고    scopus 로고
    • Detection of chlorophyll breakdown products in the senescent leaves of higher plants
    • Suzuki Y., Shioi Y. Detection of chlorophyll breakdown products in the senescent leaves of higher plants. Plant Cell Physiol. 1999, 40:909-915.
    • (1999) Plant Cell Physiol. , vol.40 , pp. 909-915
    • Suzuki, Y.1    Shioi, Y.2
  • 52
    • 0032892941 scopus 로고    scopus 로고
    • Determination of chemical oxidation products of chlorophyll and porphyrin by high-performance liquid chromatography
    • Suzuki Y., Tanabe K., Shioi Y. Determination of chemical oxidation products of chlorophyll and porphyrin by high-performance liquid chromatography. J. Chromatogr. A 1999, 839:85-91.
    • (1999) J. Chromatogr. A , vol.839 , pp. 85-91
    • Suzuki, Y.1    Tanabe, K.2    Shioi, Y.3
  • 53
    • 0000314717 scopus 로고    scopus 로고
    • Does peroxidase act as a 'Mg-dechelatase'?
    • http://www.unige.ch/LABPV/newsletters/news113/n13p145.html
    • Azuma R., Takahashi Y., Kurata H., Kawano T., Shimokawa K., Adachi M. Does peroxidase act as a 'Mg-dechelatase'?. Plant Peroxidase Newsletter 1999, 13:145-151. http://www.unige.ch/LABPV/newsletters/news113/n13p145.html.
    • (1999) Plant Peroxidase Newsletter , vol.13 , pp. 145-151
    • Azuma, R.1    Takahashi, Y.2    Kurata, H.3    Kawano, T.4    Shimokawa, K.5    Adachi, M.6
  • 55
    • 21844481520 scopus 로고
    • Catabolism of tetrapyrroles
    • Gossauer A. Catabolism of tetrapyrroles. Chimia 1994, 48:352-361.
    • (1994) Chimia , vol.48 , pp. 352-361
    • Gossauer, A.1
  • 56
    • 0029872091 scopus 로고    scopus 로고
    • Chlorophyll catabolism - structures, mechanisms, conversions
    • Gossauer A., Engel N. Chlorophyll catabolism - structures, mechanisms, conversions. J. Photochem. Photobiol. B Biol. 1996, 32:141-151.
    • (1996) J. Photochem. Photobiol. B Biol. , vol.32 , pp. 141-151
    • Gossauer, A.1    Engel, N.2
  • 59
    • 0038039557 scopus 로고    scopus 로고
    • Solving the riddle of chlorophyll breakdown
    • Kräutler B., Matile P. Solving the riddle of chlorophyll breakdown. Acc. Chem. Res. 1999, 32:35-43.
    • (1999) Acc. Chem. Res. , vol.32 , pp. 35-43
    • Kräutler, B.1    Matile, P.2
  • 61
    • 0033775653 scopus 로고    scopus 로고
    • Degradation pathway(s) of chlorophyll: what has gene cloning revealed?
    • Takamiya K., Tsuchiya T., Ohta H. Degradation pathway(s) of chlorophyll: what has gene cloning revealed?. Trends Plant Sci. 2000, 5:426-431.
    • (2000) Trends Plant Sci. , vol.5 , pp. 426-431
    • Takamiya, K.1    Tsuchiya, T.2    Ohta, H.3
  • 62
    • 33745940126 scopus 로고    scopus 로고
    • Chlorophyll degradation during senescence
    • Hörtensteiner S. Chlorophyll degradation during senescence. Annu. Rev. Plant Biol. 2006, 57:55-77.
    • (2006) Annu. Rev. Plant Biol. , vol.57 , pp. 55-77
    • Hörtensteiner, S.1
  • 63
    • 84945050150 scopus 로고
    • Nomenclature of tetrapyrroles
    • International Union of Pure and Applied Chemistry (IUPAC), International Union of Biochemistry (IUB)International Union of Biochemistry (IUB), G.P. Moss (Ed.)
    • Nomenclature of tetrapyrroles. Pure Appl. Chem. 1987, 59:779-832. International Union of Pure and Applied Chemistry (IUPAC), International Union of Biochemistry (IUB)International Union of Biochemistry (IUB). G.P. Moss (Ed.).
    • (1987) Pure Appl. Chem. , vol.59 , pp. 779-832
  • 65
    • 0000411346 scopus 로고
    • One-electron oxidation of photosynthetic pigments in micelles. Bacteriochlorophyll a, chlorophyll a, and pheophytin a
    • Chauvet J.-P., Santus R., Land E.J. One-electron oxidation of photosynthetic pigments in micelles. Bacteriochlorophyll a, chlorophyll a, and pheophytin a. J. Phys. Chem. 1981, 85:3449-3456.
    • (1981) J. Phys. Chem. , vol.85 , pp. 3449-3456
    • Chauvet, J.-P.1    Santus, R.2    Land, E.J.3
  • 66
    • 0002107763 scopus 로고
    • The structure and chemistry of the functional groups
    • Academic Press, New York, G.R. Seely, L.P. Vernon (Eds.)
    • Seely G.R. The structure and chemistry of the functional groups. The Chlorophylls 1966, 67-109. Academic Press, New York. G.R. Seely, L.P. Vernon (Eds.).
    • (1966) The Chlorophylls , pp. 67-109
    • Seely, G.R.1
  • 67
    • 0011525857 scopus 로고
    • The visible absorption spectra of the phase test intermediates of chlorophyll-a and -b
    • Weller A. The visible absorption spectra of the phase test intermediates of chlorophyll-a and -b. J. Am. Chem. Soc. 1954, 76:5819-5821.
    • (1954) J. Am. Chem. Soc. , vol.76 , pp. 5819-5821
    • Weller, A.1
  • 68
    • 0008524664 scopus 로고
    • The phase test intermediate and the allomerization of chlorophyll a
    • Holt A.S. The phase test intermediate and the allomerization of chlorophyll a. Can. J. Biochem. Physiol. 1958, 36:439-456.
    • (1958) Can. J. Biochem. Physiol. , vol.36 , pp. 439-456
    • Holt, A.S.1
  • 69
    • 19944361930 scopus 로고
    • Formation of phase test intermediate of chlorophyll by electrolytic reduction
    • Felton R., Sherman G.M., Linschitz H. Formation of phase test intermediate of chlorophyll by electrolytic reduction. Nature 1964, 203:637-639.
    • (1964) Nature , vol.203 , pp. 637-639
    • Felton, R.1    Sherman, G.M.2    Linschitz, H.3
  • 70
    • 0000545024 scopus 로고
    • Chemistry of chlorophylls: modifications
    • CRC Press, Boca Raton, FL, H. Scheer (Ed.)
    • Hynninen P.H. Chemistry of chlorophylls: modifications. Chlorophylls 1991, 145-209. CRC Press, Boca Raton, FL. H. Scheer (Ed.).
    • (1991) Chlorophylls , pp. 145-209
    • Hynninen, P.H.1
  • 72
    • 12344298074 scopus 로고
    • 1H NMR spectroscopic study of the phase-test intermediate of chlorophyll a
    • 1H NMR spectroscopic study of the phase-test intermediate of chlorophyll a. Acta Chem. Scand. 1990, 44:235-238.
    • (1990) Acta Chem. Scand. , vol.44 , pp. 235-238
    • Lötjönen, S.1    Hynninen, P.H.2
  • 73
    • 12344312371 scopus 로고    scopus 로고
    • Electronic structure of the enolate anion of chlorophyll b
    • Hynninen P.H., Kavakka J.S., Mesilaakso M. Electronic structure of the enolate anion of chlorophyll b. Tetrahedron Lett. 2005, 46:1145-1147.
    • (2005) Tetrahedron Lett. , vol.46 , pp. 1145-1147
    • Hynninen, P.H.1    Kavakka, J.S.2    Mesilaakso, M.3
  • 74
    • 0000253254 scopus 로고
    • Chlorophylls. V. Isolation of chlorophylls a and b using an improved two-phase extraction method followed by a precipitation and a separation on a sucrose column
    • Hynninen P.H. Chlorophylls. V. Isolation of chlorophylls a and b using an improved two-phase extraction method followed by a precipitation and a separation on a sucrose column. Acta Chem. Scand. 1977, B31:829-835.
    • (1977) Acta Chem. Scand. , vol.31 B , pp. 829-835
    • Hynninen, P.H.1
  • 76
    • 0000354912 scopus 로고
    • Thin-layer chromatography of chlorophylls and their derivatives on sucrose layers
    • Sahlberg I., Hynninen P.H. Thin-layer chromatography of chlorophylls and their derivatives on sucrose layers. J. Chromatogr. 1984, 291:331-338.
    • (1984) J. Chromatogr. , vol.291 , pp. 331-338
    • Sahlberg, I.1    Hynninen, P.H.2
  • 77
    • 84989748197 scopus 로고
    • Large-scale preparation of crystalline (10S)-chlorophylls a and b
    • Hynninen P.H., Lötjönen S. Large-scale preparation of crystalline (10S)-chlorophylls a and b. Synthesis 1983, 9:705-708.
    • (1983) Synthesis , vol.9 , pp. 705-708
    • Hynninen, P.H.1    Lötjönen, S.2
  • 81
    • 0027331428 scopus 로고
    • High-performance liquid chromatographic separation of the methanolic allomerization products of chlorophyll a
    • Kuronen P., Hyvärinen K., Kilpeläinen I., Hynninen P.H. High-performance liquid chromatographic separation of the methanolic allomerization products of chlorophyll a. J. Chromatogr. A 1993, 654:93-104.
    • (1993) J. Chromatogr. A , vol.654 , pp. 93-104
    • Kuronen, P.1    Hyvärinen, K.2    Kilpeläinen, I.3    Hynninen, P.H.4
  • 83
    • 0000577431 scopus 로고
    • Chlorophylls. VI. Epimerization and enolization of chlorophyll a and its magnesium-free derivatives
    • Hynninen P.H., Wasielewski M.R., Katz J.J. Chlorophylls. VI. Epimerization and enolization of chlorophyll a and its magnesium-free derivatives. Acta Chem. Scand. B 1979, 33:637-648.
    • (1979) Acta Chem. Scand. B , vol.33 , pp. 637-648
    • Hynninen, P.H.1    Wasielewski, M.R.2    Katz, J.J.3
  • 85
    • 0000388193 scopus 로고
    • Chlorophylls. II. Allomerization of chlorophylls a and b
    • Hynninen P.H., Assandri S. Chlorophylls. II. Allomerization of chlorophylls a and b. Acta Chem. Scand. 1973, 27:1478-1486.
    • (1973) Acta Chem. Scand. , vol.27 , pp. 1478-1486
    • Hynninen, P.H.1    Assandri, S.2
  • 86
    • 0010104094 scopus 로고    scopus 로고
    • PhotochemCAD: A computer-aided design and research tool in photochemistry
    • http://omlc.ogi.edu/spectra/PhotochemCAD/html/bilirubin.html
    • Du H., Fuh R.A., Li J., Corkan A., Lindsey J.S. PhotochemCAD: A computer-aided design and research tool in photochemistry. Photochem. Photobiol. 1998, 68:141-142. http://omlc.ogi.edu/spectra/PhotochemCAD/html/bilirubin.html.
    • (1998) Photochem. Photobiol. , vol.68 , pp. 141-142
    • Du, H.1    Fuh, R.A.2    Li, J.3    Corkan, A.4    Lindsey, J.S.5
  • 87
    • 0019051943 scopus 로고
    • Preparation of crystalline biliverdin IXα
    • McDonagh A.F., Palma L.A. Preparation of crystalline biliverdin IXα. Biochem. J. 1980, 189:193-208.
    • (1980) Biochem. J. , vol.189 , pp. 193-208
    • McDonagh, A.F.1    Palma, L.A.2
  • 88
    • 84989617488 scopus 로고
    • Steric interaction between the peripheral substituents of 10(S) chlorophyll derivatives and its conformational consequences. A proton magnetic resonance study
    • Hynninen P.H., Lötjönen S. Steric interaction between the peripheral substituents of 10(S) chlorophyll derivatives and its conformational consequences. A proton magnetic resonance study. Org. Magn. Reson. Chem. 1985, 23:605-615.
    • (1985) Org. Magn. Reson. Chem. , vol.23 , pp. 605-615
    • Hynninen, P.H.1    Lötjönen, S.2
  • 89
    • 0000590867 scopus 로고
    • Mechanism of the allomerization of chlorophyll. Inhibition of the allomerization by carotenoid pigments
    • Hynninen P.H. Mechanism of the allomerization of chlorophyll. Inhibition of the allomerization by carotenoid pigments. Z. Naturforsch. 1981, 36b:1010-1016.
    • (1981) Z. Naturforsch. , vol.36 b , pp. 1010-1016
    • Hynninen, P.H.1
  • 90
    • 4243310049 scopus 로고    scopus 로고
    • Recent developments in the research of the chlorophyll allomerization mechanism
    • Hyvärinen K., Hynninen P.H. Recent developments in the research of the chlorophyll allomerization mechanism. Res. Adv. Org. Bioorg. Chem. 2001, 1:1-19.
    • (2001) Res. Adv. Org. Bioorg. Chem. , vol.1 , pp. 1-19
    • Hyvärinen, K.1    Hynninen, P.H.2
  • 92
    • 33847089082 scopus 로고
    • The size, shape, and hydration of nonionic micelles. Triton X-100
    • Robson R.J., Dennis E.A. The size, shape, and hydration of nonionic micelles. Triton X-100. J. Phys. Chem. 1977, 81:1075-1078.
    • (1977) J. Phys. Chem. , vol.81 , pp. 1075-1078
    • Robson, R.J.1    Dennis, E.A.2
  • 93
    • 84981621251 scopus 로고
    • On the nature of chlorophyll a in aqueous micellar systems
    • Mukherjee T., Sapre A.V., Mittal J.P. On the nature of chlorophyll a in aqueous micellar systems. Photochem. Photobiol. 1978, 28:95-96.
    • (1978) Photochem. Photobiol. , vol.28 , pp. 95-96
    • Mukherjee, T.1    Sapre, A.V.2    Mittal, J.P.3
  • 94
    • 0022053378 scopus 로고
    • The reaction of horseradish peroxidase with hydroperoxides derived from Triton X-100
    • Miki T., Orii Y. The reaction of horseradish peroxidase with hydroperoxides derived from Triton X-100. Anal. Biochem. 1984, 146:28-34.
    • (1984) Anal. Biochem. , vol.146 , pp. 28-34
    • Miki, T.1    Orii, Y.2
  • 95
    • 0000290806 scopus 로고
    • A new aspect of the chemistry of chlorins
    • Woodward R.B., Skaric V. A new aspect of the chemistry of chlorins. J. Am. Chem. Soc. 1961, 83:4676-4678.
    • (1961) J. Am. Chem. Soc. , vol.83 , pp. 4676-4678
    • Woodward, R.B.1    Skaric, V.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.