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Volumn 169, Issue 1, 2005, Pages 177-183

Search for chlorophyll degradation enzyme, Mg-dechelatase, from extracts of Chenopodium album with native and artificial substrates

Author keywords

Chenopodium album; Chlorophyll degradation; Metal chelating substance; Mg dechelatase; Pheophorbide formation

Indexed keywords

CHELATION; CHLOROPHYLL; CHROMATOGRAPHIC ANALYSIS; CONCENTRATION (PROCESS); DEGRADATION; FILTRATION; MOLECULAR WEIGHT; PLASTICITY; SUBSTRATES;

EID: 19544377162     PISSN: 01689452     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.plantsci.2005.03.010     Document Type: Article
Times cited : (39)

References (32)
  • 1
    • 85032080326 scopus 로고
    • The degradation of chlorophyll - A biological enigma
    • G.A.F. Hendry, J.D. Houghton, and S.B. Brown The degradation of chlorophyll - a biological enigma N. Phytol. 107 1987 255 302
    • (1987) N. Phytol. , vol.107 , pp. 255-302
    • Hendry, G.A.F.1    Houghton, J.D.2    Brown, S.B.3
  • 2
    • 84989726407 scopus 로고
    • Products of chlorophyll photodegradation-1. Detection and separation
    • C.A. Llewellyn, R.F.C. Mantoura, and R.G. Brereton Products of chlorophyll photodegradation-1. Detection and separation Photochem. Photobiol. 52 1990 1037 1041
    • (1990) Photochem. Photobiol. , vol.52 , pp. 1037-1041
    • Llewellyn, C.A.1    Mantoura, R.F.C.2    Brereton, R.G.3
  • 3
    • 84989729961 scopus 로고
    • Products of chlorophyll photodegradation-2. Structural identification
    • C.A. Llewellyn, R.F.C. Mantoura, and R.G. Brereton Products of chlorophyll photodegradation-2. Structural identification Photochem. Photobiol. 52 1990 1043 1047
    • (1990) Photochem. Photobiol. , vol.52 , pp. 1043-1047
    • Llewellyn, C.A.1    Mantoura, R.F.C.2    Brereton, R.G.3
  • 4
    • 0032876883 scopus 로고    scopus 로고
    • Detection of chlorophyll breakdown products in the senescent leaves of higher plants
    • Y. Suzuki, and Y. Shioi Detection of chlorophyll breakdown products in the senescent leaves of higher plants Plant Cell Physiol. 40 1999 909 915
    • (1999) Plant Cell Physiol. , vol.40 , pp. 909-915
    • Suzuki, Y.1    Shioi, Y.2
  • 5
    • 0038039557 scopus 로고    scopus 로고
    • Solving the riddle of chlorophyll breakdown
    • B. Kräutler, and P. Matile Solving the riddle of chlorophyll breakdown Acc. Chem. Res. 32 1999 35 43
    • (1999) Acc. Chem. Res. , vol.32 , pp. 35-43
    • Kräutler, B.1    Matile, P.2
  • 7
    • 0033775653 scopus 로고    scopus 로고
    • Degradation pathway(s) of chlorophyll: What has gene cloning revealed?
    • K. Takamiya, T. Tsuchiya, and H. Ohta Degradation pathway(s) of chlorophyll: what has gene cloning revealed? Trends Plant Sci. 5 2000 426 431
    • (2000) Trends Plant Sci. , vol.5 , pp. 426-431
    • Takamiya, K.1    Tsuchiya, T.2    Ohta, H.3
  • 8
    • 0002002757 scopus 로고    scopus 로고
    • Conversion of chlorophyllide to pheophorbide by Mg-dechelation substance in extracts of Chenopodium album
    • Y. Shioi, N. Tomita, T. Tsuchiya, and K. Takamiya Conversion of chlorophyllide to pheophorbide by Mg-dechelation substance in extracts of Chenopodium album Plant Physiol. Biochem. 34 1996 41 47
    • (1996) Plant Physiol. Biochem. , vol.34 , pp. 41-47
    • Shioi, Y.1    Tomita, N.2    Tsuchiya, T.3    Takamiya, K.4
  • 9
    • 0034494568 scopus 로고    scopus 로고
    • Removal of magnesium by Mg-dechelatase is a major step in the chlorophyll-degrading pathway in Ginkgo biloba in the process of autumnal tints
    • L. Tan, A. Okazawa, E. Fukusaki, and A. Kobayashi Removal of magnesium by Mg-dechelatase is a major step in the chlorophyll-degrading pathway in Ginkgo biloba in the process of autumnal tints Z. Naturforsch. 55c 2000 923 926
    • (2000) Z. Naturforsch. , vol.55 , pp. 923-926
    • Tan, L.1    Okazawa, A.2    Fukusaki, E.3    Kobayashi, A.4
  • 10
    • 0036487185 scopus 로고    scopus 로고
    • Characterization of Mg-dechelatase activity obtained from Fragaria x ananassa fruit
    • M.L. Costa, P.M. Cievello, A.R. Chaves, and G.A. Martínes Characterization of Mg-dechelatase activity obtained from Fragaria x ananassa fruit Plant Physiol. Biochem. 40 2002 111 118
    • (2002) Plant Physiol. Biochem. , vol.40 , pp. 111-118
    • Costa, M.L.1    Cievello, P.M.2    Chaves, A.R.3    Martínes, G.A.4
  • 11
    • 0036443539 scopus 로고    scopus 로고
    • Re-examination of Mg-dechelation reaction in the degradation of chlorophylls using chlorophyllin a as a substrate
    • T. Suzuki, and Y. Shioi Re-examination of Mg-dechelation reaction in the degradation of chlorophylls using chlorophyllin a as a substrate Photosynth. Res. 74 2002 217 223
    • (2002) Photosynth. Res. , vol.74 , pp. 217-223
    • Suzuki, T.1    Shioi, Y.2
  • 13
    • 0036202462 scopus 로고    scopus 로고
    • Plant glutathione transferases
    • D.P. Dixon, A. Lapthorn, and R. Edwards Plant glutathione transferases Genome Biol. 3 2002 3004.1 3004.10 (reviews)
    • (2002) Genome Biol. , vol.3 , pp. 30041-300410
    • Dixon, D.P.1    Lapthorn, A.2    Edwards, R.3
  • 14
    • 0027236637 scopus 로고
    • A glutathione S-transferase with glutathione-peroxidase activity from Arabidopsis thaliana. Molecular cloning and functional characterization
    • D. Bartling, R. Radzio, U. Steiner, and E.W. Weiler A glutathione S-transferase with glutathione-peroxidase activity from Arabidopsis thaliana. Molecular cloning and functional characterization Eur. J. Biochem. 216 1993 579 586
    • (1993) Eur. J. Biochem. , vol.216 , pp. 579-586
    • Bartling, D.1    Radzio, R.2    Steiner, U.3    Weiler, E.W.4
  • 15
    • 0033136432 scopus 로고    scopus 로고
    • A role for glutathione transferases functioning as glutathione peroxidases in resistance to multiple herbicides in black-grass
    • I. Cummins, D.J. Cole, and R. Edwards A role for glutathione transferases functioning as glutathione peroxidases in resistance to multiple herbicides in black-grass Plant J. 18 1999 285 292
    • (1999) Plant J. , vol.18 , pp. 285-292
    • Cummins, I.1    Cole, D.J.2    Edwards, R.3
  • 16
    • 0034541507 scopus 로고    scopus 로고
    • Stress tolerance in transgenic tobacco seedlings that overexpress glutathione S-transferase/glutathione peroxidase
    • V.P. Roxas, S.A. Lodhi, D.K. Garrett, J.R. Mahan, and R.D. Allen Stress tolerance in transgenic tobacco seedlings that overexpress glutathione S-transferase/glutathione peroxidase Plant Cell Physiol. 41 2000 1229 1234
    • (2000) Plant Cell Physiol. , vol.41 , pp. 1229-1234
    • Roxas, V.P.1    Lodhi, S.A.2    Garrett, D.K.3    Mahan, J.R.4    Allen, R.D.5
  • 17
    • 0034525005 scopus 로고    scopus 로고
    • Isolation, purification, and characterization of glutathione S-transferase from oat (Avena sativa) seedlings
    • V.T. Zachariah, N. Walsh-Sayles, and B.R. Singh Isolation, purification, and characterization of glutathione S-transferase from oat (Avena sativa) seedlings J. Protein Chem. 19 2000 425 430
    • (2000) J. Protein Chem. , vol.19 , pp. 425-430
    • Zachariah, V.T.1    Walsh-Sayles, N.2    Singh, B.R.3
  • 18
    • 0029139320 scopus 로고
    • Development of an assay for Mg-dechelatase of oilseed rape cotyledons, using chlorophyllin as the substrate
    • F. Vicentini, F. Iten, and P. Matile Development of an assay for Mg-dechelatase of oilseed rape cotyledons, using chlorophyllin as the substrate Physiol. Plant 94 1995 57 63
    • (1995) Physiol. Plant , vol.94 , pp. 57-63
    • Vicentini, F.1    Iten, F.2    Matile, P.3
  • 19
    • 0030820255 scopus 로고    scopus 로고
    • Purification and characterization of two isozymes of chlorophyllase from mature leaves of Chenopodium album
    • T. Tsuchiya, H. Ohta, K. Okawa, T. Masuda, B. Mikami, N. Kita, Y. Shioi, and K. Takamiya Purification and characterization of two isozymes of chlorophyllase from mature leaves of Chenopodium album Plant Cell Physiol. 38 1997 1026 1031
    • (1997) Plant Cell Physiol. , vol.38 , pp. 1026-1031
    • Tsuchiya, T.1    Ohta, H.2    Okawa, K.3    Masuda, T.4    Mikami, B.5    Kita, N.6    Shioi, Y.7    Takamiya, K.8
  • 20
    • 0032114287 scopus 로고    scopus 로고
    • Isolation and characterization of glutathione S-transferase isozymes from sorghum
    • J.W. Gronwald, and K.L. Plaisance Isolation and characterization of glutathione S-transferase isozymes from sorghum Plant Physiol. 117 1998 877 892
    • (1998) Plant Physiol. , vol.117 , pp. 877-892
    • Gronwald, J.W.1    Plaisance, K.L.2
  • 21
    • 0029124320 scopus 로고
    • Breakdown of chlorophylls by soluble proteins extracted from leaves of Chenopodium album
    • Y. Shioi, T. Masuda, K. Takamiya, and K. Shimokawa Breakdown of chlorophylls by soluble proteins extracted from leaves of Chenopodium album J. Plant Physiol. 145 1995 416 421
    • (1995) J. Plant Physiol. , vol.145 , pp. 416-421
    • Shioi, Y.1    Masuda, T.2    Takamiya, K.3    Shimokawa, K.4
  • 22
    • 0000411157 scopus 로고
    • Absorption of light by chlorophyll solutions
    • G. Mackinney Absorption of light by chlorophyll solutions J. Biol. Chem. 140 1941 315 322
    • (1941) J. Biol. Chem. , vol.140 , pp. 315-322
    • MacKinney, G.1
  • 23
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford 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
  • 24
    • 0002107763 scopus 로고
    • The structure and chemistry of functional groups
    • L.P. Vernon G.R. Seely Academic Press New York
    • G.R. Seely The structure and chemistry of functional groups L.P. Vernon G.R. Seely The Chlorophylls 1966 Academic Press New York 67 109
    • (1966) The Chlorophylls , pp. 67-109
    • Seely, G.R.1
  • 25
    • 3543012839 scopus 로고
    • An analog computer for pyrrole, porphyrin, and chlorophyll strains
    • A.H. Corwin, J.A. Walter, and R. Singh An analog computer for pyrrole, porphyrin, and chlorophyll strains J. Org. Chem. 27 1962 4280 4285
    • (1962) J. Org. Chem. , vol.27 , pp. 4280-4285
    • Corwin, A.H.1    Walter, J.A.2    Singh, R.3
  • 26
    • 2542618972 scopus 로고
    • Stabilities of magnesium chelates of porphyrins and chlorines
    • A.H. Corwin, and P.E. Wei Stabilities of magnesium chelates of porphyrins and chlorines J. Org. Chem. 27 1962 4285 4290
    • (1962) J. Org. Chem. , vol.27 , pp. 4285-4290
    • Corwin, A.H.1    Wei, P.E.2
  • 28
    • 0029608733 scopus 로고
    • Phytochelatins and related peptides, structure, biosynthesis and function
    • W.E. Rauser Phytochelatins and related peptides, structure, biosynthesis and function Plant Physiol. 109 1995 1141 1149
    • (1995) Plant Physiol. , vol.109 , pp. 1141-1149
    • Rauser, W.E.1
  • 30
    • 84948277019 scopus 로고
    • Physiological aspect of mugineic acid, a possible phytosiderophore of graminaceous plants
    • S. Takagi, K. Nomoto, and T. Takemoto Physiological aspect of mugineic acid, a possible phytosiderophore of graminaceous plants J. Plant Nutr. 7 1984 469 477
    • (1984) J. Plant Nutr. , vol.7 , pp. 469-477
    • Takagi, S.1    Nomoto, K.2    Takemoto, T.3
  • 31
    • 0001492898 scopus 로고
    • The regulation of iron uptake and possible functions of nicotianamine in higher plants
    • G. Scholz, R. Becker, U.W. Stephan, A. Rudolph, and A. Pich The regulation of iron uptake and possible functions of nicotianamine in higher plants Biochem. Physiol. Pflanz. 183 1988 257 269
    • (1988) Biochem. Physiol. Pflanz. , vol.183 , pp. 257-269
    • Scholz, G.1    Becker, R.2    Stephan, U.W.3    Rudolph, A.4    Pich, A.5
  • 32
    • 19544367731 scopus 로고    scopus 로고
    • Mg-dechelation activity in radish cotyledons with artificial and native substrates, Mg-chlorophyllin a and chlorophyllide a
    • in press.
    • T. Suzuki, T. Kunieda, F. Murai, S. Morioka, Y. Shioi, Mg-dechelation activity in radish cotyledons with artificial and native substrates, Mg-chlorophyllin a and chlorophyllide a, Plant Physiol. Biochem. (2005), in press.
    • (2005) Plant Physiol. Biochem.
    • Suzuki, T.1    Kunieda, T.2    Murai, F.3    Morioka, S.4    Shioi, Y.5


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