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Volumn 389, Issue 2, 2009, Pages 376-387

Crystal Structure of Red Chlorophyll Catabolite Reductase: Enlargement of the Ferredoxin-Dependent Bilin Reductase Family

Author keywords

bilin reduction; chlorophyll degradation; crystal structure

Indexed keywords

ASPARAGINE; BILIVERDIN; CHLOROPHYLL; FERREDOXIN; GLUTAMINE; HOMODIMER; OXIDOREDUCTASE;

EID: 65549146011     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2009.04.017     Document Type: Article
Times cited : (31)

References (43)
  • 1
    • 33745940126 scopus 로고    scopus 로고
    • Chlorophyll degradation during senescence
    • Hörtensteiner S. Chlorophyll degradation during senescence. Annu. Rev. Plant Biol. 57 (2006) 55-77
    • (2006) Annu. Rev. Plant Biol. , vol.57 , pp. 55-77
    • Hörtensteiner, S.1
  • 2
    • 33745044635 scopus 로고    scopus 로고
    • Chlorophyll catabolites and the biochemistry of chlorophyll breakdown
    • Grimm B., Porra P.J., Rüdiger W., and Sheer H. (Eds), Springer, Dordrecht
    • Kräutler B., and Hörtensteiner S. Chlorophyll catabolites and the biochemistry of chlorophyll breakdown. In: Grimm B., Porra P.J., Rüdiger W., and Sheer H. (Eds). Chlorophylls and Bacteriochlorophylls vol. 25 (2006), Springer, Dordrecht 237-260
    • (2006) Chlorophylls and Bacteriochlorophylls , vol.25 , pp. 237-260
    • Kräutler, B.1    Hörtensteiner, S.2
  • 3
    • 0036443539 scopus 로고    scopus 로고
    • Re-examination of Mg-dechelation reaction in the degradation of chlorophylls using chlorophyllin a as a substrate
    • Suzuki T., and Shioi Y. 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
  • 4
    • 19544367731 scopus 로고    scopus 로고
    • Mg-dechelation activity in radish cotyledons with artificial and native substrates, Mg-chlorophyllin a and chlorophyllide a
    • Suzuki T., Kunieda T., Murai F., Morioka S., and Shioi Y. Mg-dechelation activity in radish cotyledons with artificial and native substrates, Mg-chlorophyllin a and chlorophyllide a. Plant Physiol. Biochem. 43 (2005) 459-464
    • (2005) Plant Physiol. Biochem. , vol.43 , pp. 459-464
    • Suzuki, T.1    Kunieda, T.2    Murai, F.3    Morioka, S.4    Shioi, Y.5
  • 5
    • 0344735844 scopus 로고    scopus 로고
    • Chlorophyll breakdown: pheophorbide a oxygenase is a Rieske-type iron-sulfur protein, encoded by the accelerated cell death 1 gene
    • Pružinskà A., Tanner G., Anders I., Roca M., and Hörtensteiner S. Chlorophyll breakdown: pheophorbide a oxygenase is a Rieske-type iron-sulfur protein, encoded by the accelerated cell death 1 gene. Proc. Natl Acad. Sci. USA 100 (2003) 15259-15264
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 15259-15264
    • Pružinskà, A.1    Tanner, G.2    Anders, I.3    Roca, M.4    Hörtensteiner, S.5
  • 6
    • 0032546794 scopus 로고    scopus 로고
    • The key step in chlorophyll breakdown in higher plants. Cleavage of pheophorbide a macrocycle by a monooxygenase
    • Hörtensteiner S., Wüthrich K.L., Matile P., Ongania K.H., and Kräutler B. The key step in chlorophyll breakdown in higher plants. Cleavage of pheophorbide a macrocycle by a monooxygenase. J. Biol. Chem. 273 (1998) 15335-15339
    • (1998) J. Biol. Chem. , vol.273 , pp. 15335-15339
    • Hörtensteiner, S.1    Wüthrich, K.L.2    Matile, P.3    Ongania, K.H.4    Kräutler, B.5
  • 7
    • 0031401522 scopus 로고    scopus 로고
    • Partial purification and characterization of red chlorophyll catabolite reductase, a stroma protein involved in chlorophyll breakdown
    • Rodoni S., Vicentini F., Schellenberg M., Matile P., and Hörtensteiner S. Partial purification and characterization of red chlorophyll catabolite reductase, a stroma protein involved in chlorophyll breakdown. Plant Physiol. 115 (1997) 677-682
    • (1997) Plant Physiol. , vol.115 , pp. 677-682
    • Rodoni, S.1    Vicentini, F.2    Schellenberg, M.3    Matile, P.4    Hörtensteiner, S.5
  • 8
    • 0031403894 scopus 로고    scopus 로고
    • Chlorophyll breakdown in senescent chloroplasts (cleavage of pheophorbide a in two enzymic steps)
    • Rodoni S., Mühlecker W., Anderl M., Kräutler B., Moser D., Thomas H., et al. Chlorophyll breakdown in senescent chloroplasts (cleavage of pheophorbide a in two enzymic steps). Plant Physiol. 115 (1997) 669-676
    • (1997) Plant Physiol. , vol.115 , pp. 669-676
    • Rodoni, S.1    Mühlecker, W.2    Anderl, M.3    Kräutler, B.4    Moser, D.5    Thomas, H.6
  • 9
  • 10
    • 0037650660 scopus 로고    scopus 로고
    • Molecular cloning, functional expression and characterisation of RCC reductase involved in chlorophyll catabolism
    • Wüthrich K.L., Bovet L., Hunziker P.E., Donnison I.S., and Hörtensteiner S. Molecular cloning, functional expression and characterisation of RCC reductase involved in chlorophyll catabolism. Plant J. 21 (2000) 189-198
    • (2000) Plant J. , vol.21 , pp. 189-198
    • Wüthrich, K.L.1    Bovet, L.2    Hunziker, P.E.3    Donnison, I.S.4    Hörtensteiner, S.5
  • 11
    • 34249788723 scopus 로고    scopus 로고
    • In vivo participation of red chlorophyll catabolite reductase in chlorophyll breakdown
    • Pružinskà A., Anders I., Aubry S., Schenk N., Tapernoux-Luthi E., Muller T., et al. In vivo participation of red chlorophyll catabolite reductase in chlorophyll breakdown. Plant Cell 19 (2007) 369-387
    • (2007) Plant Cell , vol.19 , pp. 369-387
    • Pružinskà, A.1    Anders, I.2    Aubry, S.3    Schenk, N.4    Tapernoux-Luthi, E.5    Muller, T.6
  • 12
    • 0032004066 scopus 로고    scopus 로고
    • AtMRP2, an Arabidopsis ATP binding cassette transporter able to transport glutathione S-conjugates and chlorophyll catabolites: functional comparisons with Atmrp1
    • Lu Y.P., Li Z.S., Drozdowicz Y.M., Hörtensteiner S., Martinoia E., and Rea P.A. AtMRP2, an Arabidopsis ATP binding cassette transporter able to transport glutathione S-conjugates and chlorophyll catabolites: functional comparisons with Atmrp1. Plant Cell 10 (1998) 267-282
    • (1998) Plant Cell , vol.10 , pp. 267-282
    • Lu, Y.P.1    Li, Z.S.2    Drozdowicz, Y.M.3    Hörtensteiner, S.4    Martinoia, E.5    Rea, P.A.6
  • 13
    • 0032033674 scopus 로고    scopus 로고
    • An ABC-transporter of Arabidopsis thaliana has both glutathione-conjugate and chlorophyll catabolite transport activity
    • Tommasini R., Vogt E., Fromenteau M., Hörtensteiner S., Matile P., Amrhein N., and Martinoia E. An ABC-transporter of Arabidopsis thaliana has both glutathione-conjugate and chlorophyll catabolite transport activity. Plant J. 13 (1998) 773-780
    • (1998) Plant J. , vol.13 , pp. 773-780
    • Tommasini, R.1    Vogt, E.2    Fromenteau, M.3    Hörtensteiner, S.4    Matile, P.5    Amrhein, N.6    Martinoia, E.7
  • 14
    • 0037795756 scopus 로고    scopus 로고
    • Breakdown of chlorophyll: a nonenzymatic reaction accounts for the formation of the colorless "nonfluorescent" chlorophyll catabolites
    • Oberhuber M., Berghold J., Breuker K., Hörtensteiner S., and Kräutler B. Breakdown of chlorophyll: a nonenzymatic reaction accounts for the formation of the colorless "nonfluorescent" chlorophyll catabolites. Proc. Natl Acad. Sci. USA 100 (2003) 6910-6915
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 6910-6915
    • Oberhuber, M.1    Berghold, J.2    Breuker, K.3    Hörtensteiner, S.4    Kräutler, B.5
  • 15
    • 33644798323 scopus 로고    scopus 로고
    • Chlorophyll breakdown in senescent Arabidopsis leaves. Characterization of chlorophyll catabolites and of chlorophyll catabolic enzymes involved in the degreening reaction
    • Pružinskà A., Tanner G., Aubry S., Anders I., Moser S., Muller T., et al. Chlorophyll breakdown in senescent Arabidopsis leaves. Characterization of chlorophyll catabolites and of chlorophyll catabolic enzymes involved in the degreening reaction. Plant Physiol. 139 (2005) 52-63
    • (2005) Plant Physiol. , vol.139 , pp. 52-63
    • Pružinskà, A.1    Tanner, G.2    Aubry, S.3    Anders, I.4    Moser, S.5    Muller, T.6
  • 16
    • 0035895231 scopus 로고    scopus 로고
    • The Arabidopsis-accelerated cell death gene ACD2 encodes red chlorophyll catabolite reductase and suppresses the spread of disease symptoms
    • Mach J.M., Castillo A.R., Hoogstraten R., and Greenberg J.T. The Arabidopsis-accelerated cell death gene ACD2 encodes red chlorophyll catabolite reductase and suppresses the spread of disease symptoms. Proc. Natl Acad. Sci. USA 98 (2001) 771-776
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 771-776
    • Mach, J.M.1    Castillo, A.R.2    Hoogstraten, R.3    Greenberg, J.T.4
  • 17
    • 0035032642 scopus 로고    scopus 로고
    • Functional genomic analysis of the HY2 family of ferredoxin-dependent bilin reductases from oxygenic photosynthetic organisms
    • Frankenberg N., Mukougawa K., Kohchi T., and Lagarias J.C. Functional genomic analysis of the HY2 family of ferredoxin-dependent bilin reductases from oxygenic photosynthetic organisms. Plant Cell 13 (2001) 965-978
    • (2001) Plant Cell , vol.13 , pp. 965-978
    • Frankenberg, N.1    Mukougawa, K.2    Kohchi, T.3    Lagarias, J.C.4
  • 18
    • 9844254664 scopus 로고
    • Biosynthesis of phycobilins
    • Beale S.I. Biosynthesis of phycobilins. Chem. Rev. 93 (1993) 785-802
    • (1993) Chem. Rev. , vol.93 , pp. 785-802
    • Beale, S.I.1
  • 19
    • 0033397947 scopus 로고    scopus 로고
    • Prokaryotes and phytochrome. The connection to chromophores and signaling
    • Hughes J., and Lamparter T. Prokaryotes and phytochrome. The connection to chromophores and signaling. Plant Physiol. 121 (1999) 1059-1068
    • (1999) Plant Physiol. , vol.121 , pp. 1059-1068
    • Hughes, J.1    Lamparter, T.2
  • 20
    • 0030028728 scopus 로고    scopus 로고
    • Principles of protein-protein interactions
    • Jones S., and Thornton J.M. Principles of protein-protein interactions. Proc. Natl Acad. Sci. USA 93 (1996) 13-20
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 13-20
    • Jones, S.1    Thornton, J.M.2
  • 21
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., and Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22 (1994) 4673-4680
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 22
    • 33745437116 scopus 로고    scopus 로고
    • Induced-fitting and electrostatic potential change of PcyA upon substrate binding demonstrated by the crystal structure of the substrate-free form
    • Hagiwara Y., Sugishima M., Takahashi Y., and Fukuyama K. Induced-fitting and electrostatic potential change of PcyA upon substrate binding demonstrated by the crystal structure of the substrate-free form. FEBS Lett. 580 (2006) 3823-3828
    • (2006) FEBS Lett. , vol.580 , pp. 3823-3828
    • Hagiwara, Y.1    Sugishima, M.2    Takahashi, Y.3    Fukuyama, K.4
  • 23
    • 33846985274 scopus 로고    scopus 로고
    • Insight into the radical mechanism of phycocyanobilin-ferredoxin oxidoreductase (PcyA) revealed by X-ray crystallography and biochemical measurements
    • Tu S.L., Rockwell N.C., Lagarias J.C., and Fisher A.J. Insight into the radical mechanism of phycocyanobilin-ferredoxin oxidoreductase (PcyA) revealed by X-ray crystallography and biochemical measurements. Biochemistry 46 (2007) 1484-1494
    • (2007) Biochemistry , vol.46 , pp. 1484-1494
    • Tu, S.L.1    Rockwell, N.C.2    Lagarias, J.C.3    Fisher, A.J.4
  • 24
    • 55549106138 scopus 로고    scopus 로고
    • Phycoerythrobilin synthase (PebS) of a marine virus crystal structures of the biliverdin-complex and the substrate free form
    • Dammeyer T., Hofmann E., and Frankenberg-Dinkel N. Phycoerythrobilin synthase (PebS) of a marine virus crystal structures of the biliverdin-complex and the substrate free form. J. Biol. Chem. 283 (2008) 27547-27554
    • (2008) J. Biol. Chem. , vol.283 , pp. 27547-27554
    • Dammeyer, T.1    Hofmann, E.2    Frankenberg-Dinkel, N.3
  • 25
    • 17644392830 scopus 로고    scopus 로고
    • TM-align: a protein structure alignment algorithm based on the TM-score
    • Zhang Y., and Skolnick J. TM-align: a protein structure alignment algorithm based on the TM-score. Nucleic Acids Res. 33 (2005) 2302-2309
    • (2005) Nucleic Acids Res. , vol.33 , pp. 2302-2309
    • Zhang, Y.1    Skolnick, J.2
  • 26
    • 0031715982 scopus 로고    scopus 로고
    • Protein structure alignment by incremental combinatorial extension (CE) of the optimal path
    • Shindyalov I.N., and Bourne P.E. Protein structure alignment by incremental combinatorial extension (CE) of the optimal path. Protein Eng. 11 (1998) 739-747
    • (1998) Protein Eng. , vol.11 , pp. 739-747
    • Shindyalov, I.N.1    Bourne, P.E.2
  • 27
    • 30444438168 scopus 로고    scopus 로고
    • Crystal structure of phycocyanobilin:ferredoxin oxidoreductase in complex with biliverdin IXα, a key enzyme in the biosynthesis of phycocyanobilin
    • Hagiwara Y., Sugishima M., Takahashi Y., and Fukuyama K. Crystal structure of phycocyanobilin:ferredoxin oxidoreductase in complex with biliverdin IXα, a key enzyme in the biosynthesis of phycocyanobilin. Proc. Natl Acad. Sci. USA 103 (2006) 27-32
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 27-32
    • Hagiwara, Y.1    Sugishima, M.2    Takahashi, Y.3    Fukuyama, K.4
  • 28
    • 33745608431 scopus 로고    scopus 로고
    • Crystal structures of BchU, a methyltransferase involved in bacteriochlorophyll c biosynthesis, and its complex with S-adenosylhomocysteine: implications for reaction mechanism
    • Wada K., Yamaguchi H., Harada J., Niimi K., Osumi S., Saga Y., et al. Crystal structures of BchU, a methyltransferase involved in bacteriochlorophyll c biosynthesis, and its complex with S-adenosylhomocysteine: implications for reaction mechanism. J. Mol. Biol. 360 (2006) 839-849
    • (2006) J. Mol. Biol. , vol.360 , pp. 839-849
    • Wada, K.1    Yamaguchi, H.2    Harada, J.3    Niimi, K.4    Osumi, S.5    Saga, Y.6
  • 30
    • 4043169726 scopus 로고    scopus 로고
    • Structure and function of plant-type ferredoxins
    • Fukuyama K. Structure and function of plant-type ferredoxins. Photosynth. Res. 81 (2004) 289-301
    • (2004) Photosynth. Res. , vol.81 , pp. 289-301
    • Fukuyama, K.1
  • 31
    • 55549119284 scopus 로고    scopus 로고
    • Mechanistic studies of the phytochromobilin synthase HY2 from Arabidopsis
    • Tu S.L., Chen H.C., and Ku L.W. Mechanistic studies of the phytochromobilin synthase HY2 from Arabidopsis. J. Biol. Chem. 283 (2008) 27555-27564
    • (2008) J. Biol. Chem. , vol.283 , pp. 27555-27564
    • Tu, S.L.1    Chen, H.C.2    Ku, L.W.3
  • 32
    • 0030593468 scopus 로고    scopus 로고
    • Over-production of proteins in Escherichia coli: mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels
    • Miroux B., and Walker J.E. Over-production of proteins in Escherichia coli: mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels. J. Mol. Biol. 260 (1996) 289-298
    • (1996) J. Mol. Biol. , vol.260 , pp. 289-298
    • Miroux, B.1    Walker, J.E.2
  • 34
    • 85046526624 scopus 로고
    • Evaluation of single-crystal X-ray diffraction data from a position-sensitive detector
    • Kabsch W. Evaluation of single-crystal X-ray diffraction data from a position-sensitive detector. J. Appl. Crystallogr. 21 (1988) 916-924
    • (1988) J. Appl. Crystallogr. , vol.21 , pp. 916-924
    • Kabsch, W.1
  • 35
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. Sect. D 50 (1994) 760-763
    • (1994) Acta Crystallogr. Sect. D , vol.50 , pp. 760-763
  • 36
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997) 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 38
    • 0033896691 scopus 로고    scopus 로고
    • Maximum-likelihood density modification
    • Terwilliger T.C. Maximum-likelihood density modification. Acta Crystallogr. Sect. D 56 (2000) 965-972
    • (2000) Acta Crystallogr. Sect. D , vol.56 , pp. 965-972
    • Terwilliger, T.C.1
  • 39
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit-a versatile program for manipulating atomic coordinates and electron density
    • McRee D.E. XtalView/Xfit-a versatile program for manipulating atomic coordinates and electron density. J. Struct. Biol. 125 (1999) 156-165
    • (1999) J. Struct. Biol. , vol.125 , pp. 156-165
    • McRee, D.E.1
  • 41
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov G.N., Vagin A.A., and Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. Sect. D 53 (1997) 240-255
    • (1997) Acta Crystallogr. Sect. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 42
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: an automated program for molecular replacement
    • Vagin A., and Teplyakov A. MOLREP: an automated program for molecular replacement. J. Appl. Crystallogr. 30 (1997) 1022-1025
    • (1997) J. Appl. Crystallogr. , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 43


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