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Volumn 1657, Issue 2-3, 2004, Pages 131-145

Nonenzymatic chromophore attachment in biliproteins: Conformational control by the detergent Triton X-100

Author keywords

CPC; subunit of CPC; CPC; subunit of CPC; aa; allophycocyanin; amino acid; APC; apoprotein of CPC; Attachment; C phycocyanin; Chromophore; Chromophore conformation; CPC; CpcA; CpcB; Cyanobacteria; Photosynthesis; Phycobiliprotein

Indexed keywords

ASCORBIC ACID; DETERGENT; PHYCOBILIPROTEIN; TRITON X 100;

EID: 3242705066     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2004.04.010     Document Type: Article
Times cited : (27)

References (62)
  • 2
    • 0000370919 scopus 로고
    • Adaptive variations in Phycobilisome structure
    • Glazer A.N. Adaptive variations in Phycobilisome structure. Adv. Mol. Cell. Biol. 10:1994;119-149
    • (1994) Adv. Mol. Cell. Biol. , vol.10 , pp. 119-149
    • Glazer, A.N.1
  • 3
    • 0027329062 scopus 로고
    • The Phycobilisome, a light-harvesting complex responsive to environmental conditions
    • Grossman A.R., Schaefer M.R., Chiang G.G., Collier J.L. The Phycobilisome, a light-harvesting complex responsive to environmental conditions. Microbiol. Rev. 57:1993;725-749
    • (1993) Microbiol. Rev. , vol.57 , pp. 725-749
    • Grossman, A.R.1    Schaefer, M.R.2    Chiang, G.G.3    Collier, J.L.4
  • 4
    • 0003123963 scopus 로고
    • Phycobilisome and phycobiliprotein structures
    • D.A. Bryant. Dordrecht: Kluwer
    • Sidler W.A. Phycobilisome and phycobiliprotein structures. Bryant D.A. The Molecular Biology of Cyanobacteria. 1994;139-216 Kluwer, Dordrecht
    • (1994) The Molecular Biology of Cyanobacteria , pp. 139-216
    • Sidler, W.A.1
  • 5
    • 0002323237 scopus 로고    scopus 로고
    • Biosynthesis of Phycobiliproteins in Cyanobacteria
    • G.A. Peschek, W. Löffelhardt, & G. Schmetterer. New York: Kluwer/Plenum
    • Schluchter W.M., Glazer A.N. Biosynthesis of Phycobiliproteins in Cyanobacteria. Peschek G.A., Löffelhardt W., Schmetterer G. The Phototrophic Prokaryotes. 1999;83-95 Kluwer/Plenum, New York
    • (1999) The Phototrophic Prokaryotes , pp. 83-95
    • Schluchter, W.M.1    Glazer, A.N.2
  • 6
    • 0002422835 scopus 로고
    • Biosynthesis of cyanobacterial tetrapyrrole pigments: Hemes, chlorophylls and phycobilins
    • D.A. Bryant. Dordrecht: Kluwer
    • Beale S.I. Biosynthesis of cyanobacterial tetrapyrrole pigments: hemes, chlorophylls and phycobilins. Bryant D.A. The Molecular Biology of Cyanobacteria. 1994;519-558 Kluwer, Dordrecht
    • (1994) The Molecular Biology of Cyanobacteria , pp. 519-558
    • Beale, S.I.1
  • 7
    • 0033905732 scopus 로고    scopus 로고
    • Phytobilin biosynthesis: The Synechocystis sp. PCC 6803 heme oxygenase-encoding ho1 gene complements a phytochrome-deficient Arabidopsis thaliana hy1 mutant
    • Willows R.D., Mayer S.M., Foulk M.S., DeLong A., Hanson K., Chory J., Beale S.I. Phytobilin biosynthesis: the Synechocystis sp. PCC 6803 heme oxygenase-encoding ho1 gene complements a phytochrome-deficient Arabidopsis thaliana hy1 mutant. Plant Mol. Biol. 43:2000;113-120
    • (2000) Plant Mol. Biol. , vol.43 , pp. 113-120
    • Willows, R.D.1    Mayer, S.M.2    Foulk, M.S.3    Delong, A.4    Hanson, K.5    Chory, J.6    Beale, S.I.7
  • 8
    • 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., 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
  • 9
    • 0034619430 scopus 로고    scopus 로고
    • Defining the bilin lyase domain: Lessons from the extended phytochrome superfamily
    • Wu S.-H., Lagarias J.C. Defining the bilin lyase domain: lessons from the extended phytochrome superfamily. Biochemistry. 39:2000;13487-13495
    • (2000) Biochemistry , vol.39 , pp. 13487-13495
    • Wu, S.-H.1    Lagarias, J.C.2
  • 11
    • 0010459449 scopus 로고
    • Addition of 2-mercaptopropionylglycine to biliverdin - A kinetic and thermodynamic study
    • Beltrame P.L., Monti D., Sala R., Manitto P. Addition of 2-mercaptopropionylglycine to biliverdin - a kinetic and thermodynamic study. Gaz. Chim. Ital. 115:1985;223-226
    • (1985) Gaz. Chim. Ital. , vol.115 , pp. 223-226
    • Beltrame, P.L.1    Monti, D.2    Sala, R.3    Manitto, P.4
  • 12
    • 0024279623 scopus 로고
    • In vitro attachment of Bilins to Apophycocyanin: 2. Determination of the structures of tryptic Bilin peptides derived from the Phycocyanobilin adduct
    • Arciero D.M., Dallas J.L., Glazer A.N. In vitro attachment of Bilins to Apophycocyanin: 2. Determination of the structures of tryptic Bilin peptides derived from the Phycocyanobilin adduct. J. Biol. Chem. 263:1988;18350-18357
    • (1988) J. Biol. Chem. , vol.263 , pp. 18350-18357
    • Arciero, D.M.1    Dallas, J.L.2    Glazer, A.N.3
  • 13
    • 0034191806 scopus 로고    scopus 로고
    • The photoreactions of recombinant phytochrome from the cyanobacterium Synechocystis: A low-temperature UV-Vis and FT-IR spectroscopic study
    • Förstendorf H., Lamparter T., Hughes J., Gärtner W., Siebert F. The photoreactions of recombinant phytochrome from the cyanobacterium Synechocystis: a low-temperature UV-Vis and FT-IR spectroscopic study. Photochem. Photobiol. 71:2000;655-661
    • (2000) Photochem. Photobiol. , vol.71 , pp. 655-661
    • Förstendorf, H.1    Lamparter, T.2    Hughes, J.3    Gärtner, W.4    Siebert, F.5
  • 15
    • 0028245818 scopus 로고
    • Oligomeric structure, enzyme kinetics, and substrate specificity of the phycocyanin alpha subunit phycocyanobilin lyase
    • Fairchild C.D., Glazer A.N. Oligomeric structure, enzyme kinetics, and substrate specificity of the phycocyanin alpha subunit phycocyanobilin lyase. J. Biol. Chem. 269:1994;8686-8694
    • (1994) J. Biol. Chem. , vol.269 , pp. 8686-8694
    • Fairchild, C.D.1    Glazer, A.N.2
  • 16
    • 0028046145 scopus 로고
    • Nonenzymatic bilin addition to the gamma subunit of an apophycoerythrin
    • Fairchild C.D., Glazer A.N. Nonenzymatic bilin addition to the gamma subunit of an apophycoerythrin. J. Biol. Chem. 269:1994;28988-28996
    • (1994) J. Biol. Chem. , vol.269 , pp. 28988-28996
    • Fairchild, C.D.1    Glazer, A.N.2
  • 18
    • 1642276701 scopus 로고    scopus 로고
    • The biliverdin chromophore binds covalently to a conserved cysteine residue in the N-terminus of Agrobacterium phytochrome agp1
    • Lamparter T., Carrascal M., Michael N., Martinez E., Rottwinkel G., Abian J. The biliverdin chromophore binds covalently to a conserved cysteine residue in the N-terminus of Agrobacterium phytochrome agp1. Biochemistry. 43:2004;3659-3669
    • (2004) Biochemistry , vol.43 , pp. 3659-3669
    • Lamparter, T.1    Carrascal, M.2    Michael, N.3    Martinez, E.4    Rottwinkel, G.5    Abian, J.6
  • 19
    • 0034598956 scopus 로고    scopus 로고
    • Novel activity of a phycobiliprotein lyase: Both the attachment of phycocyanobilin and the isomerization to phycoviolobilin are catalyzed by PecE and PecF
    • Zhao K.-H., Deng M.-G., Zheng M., Zhou M., Parbel A., Storf M., Meyer M., Strohmann B., Scheer H. Novel activity of a phycobiliprotein lyase: both the attachment of phycocyanobilin and the isomerization to phycoviolobilin are catalyzed by PecE and PecF. FEBS Lett. 469:2000;9-13
    • (2000) FEBS Lett. , vol.469 , pp. 9-13
    • Zhao, K.-H.1    Deng, M.-G.2    Zheng, M.3    Zhou, M.4    Parbel, A.5    Storf, M.6    Meyer, M.7    Strohmann, B.8    Scheer, H.9
  • 21
    • 0029015730 scopus 로고
    • Candidate genes for the phycoerythrocyanin alpha subunit lyase. Biochemical analysis of pecE and pecF interposon mutants
    • Jung L.J., Chan C.F., Glazer A.N. Candidate genes for the phycoerythrocyanin alpha subunit lyase. Biochemical analysis of pecE and pecF interposon mutants. J. Biol. Chem. 270:1995;12877-12884
    • (1995) J. Biol. Chem. , vol.270 , pp. 12877-12884
    • Jung, L.J.1    Chan, C.F.2    Glazer, A.N.3
  • 23
    • 0000393126 scopus 로고
    • Solution conformations, photophysics, and photochemistry of bili-pigments-bilirubin and biliverdin dimethylesters and related linear tetrapyrroles
    • Braslavsky S.E., Holzwarth A.R., Schaffner K. Solution conformations, photophysics, and photochemistry of bili-pigments-bilirubin and biliverdin dimethylesters and related linear tetrapyrroles. Angew. Chem., Int. Ed. Engl. 22:1983;656-674
    • (1983) Angew. Chem., Int. Ed. Engl. , vol.22 , pp. 656-674
    • Braslavsky, S.E.1    Holzwarth, A.R.2    Schaffner, K.3
  • 24
    • 0002427093 scopus 로고
    • Phycobiliproteins: Molecular aspects of photosynthetic antenna systems
    • F.K. Fong. Berlin: Springer Verlag
    • Scheer H. Phycobiliproteins: molecular aspects of photosynthetic antenna systems. Fong F.K. Light Reaction Path of Photosynthesis. 1982;7-45 Springer Verlag, Berlin
    • (1982) Light Reaction Path of Photosynthesis , pp. 7-45
    • Scheer, H.1
  • 26
    • 0029037179 scopus 로고
    • Isolation, crystallization, crystal structure analysis and refinement of Allophycocyanin from the cyanobacterium Spirulina platensis at 2.3 a resolution
    • Brejc K., Ficner R., Huber R., Steinbacher S. Isolation, crystallization, crystal structure analysis and refinement of Allophycocyanin from the cyanobacterium Spirulina platensis at 2.3 A resolution. J. Mol. Biol. 249:1995;424-440
    • (1995) J. Mol. Biol. , vol.249 , pp. 424-440
    • Brejc, K.1    Ficner, R.2    Huber, R.3    Steinbacher, S.4
  • 27
    • 0027373718 scopus 로고
    • Refined crystal structure of phycoerythrin from Porphyridium cruentum at 2.3 Angström resolution and localization of the gamma subunit
    • Ficner R., Huber R. Refined crystal structure of phycoerythrin from Porphyridium cruentum at 2.3 Angström resolution and localization of the gamma subunit. Eur. J. Biochem. 218:1993;103-106
    • (1993) Eur. J. Biochem. , vol.218 , pp. 103-106
    • Ficner, R.1    Huber, R.2
  • 28
    • 0025967561 scopus 로고
    • Isolation, crystallization, crystal structure analysis and refinement of constitutive c-Phycocyanin from the chromatically adapting cyanobacterium Fremyella diplosiphon at 1.66 a resolution
    • Duerring M., Schmidt G.B., Huber R. Isolation, crystallization, crystal structure analysis and refinement of constitutive c-Phycocyanin from the chromatically adapting cyanobacterium Fremyella diplosiphon at 1.66 A resolution. J. Mol. Biol. 217:1991;577-592
    • (1991) J. Mol. Biol. , vol.217 , pp. 577-592
    • Duerring, M.1    Schmidt, G.B.2    Huber, R.3
  • 29
    • 0025228693 scopus 로고
    • Refined three-dimensional structure of Phycoerythrocyanin from the cyanobacterium Mastigocladus laminosus at 2.7 a
    • Duerring M., Huber R., Bode W., Ruembeli R., Zuber H. Refined three-dimensional structure of Phycoerythrocyanin from the cyanobacterium Mastigocladus laminosus at 2.7 A. J. Mol. Biol. 211:1990;633-644
    • (1990) J. Mol. Biol. , vol.211 , pp. 633-644
    • Duerring, M.1    Huber, R.2    Bode, W.3    Ruembeli, R.4    Zuber, H.5
  • 30
    • 0023053285 scopus 로고
    • Crystal structure analysis and refinement at 2.5A of hexameric C-phycocyanin from the cyanobacterium Agmenellum quadruplicatum
    • Schirmer T., Huber R., Schneider M., Bode W., Miller M., Hackert M.L. Crystal structure analysis and refinement at 2.5A of hexameric C-phycocyanin from the cyanobacterium Agmenellum quadruplicatum. J. Mol. Biol. 188:1986;651-676
    • (1986) J. Mol. Biol. , vol.188 , pp. 651-676
    • Schirmer, T.1    Huber, R.2    Schneider, M.3    Bode, W.4    Miller, M.5    Hackert, M.L.6
  • 31
    • 0034901819 scopus 로고    scopus 로고
    • Crystal structure of R-phycocyanin and possible energy transfer pathways in the phycobilisome
    • Jiang T., Zhang J.P., Chang W.R., Liang D.C. Crystal structure of R-phycocyanin and possible energy transfer pathways in the phycobilisome. Biophys. J. 81:2001;1171-1179
    • (2001) Biophys. J. , vol.81 , pp. 1171-1179
    • Jiang, T.1    Zhang, J.P.2    Chang, W.R.3    Liang, D.C.4
  • 32
    • 0034989667 scopus 로고    scopus 로고
    • Structure of C-Phycocyanin from Spirulina Platensis at 2.2 Angstrom Resolution: A Novel Monoclinic Crystal Form for Phycobiliproteins in Phycobilisomes
    • Wang X.Q., Li L.N., Chang W.R., Zhang J.P., Gui L.L., Guo B.J., Liang D.C. Structure of C-Phycocyanin From Spirulina Platensis at 2.2 Angstrom Resolution: a Novel Monoclinic Crystal Form for Phycobiliproteins in Phycobilisomes. Acta Crystallogr., D Biol. Crystallogr. 57:2001;784-792
    • (2001) Acta Crystallogr., D Biol. Crystallogr. , vol.57 , pp. 784-792
    • Wang, X.Q.1    Li, L.N.2    Chang, W.R.3    Zhang, J.P.4    Gui, L.L.5    Guo, B.J.6    Liang, D.C.7
  • 33
    • 0030580059 scopus 로고    scopus 로고
    • Crystal structure of R-phycoerythrin from Polysiphonia urceolata at 2.8 angstrom resolution
    • Chang W.R., Jiang T., Wan Z.L., Zhang J.P., Yang Z.X., Liang D.C. Crystal structure of R-phycoerythrin from Polysiphonia urceolata at 2.8 angstrom resolution. J. Mol. Biol. 262:1996;721-731
    • (1996) J. Mol. Biol. , vol.262 , pp. 721-731
    • Chang, W.R.1    Jiang, T.2    Wan, Z.L.3    Zhang, J.P.4    Yang, Z.X.5    Liang, D.C.6
  • 34
    • 84989665755 scopus 로고
    • Phytochrome models: Part 10. Concentration, sonication and temperature affecting the population of the ground-state conformers of biliverdin dimethyl ester in solution
    • Al-Ekabi H., Tegmo-Larsson I.M., Braslavsky S.E., Holzwarth A.R., Schaffner K. Phytochrome models: Part 10. Concentration, sonication and temperature affecting the population of the ground-state conformers of biliverdin dimethyl ester in solution. Photochem. Photobiol. 44:1986;433-440
    • (1986) Photochem. Photobiol. , vol.44 , pp. 433-440
    • Al-Ekabi, H.1    Tegmo-Larsson, I.M.2    Braslavsky, S.E.3    Holzwarth, A.R.4    Schaffner, K.5
  • 35
    • 0010528742 scopus 로고
    • Phytochrome models. 6. Conformation control by membrane of Biliverdin dimethylester incorporated into lipid vesicles
    • Tegmo-Larsson I.-M., Braslavsky S.E., Culshaw S., Ellul R.E., Nicolau C., Schaffner K. Phytochrome models. 6. Conformation control by membrane of Biliverdin dimethylester incorporated into lipid vesicles. J. Am. Chem. Soc. 103:1981;7152-7158
    • (1981) J. Am. Chem. Soc. , vol.103 , pp. 7152-7158
    • Tegmo-Larsson, I.-M.1    Braslavsky, S.E.2    Culshaw, S.3    Ellul, R.E.4    Nicolau, C.5    Schaffner, K.6
  • 36
    • 0036379292 scopus 로고    scopus 로고
    • Characterization of phycoviolobilin phycoerythrocyanin-α 84-cystein-lyase-(isomerizing) from Mastigocladus laminosus
    • Zhao K.-H., Wu D., Wang L., Zhou M., Storf M., Bubenzer C., Strohmann B., Scheer H. Characterization of phycoviolobilin phycoerythrocyanin-α 84-cystein-lyase-(isomerizing) from Mastigocladus laminosus. Eur. J. Biochem. 269:2002;4542-4550
    • (2002) Eur. J. Biochem. , vol.269 , pp. 4542-4550
    • Zhao, K.-H.1    Wu, D.2    Wang, L.3    Zhou, M.4    Storf, M.5    Bubenzer, C.6    Strohmann, B.7    Scheer, H.8
  • 38
    • 0343316357 scopus 로고
    • Isolation and characterization of Phycoerythrocyanin and chromatic adaptation of the thermophilic cyanobacterium Mastigocladus laminosus
    • Füglistaller P., Widmer H., Sidler W., Frank G., Zuber H. Isolation and characterization of Phycoerythrocyanin and chromatic adaptation of the thermophilic cyanobacterium Mastigocladus laminosus. Arch. Microbiol. 129:1981;268-274
    • (1981) Arch. Microbiol. , vol.129 , pp. 268-274
    • Füglistaller, P.1    Widmer, H.2    Sidler, W.3    Frank, G.4    Zuber, H.5
  • 39
  • 40
    • 0028967604 scopus 로고
    • Type I and type II reversible photochemistry of phycoerythrocyanin α-subunit from Mastigcoladus laminosus both involve Z, e isomerization of phycoviolobilin chromophore and are controlled by sulfhydryls in apoprotein
    • Zhao K.H., Scheer H. Type I and type II reversible photochemistry of phycoerythrocyanin α-subunit from Mastigcoladus laminosus both involve Z, E isomerization of phycoviolobilin chromophore and are controlled by sulfhydryls in apoprotein. Biochim. Biophys. Acta. 1228:1995;244-253
    • (1995) Biochim. Biophys. Acta , vol.1228 , pp. 244-253
    • Zhao, K.H.1    Scheer, H.2
  • 41
    • 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
  • 42
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriopharge T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriopharge T4. Nature. 227:1970;680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 43
    • 0022486877 scopus 로고
    • Visualization of bilin-linked peptides and proteins in polyacrylamide gels
    • Berkelman T., Lagarias J.C. Visualization of bilin-linked peptides and proteins in polyacrylamide gels. Anal. Biochem. 156:1986;194-201
    • (1986) Anal. Biochem. , vol.156 , pp. 194-201
    • Berkelman, T.1    Lagarias, J.C.2
  • 44
    • 0030695502 scopus 로고    scopus 로고
    • Chromophore assignment in phycoerythrocyanin from Mastigocladus laminosus
    • Parbel A., Zhao K.H., Breton J., Scheer H. Chromophore assignment in phycoerythrocyanin from Mastigocladus laminosus. Photosynth. Res. 54:1997;25-34
    • (1997) Photosynth. Res. , vol.54 , pp. 25-34
    • Parbel, A.1    Zhao, K.H.2    Breton, J.3    Scheer, H.4
  • 46
    • 45449125524 scopus 로고
    • Excitation transfer in C-phycocyanin. Förster transfer rate and exciton calculations based on new crystal structure data for C-phycocyanins from Agmenellum quadruplicatum and Mastigocladus laminosus
    • Sauer K., Scheer H. Excitation transfer in C-phycocyanin. Förster transfer rate and exciton calculations based on new crystal structure data for C-phycocyanins from Agmenellum quadruplicatum and Mastigocladus laminosus. Biochim. Biophys. Acta. 936:1988;157-170
    • (1988) Biochim. Biophys. Acta , vol.936 , pp. 157-170
    • Sauer, K.1    Scheer, H.2
  • 47
    • 0029307218 scopus 로고
    • Comparison of calculated and experimentally resolved rate constants for excitation energy transfer in C-Phycocyanin. 1. Monomers
    • Debreczeny M.P., Sauer K., Zhou J., Bryant D.A. Comparison of calculated and experimentally resolved rate constants for excitation energy transfer in C-Phycocyanin. 1. Monomers. J. Phys. Chem. 99:1995;8412-8419
    • (1995) J. Phys. Chem. , vol.99 , pp. 8412-8419
    • Debreczeny, M.P.1    Sauer, K.2    Zhou, J.3    Bryant, D.A.4
  • 48
    • 0004244494 scopus 로고
    • Energy transfer calculations for two C-phycocyanins based on refined X-ray crystal structure coordinates of chromophores
    • H. Scheer, & S. Schneider.
    • Sauer K., Scheer H. Energy transfer calculations for two C-phycocyanins based on refined X-ray crystal structure coordinates of chromophores. Scheer H., Schneider S. Photosynthetic Light-Harvesting Systems, Organization and Function. 1988;507-513
    • (1988) Photosynthetic Light-Harvesting Systems, Organization and Function , pp. 507-513
    • Sauer, K.1    Scheer, H.2
  • 49
    • 0036411681 scopus 로고    scopus 로고
    • Purification, crystallization, NMR spectroscopy and biochemical analyses of alpha-phycoerythrocyanin peptides
    • Wiegand G., Parbel A., Seifert M.H., Holak T.A., Reuter W. Purification, crystallization, NMR spectroscopy and biochemical analyses of alpha-phycoerythrocyanin peptides. Eur. J. Biochem. 269:2002;5046-5055
    • (2002) Eur. J. Biochem. , vol.269 , pp. 5046-5055
    • Wiegand, G.1    Parbel, A.2    Seifert, M.H.3    Holak, T.A.4    Reuter, W.5
  • 54
    • 0028987206 scopus 로고
    • Deconvolution of C-Phycocyanin β-84 and β-155 chromophore absorption and fluorescence spectra of cyanobacterium Mastigocladus laminosus
    • Demidov A.A., Mimuro M. Deconvolution of C-Phycocyanin β-84 and β-155 chromophore absorption and fluorescence spectra of cyanobacterium Mastigocladus laminosus. Biophys. J. 68:1995;1500-1506
    • (1995) Biophys. J. , vol.68 , pp. 1500-1506
    • Demidov, A.A.1    Mimuro, M.2
  • 55
    • 0002531047 scopus 로고
    • Studies on chromophore coupling in isolated phycobiliproteins: 4. Femtosecond transient absorption study of ultrafast excited state dynamics in trimeric phycoerythrocyanin complexes
    • Hucke M., Schweitzer G., Holzwarth A.R., Sidler W., Zuber H. Studies on chromophore coupling in isolated phycobiliproteins: 4. Femtosecond transient absorption study of ultrafast excited state dynamics in trimeric phycoerythrocyanin complexes. Photochem. Photobiol. 57:1993;76-80
    • (1993) Photochem. Photobiol. , vol.57 , pp. 76-80
    • Hucke, M.1    Schweitzer, G.2    Holzwarth, A.R.3    Sidler, W.4    Zuber, H.5
  • 56
    • 0023645201 scopus 로고
    • Refined three-dimensional structures of two cyanobacterial C-phycocyanins at 2.1. and 2.5 a resolution - A common principle of phycobilin-protein interaction
    • Schirmer T., Bode W., Huber R. Refined three-dimensional structures of two cyanobacterial C-phycocyanins at 2.1. and 2.5 A resolution - a common principle of phycobilin-protein interaction. J. Mol. Biol. 196:1987;677-695
    • (1987) J. Mol. Biol. , vol.196 , pp. 677-695
    • Schirmer, T.1    Bode, W.2    Huber, R.3
  • 57
    • 37049101251 scopus 로고
    • Chiral induction in Biliverdin covalently bound to Amino-acids
    • Haidl E., Krois D., Lehner H. Chiral induction in Biliverdin covalently bound to Amino-acids. J. Chem. Soc., Perkin Trans., II. 3:1985;421-425
    • (1985) J. Chem. Soc., Perkin Trans., II , vol.3 , pp. 421-425
    • Haidl, E.1    Krois, D.2    Lehner, H.3
  • 58
    • 3242692329 scopus 로고
    • Aspects of the reactivity of IX-beta-Biliverdin and IX-gamma-Biliverdin dimethyl esters - Structural studies of new Biliverdins
    • Petrier C., Dupuy C., Jardon P., Gautron R. Aspects of the reactivity of IX-beta-Biliverdin and IX-gamma-Biliverdin dimethyl esters - structural studies of new Biliverdins. Nouv. J. Chim. 6:1982;495-503
    • (1982) Nouv. J. Chim. , vol.6 , pp. 495-503
    • Petrier, C.1    Dupuy, C.2    Jardon, P.3    Gautron, R.4
  • 59
    • 0005777976 scopus 로고
    • Force field calculations on linear Polypyrrole systems
    • Falk H., Müller N. Force field calculations on linear Polypyrrole systems. Tetrahedron Lett. 39:1983;1875-1885
    • (1983) Tetrahedron Lett. , vol.39 , pp. 1875-1885
    • Falk, H.1    Müller, N.2
  • 60
    • 84981378978 scopus 로고
    • Die interkonversionsbarriere der bilatrien-helix
    • Lehner H., Riemer W., Schaffner K. Die interkonversionsbarriere der bilatrien-helix. Liebigs Ann. Chem. 1979:1979;1798-1801
    • (1979) Liebigs Ann. Chem. , vol.1979 , pp. 1798-1801
    • Lehner, H.1    Riemer, W.2    Schaffner, K.3
  • 61
    • 0003156298 scopus 로고
    • Rubins and rubinoid addition products from phycocyanin
    • Kufer W., Scheer H. Rubins and rubinoid addition products from phycocyanin. Z. Naturforsch. 37c:1982;179-192
    • (1982) Z. Naturforsch. , vol.37 , pp. 179-192
    • Kufer, W.1    Scheer, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.