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Volumn 44, Issue 22, 2005, Pages 8126-8137

Amino acid residues associated with enzymatic activities of the isomerizing phycoviolobilin-lyase PecE/F

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; ENZYMES; ESCHERICHIA COLI; FLUORESCENCE; ISOMERIZATION; MUTAGENESIS; STATISTICAL METHODS;

EID: 20144383967     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0500168     Document Type: Article
Times cited : (29)

References (58)
  • 1
    • 3442880261 scopus 로고    scopus 로고
    • Antenna systems of red algae: Phycobilisomes with photosystem II and chlorophyll complexes with photosystem I
    • (Green B., and Parson, W., Eds.), Kluwer/Dordrecht
    • Gantt, B., Grabowski, B., and Cunningham, F. X. (2003) Antenna systems of red algae: Phycobilisomes with photosystem II and chlorophyll complexes with photosystem I. in Light-harvesting antennas in photosynthesis (Green, B., and Parson, W., Eds.) pp 307-322, Kluwer/Dordrecht.
    • (2003) Light-harvesting Antennas in Photosynthesis , pp. 307-322
    • Gantt, B.1    Grabowski, B.2    Cunningham, F.X.3
  • 2
    • 0000370919 scopus 로고
    • Adaptive variations in phycobilisome structure
    • Glazer, A. N. (1994) Adaptive variations in phycobilisome structure, Adv. Mol. Cell Biol. 10, 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., and Collier, J. L. (1993) The phycobilisome, a light-harvesting complex responsive to environmental conditions, Microbiol Rev. 57, 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
    • (Bryant D. A., Ed.), Kluwer, Dordrecht
    • Sidler, W. A. (1994) Phycobilisome and phycobiliprotein structures, in The molecular biology of cyanobacteria (Bryant. D. A., Ed.) pp 139-216, Kluwer, Dordrecht.
    • (1994) The Molecular Biology of Cyanobacteria , pp. 139-216
    • Sidler, W.A.1
  • 5
    • 0002427093 scopus 로고
    • Phycobiliproteins: Molecular aspects of photosynthetic antenna systems
    • (Fong F. K., Ed.), Springer, Berlin
    • Scheer, H. (1982) Phycobiliproteins: Molecular aspects of photosynthetic antenna systems, in Light reaction path of photosynthesis (Fong, F. K., Ed.) pp 7-45, Springer, Berlin.
    • (1982) Light Reaction Path of Photosynthesis , pp. 7-45
    • Scheer, H.1
  • 6
    • 0021814065 scopus 로고
    • Bilin attachment sites in the alpha-subunits, beta-subunits and gamma-subunits of R-phycoerythrin-Structural studies on singly and doubly linked phycourobilins
    • Nagy, J. O., Bishop, J. E., Klotz, A. V., Glazer, A. N., and Rapoport, H. (1985) Bilin attachment sites in the alpha-subunits, beta-subunits and gamma-subunits of R-phycoerythrin-Structural studies on singly and doubly linked phycourobilins, J. Biol. Chem. 260, 4864-4868.
    • (1985) J. Biol. Chem. , vol.260 , pp. 4864-4868
    • Nagy, J.O.1    Bishop, J.E.2    Klotz, A.V.3    Glazer, A.N.4    Rapoport, H.5
  • 7
    • 0024288695 scopus 로고
    • Exclusive a-ring linkage for stingly attached phycocyanobilins and phycoerythrobilins in phycobiliproteins-Absence of singly d-ring linked bilins
    • Lagarias, J. C., Klotz, A. V., Dallas, J. L., Glazer, A. N., Bishop, J. E., Oconnell, J. F., and Rapoport, H. (1988) Exclusive a-ring linkage for stingly attached phycocyanobilins and phycoerythrobilins in phycobiliproteins- Absence of singly d-ring linked bilins, J. Biol. Chem. 263, 2977-2985.
    • (1988) J. Biol. Chem. , vol.263 , pp. 2977-2985
    • Lagarias, J.C.1    Klotz, A.V.2    Dallas, J.L.3    Glazer, A.N.4    Bishop, J.E.5    Oconnell, J.F.6    Rapoport, H.7
  • 8
    • 0002323237 scopus 로고    scopus 로고
    • Biosynthesis of phycobiliproteins in cyanobacteria
    • (Peschek G. A., Loffelhardt, W., and Schmetterer, G., Eds.), Kluwer/Plenum Press, New York
    • Schluchter, W. M., and Glazer, A. N. (1999) Biosynthesis of phycobiliproteins in cyanobacteria, in The phototrophic prokaryotes (Peschek, G. A., Loffelhardt, W., and Schmetterer, G., Eds.) pp 83-95, Kluwer/Plenum Press, New York.
    • (1999) The Phototrophic Prokaryotes , pp. 83-95
    • Schluchter, W.M.1    Glazer, A.N.2
  • 9
    • 0002422835 scopus 로고
    • Biosynthesis of cyanobacterial tetrapyrrole pigments: Hemes, chlorophylls and phycobilins
    • (Bryant, D. A., Ed.), Kluwer, Dordrecht
    • Beale, S. I. (1994) Biosynthesis of cyanobacterial tetrapyrrole pigments: Hemes, chlorophylls and phycobilins, in The molecular biology of cyanobacteria (Bryant, D. A., Ed.) pp 519-558, Kluwer, Dordrecht.
    • (1994) The Molecular Biology of Cyanobacteria , pp. 519-558
    • Beale, S.I.1
  • 10
    • 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., and Beale, S. I. (2000) Phytobilin biosynthesis: The Synechocystis sp. PCC 6803 heme oxygenase-encoding ho1 gene complements a phytochrome- deficient Arabidopsis thaliana hy1 mutant, Plant Mol. Biol. 43, 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
  • 11
    • 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. (2001) Functional genomic analysis of the hy2 family of ferredoxin-dependent bilin reductases from oxygenic photosynthetic organisms, Plant Cell 13, 965-978.
    • (2001) Plant Cell , vol.13 , pp. 965-978
    • Frankenberg, N.1    Mukougawa, K.2    Kohchi, T.3    Lagarias, J.C.4
  • 12
    • 0034619430 scopus 로고    scopus 로고
    • Defining the bilin lyase domain: Lessons from the extended phytochrome superfamily
    • Wu, S.-H., and Lagarias, J. C. (2000) Defining the bilin lyase domain: Lessons from the extended phytochrome superfamily, Biochemistry 39, 13487-13495.
    • (2000) Biochemistry , vol.39 , pp. 13487-13495
    • Wu, S.-H.1    Lagarias, J.C.2
  • 14
    • 0010459449 scopus 로고
    • Addition of 2-mercaptopropionylglycine to biliverdin - A kinetic and thermodynamic study, Gazz
    • Beltrame, P. L., Monti, D., Sala, R., and Manitto, P. (1985) Addition of 2-mercaptopropionylglycine to biliverdin-A kinetic and thermodynamic study, Gazz. Chim. Ital. 115, 223-226.
    • (1985) Chim. Ital. , vol.115 , pp. 223-226
    • Beltrame, P.L.1    Monti, D.2    Sala, R.3    Manitto, P.4
  • 15
    • 0028046145 scopus 로고
    • Nonenzymatic bilin addition to the gamma subunit of an apophycoerythrin
    • Fairchild, C. D., and Glazer, A. N. (1994) Nonenzymatic bilin addition to the gamma subunit of an apophycoerythrin, J. Biol. Chem. 269, 28988-28996.
    • (1994) J. Biol. Chem. , vol.269 , pp. 28988-28996
    • Fairchild, C.D.1    Glazer, A.N.2
  • 16
    • 4444326150 scopus 로고    scopus 로고
    • Photochromic biliproteins from the cyanobacterium Anabaena sp. PCC 7120: Lyase activities, chromophore exchange and photochromism in phytochrome and phycoerythrocyanin
    • Zhao, K.-H., Ran, Y., Li, M., Sun, Y.-N., Zhou, M., Storf, M., Kupka, M., Böhm, S., Bubenzer, C., and Scheer, H. (2004) Photochromic biliproteins from the cyanobacterium Anabaena sp. PCC 7120: lyase activities, chromophore exchange and photochromism in phytochrome and phycoerythrocyanin, Biochemistry 43, 11576-11588.
    • (2004) Biochemistry , vol.43 , pp. 11576-11588
    • Zhao, K.-H.1    Ran, Y.2    Li, M.3    Sun, Y.-N.4    Zhou, M.5    Storf, M.6    Kupka, M.7    Böhm, S.8    Bubenzer, C.9    Scheer, H.10
  • 17
    • 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., and Abian, J. (2004) The biliverdin chromophore binds covalently to a conserved cysteine residue in the N-terminus of Agrobacterium phytochrome Agp1, Biochemistry 43, 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
  • 18
    • 0942268739 scopus 로고    scopus 로고
    • RcaE is a complementary chromatic adaptation photoreceptor required for green and red light responsiveness
    • Terauchi, K., Montgomery, B. L., Grossman, A. R., Lagarias, J. C., and Kehoe, D. M. (2004) RcaE is a complementary chromatic adaptation photoreceptor required for green and red light responsiveness, Mol. Microbiol. 51, 567-577.
    • (2004) Mol. Microbiol. , vol.51 , pp. 567-577
    • Terauchi, K.1    Montgomery, B.L.2    Grossman, A.R.3    Lagarias, J.C.4    Kehoe, D.M.5
  • 21
    • 14244253561 scopus 로고    scopus 로고
    • Characterization of two novel phycoerythrin-associated linker proteins in the marine cyanobacterium Synechococcus sp. WH8102
    • Six, C., Thomas, J.-C., Thion, L., Lemoine, Y., Zal, F., and Partensky, F. (2005) Characterization of two novel phycoerythrin-associated linker proteins in the marine cyanobacterium Synechococcus sp. WH8102, J. Bacteriol., 187, 1685-1694.
    • (2005) J. Bacteriol. , vol.187 , pp. 1685-1694
    • Six, C.1    Thomas, J.-C.2    Thion, L.3    Lemoine, Y.4    Zal, F.5    Partensky, F.6
  • 23
    • 84987045394 scopus 로고
    • Photochemistry of phycobiliproteins; Reciprocity of reversible photochemistry and aggregation in phycoerythrocyanin from Mastigocladus laminosus
    • Siebzehnrübl, S., Fischer, R., Kufer, W., and Scheer, H, (1989) Photochemistry of phycobiliproteins; Reciprocity of reversible photochemistry and aggregation in phycoerythrocyanin from Mastigocladus laminosus, Photochem. Photobiol. 49, 753-761.
    • (1989) Photochem. Photobiol. , vol.49 , pp. 753-761
    • Siebzehnrübl, S.1    Fischer, R.2    Kufer, W.3    Scheer, H.4
  • 24
    • 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., and Scheer, H. (1995) 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, 244-253.
    • (1995) Biochim. Biophys. Acta , vol.1228 , pp. 244-253
    • Zhao, K.H.1    Scheer, H.2
  • 25
    • 0028936568 scopus 로고
    • Type I reversible of phycoerythrocyanin involves Z/E-isomerization of α-84 phycoviolobilin chromophore
    • Zhao, K. H., Haessner, R., Cmiel, E., and Scheer, H. (1995) Type I reversible of phycoerythrocyanin involves Z/E-isomerization of α-84 phycoviolobilin chromophore, Biochim, Biophys. Acta 1228, 235-243.
    • (1995) Biochim, Biophys. Acta , vol.1228 , pp. 235-243
    • Zhao, K.H.1    Haessner, R.2    Cmiel, E.3    Scheer, H.4
  • 26
    • 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., and Scheer, H. (2000) 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, 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
  • 28
    • 4243586965 scopus 로고
    • Structure and molecular evolution of the gene cluster encoding proteins of the rod substructure of the phycobilisome from the cyanobacterium Mastigocladus laminosus
    • Kufer, W., Högner, A., Eberlein, M., Mayer, K., Buchner, A., and Gottschalk, L. (1991) Structure and molecular evolution of the gene cluster encoding proteins of the rod substructure of the phycobilisome from the cyanobacterium Mastigocladus laminosus, GenBank M75599.
    • (1991) GenBank
    • Kufer, W.1    Högner, A.2    Eberlein, M.3    Mayer, K.4    Buchner, A.5    Gottschalk, L.6
  • 29
    • 0026658880 scopus 로고
    • Genes encoding the phycobilisome rod substructure are clustered on the Anabaena chromosome: Characterization of the Phycoerythrocyanin operon
    • Swanson, R. V., Lorimier de, R., and Glazer, A. N. (1992) Genes encoding the phycobilisome rod substructure are clustered on the Anabaena chromosome: Characterization of the Phycoerythrocyanin operon, J. Bacteriol. 174, 2640-2647.
    • (1992) J. Bacteriol. , vol.174 , pp. 2640-2647
    • Swanson, R.V.1    Lorimier De, R.2    Glazer, A.N.3
  • 31
    • 0036379292 scopus 로고    scopus 로고
    • Characterization of phycoviolobilin phycoerythrocyanin-α84-cystein- lyase-(isomerizing) from Mastigocladus laminosus
    • Zhao, K.-H., Wu, D., Wang, L., Zhou, M., Storf, M., Bubenzer, C., Strohmann, B., and Scheer, H. (2002) Characterization of phycoviolobilin phycoerythrocyanin-α84-cystein-lyase-(isomerizing) from Mastigocladus laminosus, Eur. J. Biochem. 269, 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
  • 33
    • 0025325983 scopus 로고
    • The "megaprimer" method of site-directed mutagenesis
    • Sarkar, G., and Sommer, S. S. (1990) The "megaprimer" method of site-directed mutagenesis, BioTechniques 8, 404-407.
    • (1990) BioTechniques , vol.8 , pp. 404-407
    • Sarkar, G.1    Sommer, S.S.2
  • 34
    • 0029144643 scopus 로고
    • A one-step polymerase chain reaction site-directed mutagenesis method for large gene-cassettes with high efficiency, yield, and fidelity
    • Ling, M., and Robinson, B. H. (1995) A one-step polymerase chain reaction site-directed mutagenesis method for large gene-cassettes with high efficiency, yield, and fidelity, Anal. Biochem. 230, 167-172.
    • (1995) Anal. Biochem. , vol.230 , pp. 167-172
    • Ling, M.1    Robinson, B.H.2
  • 35
    • 0017184389 scopus 로고
    • A rapid arid sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid arid sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 36
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriopharge T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriopharge T4, Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 37
    • 0022486877 scopus 로고
    • Visualization of bilin-linked peptides and proteins in polyacrylamide gels
    • Berkelman, T., and Lagarias, J. C. (1986) Visualization of bilin-linked peptides and proteins in polyacrylamide gels, Anal. Biochem. 156, 194-201.
    • (1986) Anal. Biochem. , vol.156 , pp. 194-201
    • Berkelman, T.1    Lagarias, J.C.2
  • 39
    • 0026625689 scopus 로고
    • Protein surface topology-probing by selective chemical modification and mass spectrometric peptide mapping
    • Suckau, D., Mak, M., and Przybylski, M. (1992) Protein surface topology-probing by selective chemical modification and mass spectrometric peptide mapping, Proc. Natl. Acad. Sci. U.S.A. 89, 5630-5634.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 5630-5634
    • Suckau, D.1    Mak, M.2    Przybylski, M.3
  • 40
    • 0029968434 scopus 로고    scopus 로고
    • Probing the active site residues in aromatic donor oxidation in horseradish peroxidase: Involvement of an arginine and a tyrosine residue in aromatic donor binding
    • Adak, S., Mazumder, A., and Banerjee, R. K. (1996) Probing the active site residues in aromatic donor oxidation in horseradish peroxidase: Involvement of an arginine and a tyrosine residue in aromatic donor binding, Biochem. J. 314, 985-991.
    • (1996) Biochem. J. , vol.314 , pp. 985-991
    • Adak, S.1    Mazumder, A.2    Banerjee, R.K.3
  • 41
    • 0000399944 scopus 로고
    • Inactivation of myosin by 2,4-dinitrophenol and protection by adenosine triphosphatase and other phosphate compounds
    • Levy, H. M., Leber, P. D., and Ryan, E. M. (1963) Inactivation of myosin by 2,4-dinitrophenol and protection by adenosine triphosphatase and other phosphate compounds, J. Biol. Chem. 238, 3654-3659.
    • (1963) J. Biol. Chem. , vol.238 , pp. 3654-3659
    • Levy, H.M.1    Leber, P.D.2    Ryan, E.M.3
  • 42
    • 0028909473 scopus 로고
    • Identification of reactive lysines in phosphoenolpyruvate carboxy-kinases from Escherichia coli and Saccharomyces cerevisiae
    • Bazaes, S., Goldie, H., Cardemil, E., and Jabalquinto, A. M. (1995) Identification of reactive lysines in phosphoenolpyruvate carboxy-kinases from Escherichia coli and Saccharomyces cerevisiae, FEBS Lett. 360, 207-210.
    • (1995) FEBS Lett. , vol.360 , pp. 207-210
    • Bazaes, S.1    Goldie, H.2    Cardemil, E.3    Jabalquinto, A.M.4
  • 43
    • 0014216749 scopus 로고
    • A method for the quantitative modification and estimation of carboxylic acid group in proteins
    • Hoare, D. G., and Koshland, J. D. E. (1967) A method for the quantitative modification and estimation of carboxylic acid group in proteins, J. Biol. Chem. 242, 2447-2453.
    • (1967) J. Biol. Chem. , vol.242 , pp. 2447-2453
    • Hoare, D.G.1    Koshland, J.D.E.2
  • 44
    • 0034717042 scopus 로고    scopus 로고
    • Enzyme kinetics and chemical modification of alpha-1,4-glucan lyase from Gracilariopsis sp.
    • Nyvall, P., Pedersen, M., Kenne, L., and Gacesa, P. (2000) Enzyme kinetics and chemical modification of alpha-1,4-glucan lyase from Gracilariopsis sp., Phytochemistry 54, 139-145.
    • (2000) Phytochemistry , vol.54 , pp. 139-145
    • Nyvall, P.1    Pedersen, M.2    Kenne, L.3    Gacesa, P.4
  • 45
    • 77956994950 scopus 로고
    • Determination of the tryptophan content of proteins with N-bromosuccinimide
    • Spande, T. F., and Witkop, B. (1967) Determination of the tryptophan content of proteins with N-bromosuccinimide, Methods Enzymol. 11, 498-506.
    • (1967) Methods Enzymol. , vol.11 , pp. 498-506
    • Spande, T.F.1    Witkop, B.2
  • 46
    • 0017632673 scopus 로고
    • Modification of histidyl residues in proteins by diethylpyrocarbonate
    • Miles, E. W. (1977) Modification of histidyl residues in proteins by diethylpyrocarbonate, Methods Enzymol. 47, 431-442.
    • (1977) Methods Enzymol. , vol.47 , pp. 431-442
    • Miles, E.W.1
  • 47
    • 0001078895 scopus 로고
    • Relation between modification of functional groups of proteins and their biological activity. 1. A graphical method for the determination of the number and type of essential groups
    • Tsou, C. L. (1962) Relation between modification of functional groups of proteins and their biological activity. 1. A graphical method for the determination of the number and type of essential groups, Sci. Sin. 11, 1535-1558.
    • (1962) Sci. Sin. , vol.11 , pp. 1535-1558
    • Tsou, C.L.1
  • 48
    • 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., and Schaffner, K. (1983) Solution conformations, photophysics, and photochemistry of bili-pigments-Bilirubin and biliverdin dimethylesters and related linear tetrapyrroles, Angew. Chem., Int. Ed. Engl. 22, 656-674.
    • (1983) Angew. Chem., Int. Ed. Engl. , vol.22 , pp. 656-674
    • Braslavsky, S.E.1    Holzwarth, A.R.2    Schaffner, K.3
  • 50
    • 3242705066 scopus 로고    scopus 로고
    • Nonenzymatic chromophore attachment in biliproteins: Conform ational control by the detergent Triton X-100
    • Zhao, K. H., Zhu, J. P., Song, B., Zhou, M., Storf, M., Böhm, S., Bubenzer, C., and Scheer, H. (2004) Nonenzymatic chromophore attachment in biliproteins: Conform ational control by the detergent Triton X-100, Biochim. Biophys. Acta 1657, 131-145.
    • (2004) Biochim. Biophys. Acta , vol.1657 , pp. 131-145
    • Zhao, K.H.1    Zhu, J.P.2    Song, B.3    Zhou, M.4    Storf, M.5    Böhm, S.6    Bubenzer, C.7    Scheer, H.8
  • 51
    • 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., and Zuber, H. (1981) Isolation and characterization of phycoerythrocyanin and chromatic adaptation of the thermophilic cyanobacterium Mastigocladus laminosus, Arch. Microbiol. 129, 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
  • 52
    • 0025228693 scopus 로고
    • Refined three-dimensional structure of phycoerythrocyanin from the cyanobacterium Mastigocladus laminosus at 2.7 Å
    • Dürring, M., Huber, R., Bode, W., Rümbeli, R., and Zuber, H. (1990) Refined three-dimensional structure of phycoerythrocyanin from the cyanobacterium Mastigocladus laminosus at 2.7 Å, J. Mol. Biol. 211, 633-644.
    • (1990) J. Mol. Biol. , vol.211 , pp. 633-644
    • Dürring, M.1    Huber, R.2    Bode, W.3    Rümbeli, R.4    Zuber, H.5
  • 53
    • 0029884694 scopus 로고    scopus 로고
    • GOR method for predicting protein secondary structure from amino acid sequence
    • Garnier, J., Gibrat, J. F., and Robson, B. (1996) GOR method for predicting protein secondary structure from amino acid sequence, Methods Enzymol. 266, 540-553.
    • (1996) Methods Enzymol. , vol.266 , pp. 540-553
    • Garnier, J.1    Gibrat, J.F.2    Robson, B.3
  • 55
    • 84989762358 scopus 로고
    • Photochromic pigments in akinetes and pigment characteristics of akinetes in comparison with vegetative cells of Anabaena variabilis
    • Bjoern, G. S., Braune, W., and Bjoern, L. O. (1983) Photochromic pigments in akinetes and pigment characteristics of akinetes in comparison with vegetative cells of Anabaena variabilis, Physiol. Plant 59, 493-500.
    • (1983) Physiol. Plant. , vol.59 , pp. 493-500
    • Bjoern, G.S.1    Braune, W.2    Bjoern, L.O.3
  • 56
    • 0019946846 scopus 로고
    • Phycoerythrocyanin and phycoerythrin-Properties and occurrence in cyanobacteria
    • Bryant, D. A. (1982) Phycoerythrocyanin and phycoerythrin-Properties and occurrence in cyanobacteria, J. Gen. Microbiol. 128, 835-844.
    • (1982) J. Gen. Microbiol. , vol.128 , pp. 835-844
    • Bryant, D.A.1
  • 57
    • 0025779067 scopus 로고
    • Phycoerythrins of marine unicellular cyanobacteria. II. Characterization of phycobiliproteins with unusually high phycourobilin content
    • Swanson, R. V., Ong, L. J., Wilbanks, S. M., and Glazer, A. N. (1991) Phycoerythrins of marine unicellular cyanobacteria. II. Characterization of phycobiliproteins with unusually high phycourobilin content, J. Biol. Chem. 266, 9528-9534.
    • (1991) J. Biol. Chem. , vol.266 , pp. 9528-9534
    • Swanson, R.V.1    Ong, L.J.2    Wilbanks, S.M.3    Glazer, A.N.4
  • 58
    • 0031466353 scopus 로고    scopus 로고
    • Phytochrome photocnromism probed by site-directed mutations and chromophore esterification
    • Bhoo, S. H., Hirano, T., Jeong, H., Lee, J., Furuya, M., and Song, P. (1997) Phytochrome photocnromism probed by site-directed mutations and chromophore esterification, J. Am. Chem. Soc. 119, 11717-11718.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 11717-11718
    • Bhoo, S.H.1    Hirano, T.2    Jeong, H.3    Lee, J.4    Furuya, M.5    Song, P.6


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