메뉴 건너뛰기




Volumn 251, Issue 1-2, 1998, Pages 142-154

Role of Arg180 of the D2 protein in photosystem II structure and function

Author keywords

Cyanobacteria; Electron transport; Photosynthesis; Thylakoids; Tyrosine radicals

Indexed keywords

BACTERIOCHLOROPHYLL; MUTANT PROTEIN; TYROSINE;

EID: 0032518552     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1998.2510142.x     Document Type: Article
Times cited : (24)

References (58)
  • 1
    • 0023408258 scopus 로고
    • Structure of the reaction center from Rhodobacter sphaeroides R-26: The protein subunits
    • Allen, J. P., Feher, G., Yeates, T. O., Komiya, H. & Rees, D. C. (1987) Structure of the reaction center from Rhodobacter sphaeroides R-26: the protein subunits, Proc. Natl Acad. Sci. USA 84, 5730-5734.
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 5730-5734
    • Allen, J.P.1    Feher, G.2    Yeates, T.O.3    Komiya, H.4    Rees, D.C.5
  • 3
    • 0028980975 scopus 로고
    • 2+ depletion modifies the electron transfer on both donor and acceptor sides in photosystem II
    • 2+ depletion modifies the electron transfer on both donor and acceptor sides in photosystem II, Biochim. Biophys. Acta 1230, 155-164.
    • (1995) Biochim. Biophys. Acta , vol.1230 , pp. 155-164
    • Andréasson, L.-E.1    Vass, I.2    Styring, S.3
  • 4
    • 77956867712 scopus 로고
    • The photosynthetic oxygen evolving process
    • Amesz, J., ed. Elsevier, Amsterdam
    • Babcock, G. T. (1987) The photosynthetic oxygen evolving process, in New comprehensive biochemistry (Amesz, J., ed.) vol. 8, pp. 125-158, Elsevier, Amsterdam.
    • (1987) New Comprehensive Biochemistry , vol.8 , pp. 125-158
    • Babcock, G.T.1
  • 5
    • 0023426051 scopus 로고
    • Tyrosine radicals are involved in the photosynthetic oxygen-evolving system
    • Barry, B. A. & Babcock, G. T. (1987) Tyrosine radicals are involved in the photosynthetic oxygen-evolving system, Proc. Natl Acad. Sci. USA 84, 7099-7103.
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 7099-7103
    • Barry, B.A.1    Babcock, G.T.2
  • 6
    • 0025201528 scopus 로고
    • Tyrosine radicals in photosystem II and related model compounds. Characterization by isotopic labeling and EPR spectroscopy
    • Barry, B. A., El-Deeb, M. K., Sandusky, P. O. & Babcock, G. T. (1990) Tyrosine radicals in photosystem II and related model compounds. Characterization by isotopic labeling and EPR spectroscopy, J. Biol. Chem. 265, 20139-20143.
    • (1990) J. Biol. Chem. , vol.265 , pp. 20139-20143
    • Barry, B.A.1    El-Deeb, M.K.2    Sandusky, P.O.3    Babcock, G.T.4
  • 7
    • 0000365156 scopus 로고
    • The role of accessory bacteriochlorophyll in reaction centers of photosynthetic bacteria: Intermediate acceptor in the primary electron transfer
    • Bixon, M., Jortner, J., Michel-Beyerle, M. E., Ogrodnick, A. & Lersch, W. (1987) The role of accessory bacteriochlorophyll in reaction centers of photosynthetic bacteria: Intermediate acceptor in the primary electron transfer, Chem. Phys. Lett. 140, 626-630.
    • (1987) Chem. Phys. Lett. , vol.140 , pp. 626-630
    • Bixon, M.1    Jortner, J.2    Michel-Beyerle, M.E.3    Ogrodnick, A.4    Lersch, W.5
  • 10
    • 0028303152 scopus 로고
    • Site-directed photosystem II mutants with perturbed oxygen-evolving properties. 1. Instability or inefficient assembly of the manganese cluster in vivo
    • Chu, H. A., Nguyen, A. P. & Debus, R. J. (1994) Site-directed photosystem II mutants with perturbed oxygen-evolving properties. 1. Instability or inefficient assembly of the manganese cluster in vivo, Biochemistry 33, 6137-6149.
    • (1994) Biochemistry , vol.33 , pp. 6137-6149
    • Chu, H.A.1    Nguyen, A.P.2    Debus, R.J.3
  • 11
    • 0000652732 scopus 로고
    • Mutagenesis of His D1-198 and His D2-197 in Synechocystis PCC 6803: Effects on the primary donor of photosystem II
    • Mathis, P., ed. Kluwer Academic Publishers, Dordrecht
    • Coleman, W. J., Nixon, P. J., Vermaas, W. F. J. & Diner, B. A. (1995) Mutagenesis of His D1-198 and His D2-197 in Synechocystis PCC 6803: Effects on the primary donor of photosystem II, in Photosynthesis: from light to biosphere (Mathis, P., ed.) vol. 1, pp. 779-782, Kluwer Academic Publishers, Dordrecht.
    • (1995) Photosynthesis: From Light to Biosphere , vol.1 , pp. 779-782
    • Coleman, W.J.1    Nixon, P.J.2    Vermaas, W.F.J.3    Diner, B.A.4
  • 12
    • 33845279458 scopus 로고
    • Simulating the dynamics of the primary charge separation process in bacterial photosynthesis
    • Creighton, S., Hwang, J.-K., Warshel, A., Parson, W. W. & Norris, J. R. (1988) Simulating the dynamics of the primary charge separation process in bacterial photosynthesis, Biochemistry 27, 774-781.
    • (1988) Biochemistry , vol.27 , pp. 774-781
    • Creighton, S.1    Hwang, J.-K.2    Warshel, A.3    Parson, W.W.4    Norris, J.R.5
  • 13
    • 0028177452 scopus 로고
    • Redox interaction of Tyrosine-D with the S-states of the water-splitting complex in intact and chloride-depleted photosystem II
    • Deák, Z., Vass, I. & Styring, S. (1994) Redox interaction of Tyrosine-D with the S-states of the water-splitting complex in intact and chloride-depleted photosystem II, Biochim. Biophys. Acta 1185, 65-74.
    • (1994) Biochim. Biophys. Acta , vol.1185 , pp. 65-74
    • Deák, Z.1    Vass, I.2    Styring, S.3
  • 15
    • 0023781850 scopus 로고
    • Site-directed mutagenesis identifies a tyrosine radical involved in the photosynthetic oxygen-evolving system
    • Debus, R. J., Barry, B. A., Babcock G. T. & McIntosh, L. (1988b) Site-directed mutagenesis identifies a tyrosine radical involved in the photosynthetic oxygen-evolving system, Proc. Natl Acad. Sci. USA 85, 427-430.
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 427-430
    • Debus, R.J.1    Barry, B.A.2    Babcock, G.T.3    McIntosh, L.4
  • 16
    • 0022348605 scopus 로고
    • Structure of the protein subunits in the photosynthetic reaction center of Rhodopseudomonas viridis at 3 Å resolution
    • Deisenhofer, J., Epp, O., Miki, K., Huber, R. & Michel, H. (1985) Structure of the protein subunits in the photosynthetic reaction center of Rhodopseudomonas viridis at 3 Å resolution, Nature 318, 618-624.
    • (1985) Nature , vol.318 , pp. 618-624
    • Deisenhofer, J.1    Epp, O.2    Miki, K.3    Huber, R.4    Michel, H.5
  • 17
    • 0024433591 scopus 로고
    • The photosynthetic reaction center from the purple bacterium Rhodopseudomonas viridis
    • Deisenhofer, J. & Michel, H. (1989) The photosynthetic reaction center from the purple bacterium Rhodopseudomonas viridis, Science 245, 1463-1473.
    • (1989) Science , vol.245 , pp. 1463-1473
    • Deisenhofer, J.1    Michel, H.2
  • 19
    • 0029163236 scopus 로고
    • Determination of the pigment stoichiometry of the photochemical reaction center of photosystem II
    • Eijckelhoff, C. & Dekker, J. P. (1995) Determination of the pigment stoichiometry of the photochemical reaction center of photosystem II, Biochim. Biophys. Acta 1231, 21-28.
    • (1995) Biochim. Biophys. Acta , vol.1231 , pp. 21-28
    • Eijckelhoff, C.1    Dekker, J.P.2
  • 20
    • 0029794855 scopus 로고    scopus 로고
    • Purification and spectroscopic characterization of photosystem II reaction center complexes isolated with or without Triton X-100
    • Eijckelhoff, C., van Roon, H., de Groot, M.-L., van Grondelle, R. & Dekker, J. P. (1996) Purification and spectroscopic characterization of photosystem II reaction center complexes isolated with or without Triton X-100, Biochemistry 35, 12864-12872.
    • (1996) Biochemistry , vol.35 , pp. 12864-12872
    • Eijckelhoff, C.1    Van Roon, H.2    De Groot, M.-L.3    Van Grondelle, R.4    Dekker, J.P.5
  • 21
    • 0025776468 scopus 로고
    • Comparison of reaction centers from Rhodobacter sphaeroides and Rhodopseudomonas viridis: Overall architecture and protein-pigment interactions
    • El-Kabbani, O., Chang, C.-H., Tiede, D., Morris, J. & Schiffer, M. (1991) Comparison of reaction centers from Rhodobacter sphaeroides and Rhodopseudomonas viridis: overall architecture and protein-pigment interactions, Biochemistry 30, 5361-5369.
    • (1991) Biochemistry , vol.30 , pp. 5361-5369
    • El-Kabbani, O.1    Chang, C.-H.2    Tiede, D.3    Morris, J.4    Schiffer, M.5
  • 22
    • 0001294371 scopus 로고
    • Development of a photosystem I-less strain of Synechocystis sp. PCC 6803 for analysis of mutations in the photosystem II proteins D2 and CP43
    • Mathis, P., ed. Kluwer Academic Publishers, Dordrecht
    • Ermakova-Gerdes, S., Shestakov, S. & Vermaas, W. (1995) Development of a photosystem I-less strain of Synechocystis sp. PCC 6803 for analysis of mutations in the photosystem II proteins D2 and CP43, in Photosynthesis: from light to biosphere (Mathis, P., ed.) vol. 1, pp. 483-486, Kluwer Academic Publishers, Dordrecht.
    • (1995) Photosynthesis: From Light to Biosphere , vol.1 , pp. 483-486
    • Ermakova-Gerdes, S.1    Shestakov, S.2    Vermaas, W.3
  • 23
    • 0000058886 scopus 로고
    • Structure and function of bacterial photosynthetic reaction center
    • Feher, G., Allen, J. P., Okamura, M. Y. & Rees, D. C. (1989) Structure and function of bacterial photosynthetic reaction center, Nature 339, 111-116.
    • (1989) Nature , vol.339 , pp. 111-116
    • Feher, G.1    Allen, J.P.2    Okamura, M.Y.3    Rees, D.C.4
  • 24
    • 0030030312 scopus 로고    scopus 로고
    • Mg coordination by amino acid side chains is not required for assembly and function of the special pair in bacterial photosynthetic reaction centers
    • Goldsmith, J. O., King, B. & Boxer, S. G. (1996) Mg coordination by amino acid side chains is not required for assembly and function of the special pair in bacterial photosynthetic reaction centers, Biochemistry 35, 2421-2428.
    • (1996) Biochemistry , vol.35 , pp. 2421-2428
    • Goldsmith, J.O.1    King, B.2    Boxer, S.G.3
  • 25
    • 0027299939 scopus 로고
    • Functionally important domains of the large hydrophilic loop of CP47 as probed by oligonucleotide-directed mutagenesis in Synechocystis sp. PCC 6803
    • Haag, E., Eaton-Rye, J. J., Renger, G. & Vermaas, W. (1993) Functionally important domains of the large hydrophilic loop of CP47 as probed by oligonucleotide-directed mutagenesis in Synechocystis sp. PCC 6803, Biochemistry 32, 4444-4454.
    • (1993) Biochemistry , vol.32 , pp. 4444-4454
    • Haag, E.1    Eaton-Rye, J.J.2    Renger, G.3    Vermaas, W.4
  • 27
    • 0002079634 scopus 로고
    • Observation of a bacteriochlorophyll anion radical during the primary charge separation in a reaction center
    • Holzapfel, W., Finkele, U., Kaiser, W., Osterhelt, D. & Scheer, H. (1989) Observation of a bacteriochlorophyll anion radical during the primary charge separation in a reaction center, Chem. Phys. Lett. 160, 1-7.
    • (1989) Chem. Phys. Lett. , vol.160 , pp. 1-7
    • Holzapfel, W.1    Finkele, U.2    Kaiser, W.3    Osterhelt, D.4    Scheer, H.5
  • 31
    • 0001007875 scopus 로고
    • Site-selection spectroscopy of the reaction center complex of photosystem II. 1. Triplet-minus-singlet absorption difference: Search for a second exciton band of P-680
    • Kwa, S. L. S., Eijckelhoff, C., van Grondelle, R. & Dekker, J. P. (1994) Site-selection spectroscopy of the reaction center complex of photosystem II. 1. Triplet-minus-singlet absorption difference: search for a second exciton band of P-680, J. Phys. Chem. 98, 7702-7711.
    • (1994) J. Phys. Chem. , vol.98 , pp. 7702-7711
    • Kwa, S.L.S.1    Eijckelhoff, C.2    Van Grondelle, R.3    Dekker, J.P.4
  • 32
    • 0024976548 scopus 로고
    • Directed alteration of the D1 polypeptide of photosystem II: Evidence that tyrosine-161 is the redox component, Z, connecting the oxygen-evolving complex to the primary electron donor, P680
    • Metz, J. G., Nixon, P. J., Rogner, M., Brudvig, G. W. & Diner, B. A. (1989) Directed alteration of the D1 polypeptide of photosystem II: evidence that tyrosine-161 is the redox component, Z, connecting the oxygen-evolving complex to the primary electron donor, P680, Biochemistry 28, 6960-6969.
    • (1989) Biochemistry , vol.28 , pp. 6960-6969
    • Metz, J.G.1    Nixon, P.J.2    Rogner, M.3    Brudvig, G.W.4    Diner, B.A.5
  • 33
    • 0000999832 scopus 로고
    • Pigment-protein interactions in the photosynthetic reaction center from Rhodopseudomonas viridis
    • Michel, H., Epp, O. & Deisenhofer, J. (1986) Pigment-protein interactions in the photosynthetic reaction center from Rhodopseudomonas viridis, EMBO J. 5, 1149-1158.
    • (1986) EMBO J. , vol.5 , pp. 1149-1158
    • Michel, H.1    Epp, O.2    Deisenhofer, J.3
  • 34
    • 0043145962 scopus 로고
    • Relevance of the photosynthetic reaction center from purple bacteria to the structure of photosystem II
    • Michel, H. & Deisenhofer, J. (1988) Relevance of the photosynthetic reaction center from purple bacteria to the structure of photosystem II, Biochemistry 27, 1-7.
    • (1988) Biochemistry , vol.27 , pp. 1-7
    • Michel, H.1    Deisenhofer, J.2
  • 36
    • 0029582958 scopus 로고
    • Genetic analysis of the form and function of photosystem I and photosystem II
    • Pakrasi, H. B. (1995) Genetic analysis of the form and function of photosystem I and photosystem II, Annu. Rev. Genet. 29, 755-776.
    • (1995) Annu. Rev. Genet. , vol.29 , pp. 755-776
    • Pakrasi, H.B.1
  • 37
    • 0001035861 scopus 로고
    • Protein engineering of photosystem II
    • Barber, J., ed. Elsevier Science Publishers, Amsterdam
    • Pakrasi, H. B. & Vermaas, W. F. J. (1992) Protein engineering of photosystem II, in The photosystems: Structure, function and molecular biology (Barber, J., ed.) vol. 11, pp. 231-256, Elsevier Science Publishers, Amsterdam.
    • (1992) The Photosystems: Structure, Function and Molecular Biology , vol.11 , pp. 231-256
    • Pakrasi, H.B.1    Vermaas, W.F.J.2
  • 38
    • 34249842840 scopus 로고
    • A three-dimensional model of the photosystem II reaction center of Pisum sativum
    • Ruffle, S. V., Donnelly, D., Blundell, T. L. & Nugent, J. H. A. (1992) A three-dimensional model of the photosystem II reaction center of Pisum sativum, Photosynth. Res. 34, 287-300.
    • (1992) Photosynth. Res. , vol.34 , pp. 287-300
    • Ruffle, S.V.1    Donnelly, D.2    Blundell, T.L.3    Nugent, J.H.A.4
  • 39
    • 0027198655 scopus 로고
    • Mutation of histidine residues in CP47 leads to destabilization of the photosystem II complex and to impairment of light energy transfer
    • Shen, G., Eaton-Rye, J. J. & Vermaas, W. F. J. (1993a) Mutation of histidine residues in CP47 leads to destabilization of the photosystem II complex and to impairment of light energy transfer, Biochemistry 32, 5109-5115.
    • (1993) Biochemistry , vol.32 , pp. 5109-5115
    • Shen, G.1    Eaton-Rye, J.J.2    Vermaas, W.F.J.3
  • 40
    • 0027714687 scopus 로고
    • Synechocystis sp PCC 6803 strains lacking photosystem I and phycobilisome function
    • Shen, G., Boussiba, S. & Vermaas, W. F. J. (1993b) Synechocystis sp PCC 6803 strains lacking photosystem I and phycobilisome function, Plant Cell 5, 1853-1863.
    • (1993) Plant Cell , vol.5 , pp. 1853-1863
    • Shen, G.1    Boussiba, S.2    Vermaas, W.F.J.3
  • 41
    • 0028362512 scopus 로고
    • Mutation of chlorophyll ligands in the chlorophyll-binding CP47 protein as studied in a Synechocystis sp. PCC 6803 photosystem I-less background
    • Shen, G. & Vermaas, W. F. J. (1994) Mutation of chlorophyll ligands in the chlorophyll-binding CP47 protein as studied in a Synechocystis sp. PCC 6803 photosystem I-less background, Biochemistry 33, 7379-7388.
    • (1994) Biochemistry , vol.33 , pp. 7379-7388
    • Shen, G.1    Vermaas, W.F.J.2
  • 42
    • 0023656120 scopus 로고
    • The photochemical reaction center of Chloroflexus aurantiacus is composed of two structurally similar polypeptides
    • Shiozawa, J. A., Lottspeich, F. & Feick, R. (1987) The photochemical reaction center of Chloroflexus aurantiacus is composed of two structurally similar polypeptides, Eur. J. Biochem. 167, 595-600.
    • (1987) Eur. J. Biochem. , vol.167 , pp. 595-600
    • Shiozawa, J.A.1    Lottspeich, F.2    Feick, R.3
  • 43
    • 0025298292 scopus 로고
    • Structure of donor side components in photosystem II predicted by computer modeling
    • Svensson, B., Vass, I., Cedergren, E. & Styring, S. (1990) Structure of donor side components in photosystem II predicted by computer modeling, EMBO J. 9, 2051-2059.
    • (1990) EMBO J. , vol.9 , pp. 2051-2059
    • Svensson, B.1    Vass, I.2    Cedergren, E.3    Styring, S.4
  • 44
    • 0026215160 scopus 로고
    • Sequence analysis of the D1 and D2 reaction center proteins of photosystem II
    • Svensson, B., Vass, I. & Styring, S. (1991) Sequence analysis of the D1 and D2 reaction center proteins of photosystem II, Z. Naturforsch. 46c, 765-776.
    • (1991) Z. Naturforsch. , vol.46 C , pp. 765-776
    • Svensson, B.1    Vass, I.2    Styring, S.3
  • 45
    • 0030448542 scopus 로고    scopus 로고
    • A model for the photosystem II reaction center core including the structure of the primary donor P680
    • Svensson, B., Etchebest, C., Tuffery, P., van Kan, P., Smith, J. & Styring, S. (1996) A model for the photosystem II reaction center core including the structure of the primary donor P680, Biochemistry 35, 14486-14502.
    • (1996) Biochemistry , vol.35 , pp. 14486-14502
    • Svensson, B.1    Etchebest, C.2    Tuffery, P.3    Van Kan, P.4    Smith, J.5    Styring, S.6
  • 46
    • 0027762443 scopus 로고
    • Spectroscopic evidence from site-directed mutants of Synechocystis PCC6803 in favor of a close interaction between histidine 189 and redox-active tyrosine 160, both of polypeptide D2 of the pholosystem II reaction center
    • Tang, X.-S., Chisholm, D. A., Dismukes, G. C., Brudvig, G. W. & Diner, B. A. (1993) Spectroscopic evidence from site-directed mutants of Synechocystis PCC6803 in favor of a close interaction between histidine 189 and redox-active tyrosine 160, both of polypeptide D2 of the pholosystem II reaction center, Biochemistry 32, 13742-13748.
    • (1993) Biochemistry , vol.32 , pp. 13742-13748
    • Tang, X.-S.1    Chisholm, D.A.2    Dismukes, G.C.3    Brudvig, G.W.4    Diner, B.A.5
  • 47
    • 0000087299 scopus 로고
    • Spectral properties of stabilized D1/D2/cytochrome b-559 photosystem II reaction center complex. Effects of Triton X-100, the redox state of pheophytin, and β-carotene
    • Tetenkin, V. L., Gulyaev, B. A., Seibert, M. & Rubin, A. B. (1989) Spectral properties of stabilized D1/D2/cytochrome b-559 photosystem II reaction center complex. Effects of Triton X-100, the redox state of pheophytin, and β-carotene, FEBS Lett. 250, 459-463.
    • (1989) FEBS Lett. , vol.250 , pp. 459-463
    • Tetenkin, V.L.1    Gulyaev, B.A.2    Seibert, M.3    Rubin, A.B.4
  • 49
    • 0028063283 scopus 로고
    • D in photosystem II. Characterization by isotopic labeling and spectral simulation
    • D in photosystem II. Characterization by isotopic labeling and spectral simulation, Biochemistry 33, 11 805-11 813.
    • (1994) Biochemistry , vol.33 , pp. 11805-11813
    • Tommos, C.1    Madsen, C.2    Styring, S.3    Vermaas, W.F.J.4
  • 50
    • 0000960124 scopus 로고
    • Kok's oxygen clock: What makes it tick? The structure of P680 and consequences of its relation to the Kok cycle
    • van Gorkom, H. J. & Schelvis, J. P. M. (1993) Kok's oxygen clock: what makes it tick? The structure of P680 and consequences of its relation to the Kok cycle, Photosynth. Res. 38, 297-301.
    • (1993) Photosynth. Res. , vol.38 , pp. 297-301
    • Van Gorkom, H.J.1    Schelvis, J.P.M.2
  • 51
    • 0025891869 scopus 로고
    • A chlorophyll tilted 30° relative to the membrane in photosystem II reaction center
    • van Mieghem, F. J. E., Satoh, K. & Rutherford, A. W. (1991) A chlorophyll tilted 30° relative to the membrane in photosystem II reaction center, Biochim. Biophys. Acta 1058, 379-385.
    • (1991) Biochim. Biophys. Acta , vol.1058 , pp. 379-385
    • Van Mieghem, F.J.E.1    Satoh, K.2    Rutherford, A.W.3
  • 52
    • 0026096798 scopus 로고
    • pH-dependent charge equilibrium between tyrosine-D and the S states in photosystem II. Estimation of relative midpoint redox potentials
    • Vass, I. & Styring, S. (1991) pH-dependent charge equilibrium between tyrosine-D and the S states in photosystem II. Estimation of relative midpoint redox potentials, Biochemistry 30, 830-839.
    • (1991) Biochemistry , vol.30 , pp. 830-839
    • Vass, I.1    Styring, S.2
  • 53
    • 0000398284 scopus 로고
    • Molecular biological approaches to analyze photosystem II structure and function
    • Vermaas, W. F. J. (1993) Molecular biological approaches to analyze photosystem II structure and function, Annu. Rev. Plant Physiol. Plant Biol. 44, 457-481.
    • (1993) Annu. Rev. Plant Physiol. Plant Biol. , vol.44 , pp. 457-481
    • Vermaas, W.F.J.1
  • 54
    • 0001375803 scopus 로고
    • Site-directed mutagenesis in photosystem II of the cyanobacterium Synechocystis sp. PCC 6803: Donor D is a tyrosine residue in the D2 protein
    • Vermaas, W. F. J., Rutherford, A. W. & Hansson, Ö. (1988) Site-directed mutagenesis in photosystem II of the cyanobacterium Synechocystis sp. PCC 6803: donor D is a tyrosine residue in the D2 protein, Proc. Natl Acad. Sci. USA 85, 8477-8481.
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 8477-8481
    • Vermaas, W.F.J.1    Rutherford, A.W.2    Hansson, Ö.3
  • 55
    • 0000042415 scopus 로고
    • System for site-directed mutagenesis in psbD1/C operon of Synechocystis sp. 6803
    • Baltscheffsky, M., ed. Kluwer Academic Publishers, Dordrecht
    • Vermaas, W. F. J., Charité, J. & Eggers, B. (1990a) System for site-directed mutagenesis in psbD1/C operon of Synechocystis sp. 6803, in Current Research in Photosynthesis (Baltscheffsky, M., ed.) vol. 1, pp. 231-238, Kluwer Academic Publishers, Dordrecht.
    • (1990) Current Research in Photosynthesis , vol.1 , pp. 231-238
    • Vermaas, W.F.J.1    Charité, J.2    Eggers, B.3
  • 56
    • 84945025470 scopus 로고
    • A binding in D2 contributes to the functional and structural stability of photosystem II
    • A binding in D2 contributes to the functional and structural stability of photosystem II, Z. Naturforsch. 45c, 359-365.
    • (1990) Z. Naturforsch. , vol.45 C , pp. 359-365
    • Vermaas, W.1    Charité, J.2    Shen, G.3
  • 57
    • 0023942373 scopus 로고
    • A new possible binding site for bacteriochlorophyll b in a light-harvesting polypeptide of the bacterium Ectothiorhodospira halochloris
    • Wagner-Huber, R., Brunisholz, R. A., Bissig, I., Frank, G. & Zuber, H. (1988) A new possible binding site for bacteriochlorophyll b in a light-harvesting polypeptide of the bacterium Ectothiorhodospira halochloris, FEBS Lett. 283, 7-11.
    • (1988) FEBS Lett. , vol.283 , pp. 7-11
    • Wagner-Huber, R.1    Brunisholz, R.A.2    Bissig, I.3    Frank, G.4    Zuber, H.5
  • 58
    • 0030476341 scopus 로고
    • Heterogeneity and pigment composition of isolated photosystem II reaction centers
    • Zheleva, D., Hankamer, B. & Barber, J. (1990) Heterogeneity and pigment composition of isolated photosystem II reaction centers, Biochemistry 35, 15074-15079.
    • (1990) Biochemistry , vol.35 , pp. 15074-15079
    • Zheleva, D.1    Hankamer, B.2    Barber, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.