메뉴 건너뛰기




Volumn 83, Issue 1, 2007, Pages 177-186

Type 1 reaction center of photosynthetic heliobacteria

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; BENZOQUINONE; BENZOQUINONE DERIVATIVE; CHLOROPHYLL; CHLOROPHYLL A; CYTOCHROME C; IRON SULFUR PROTEIN; PSCA PROTEIN, GREEN SULFUR BACTERIA; UNCLASSIFIED DRUG;

EID: 34247850982     PISSN: 00318655     EISSN: None     Source Type: Journal    
DOI: 10.1562/2006-03-29-IR-860     Document Type: Conference Paper
Times cited : (58)

References (93)
  • 1
    • 0001832861 scopus 로고
    • The family Heliobacteriaceae
    • In. Edited by. A. Balows, H. G. Trüper, M. Dworkin, W. Harder. K.-H. Schleifer. pp. Springer, Berlin Heidelberg New York.
    • Madigan, M. T. (1992) The family Heliobacteriaceae. In The prokaryotes, 2nd edn Edited by A. Balows, H. G. Trüper, M. Dworkin, W. Harder K.-H. Schleifer pp. 1981 1992. Springer, Berlin Heidelberg New York.
    • (1992) The prokaryotes, 2nd edn , pp. 1981-1992
    • Madigan, M.T.1
  • 2
    • 0027105895 scopus 로고
    • Origin and early evolution of photosynthesis
    • Blankenship, R. E. (1992) Origin and early evolution of photosynthesis. Photosynth. Res. 33, 91 111.
    • (1992) Photosynth. Res. , vol.33 , pp. 91-111
    • Blankenship, R.E.1
  • 3
    • 0034622999 scopus 로고    scopus 로고
    • Molecular evidence for the early evolution of photosynthesis
    • Xiong, J., W. M. Fischer, K. Inoue, M. Nakahara C. E. Bauer (2000) Molecular evidence for the early evolution of photosynthesis. Science 289, 1724 1730.
    • (2000) Science , vol.289 , pp. 1724-1730
    • Xiong, J.1    Fischer, W.M.2    Inoue, K.3    Nakahara, M.4    Bauer, C.E.5
  • 4
    • 0001822260 scopus 로고
    • Taxonomy, physiology and ecology of heliobacteria
    • In. Edited by. R. E. Blankenship, M. T. Madigan. C. E. Bauer. pp. Kluwer Academic Publishers, Dordrecht, The Netherlands.
    • Madigan, M. T. J. G. Ormerod (1995) Taxonomy, physiology and ecology of heliobacteria. In Anoxygenic Photosynthetic Bacteria (Edited by R. E. Blankenship, M. T. Madigan C. E. Bauer pp. 17 30. Kluwer Academic Publishers, Dordrecht, The Netherlands.
    • (1995) Anoxygenic Photosynthetic Bacteria , pp. 17-30
    • Madigan, M.T.1    Ormerod, J.G.2
  • 5
    • 0032872485 scopus 로고    scopus 로고
    • Heliorestis daurensis, gen. nov. sp. nov., an alkaliphilic rod-to-coiled-shaped phototrophic heliobacterium from a Siberian soda lake
    • Bryantseva, I. A., V. M. Gorlenko, E. I. Kompantseva, L. A. Achenbach M. T. Madigan (1999) Heliorestis daurensis, gen. nov. sp. nov., an alkaliphilic rod-to-coiled-shaped phototrophic heliobacterium from a Siberian soda lake. Arch. Microbiol. 172, 167 174.
    • (1999) Arch. Microbiol. , vol.172 , pp. 167-174
    • Bryantseva, I.A.1    Gorlenko, V.M.2    Kompantseva, E.I.3    Achenbach, L.A.4    Madigan, M.T.5
  • 7
    • 0002957528 scopus 로고
    • The antenna-reaction center complex of heliobacteria
    • In. Edited by. R. E. Blankenship, M. T. Madigan. C. E. Bauer. pp. Kluwer Academic Publishers, Dordrecht, The Netherlands.
    • Amesz, J. (1995) The antenna-reaction center complex of heliobacteria. In Anoxygenic Photosynthetic Bacteria (Edited by R. E. Blankenship, M. T. Madigan C. E. Bauer pp. 687 697. Kluwer Academic Publishers, Dordrecht, The Netherlands.
    • (1995) Anoxygenic Photosynthetic Bacteria , pp. 687-697
    • Amesz, J.1
  • 8
    • 0027186183 scopus 로고
    • Single core polypeptide in the reaction center of the photosynthetic bacterium Heliobacillus mobilis: Structural implication and relations to other photosystems
    • Liebl, U., M. Mockensturm-Wilson, J. T. Trost, D. C. Brune, R. E. Blankenship W. Vermaas (1993) Single core polypeptide in the reaction center of the photosynthetic bacterium Heliobacillus mobilis: Structural implication and relations to other photosystems. Proc. Natl. Acad. Sci. USA 90, 7124 7128.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 7124-7128
    • Liebl, U.1    Mockensturm-Wilson, M.2    Trost, J.T.3    Brune, D.C.4    Blankenship, R.E.5    Vermaas, W.6
  • 10
    • 0022348605 scopus 로고
    • Structure of the protein subunits in the photosynthetic reaction centre of Rhodopseudomonas viridis at 3 Å resolution
    • Deisenhofer, J., O. Epp, K. Miki, R. Huber H. Michel (1985) Structure of the protein subunits in the photosynthetic reaction centre 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
  • 11
    • 0035927420 scopus 로고    scopus 로고
    • Three-dimensional structure of cyanobacterial photosystem I at 2.5 Å resolution
    • Jordan, P., P. Fromme, H. T. Witt, O. Klukas, W. Saenger N. Krauss (2001) Three-dimensional structure of cyanobacterial photosystem I at 2.5 Å resolution. Nature 411, 909 917.
    • (2001) Nature , vol.411 , pp. 909-917
    • Jordan, P.1    Fromme, P.2    Witt, H.T.3    Klukas, O.4    Saenger, W.5    Krauss, N.6
  • 12
    • 0035825682 scopus 로고    scopus 로고
    • Crystal structure of photosystem II from Synechococcus elongatus at 3.8 Å resolution
    • Zouni, A., H. T. Witt, J. Kern, P. Fromme, N. Krauss, W. Saenger P. Orth (2001) Crystal structure of photosystem II from Synechococcus elongatus at 3.8 Å resolution. Nature 409, 739 743.
    • (2001) Nature , vol.409 , pp. 739-743
    • Zouni, A.1    Witt, H.T.2    Kern, J.3    Fromme, P.4    Krauss, N.5    Saenger, W.6    Orth, P.7
  • 13
    • 0348148910 scopus 로고    scopus 로고
    • Crystal structure of plant photosystem I
    • Ben-Shem, A., F. Frolow N. Nelson (2003) Crystal structure of plant photosystem I. Nature 426, 630 635.
    • (2003) Nature , vol.426 , pp. 630-635
    • Ben-Shem, A.1    Frolow, F.2    Nelson, N.3
  • 14
    • 0035976008 scopus 로고    scopus 로고
    • The antenna reaction center complex of heliobacteria: Composition, energy conversion and electron transfer
    • Neerken, S. J. Amesz (2001) The antenna reaction center complex of heliobacteria: Composition, energy conversion and electron transfer. Biochim. Biophys. Acta 1507, 278 290.
    • (2001) Biochim. Biophys. Acta , vol.1507 , pp. 278-290
    • Neerken, S.1    Amesz, J.2
  • 15
    • 0024844619 scopus 로고
    • Isolation of a photoactive photosynthetic reaction center-core antenna complex from Helobacillus mobilis
    • Trost, J. T. R. E. Blankenship (1989) Isolation of a photoactive photosynthetic reaction center-core antenna complex from Helobacillus mobilis. Biochemistry 28, 9898 9904.
    • (1989) Biochemistry , vol.28 , pp. 9898-9904
    • Trost, J.T.1    Blankenship, R.E.2
  • 16
    • 0025136715 scopus 로고
    • Purification and properties of an antenna-reaction center complex from heliobacteria
    • van de Meent, E. J., F. A. M. Kleinherenbrink J. Amesz (1990) Purification and properties of an antenna-reaction center complex from heliobacteria. Biochim. Biophys. Acta 1015, 223 230.
    • (1990) Biochim. Biophys. Acta , vol.1015 , pp. 223-230
    • Van De Meent, E.J.1    Kleinherenbrink, F.A.M.2    Amesz, J.3
  • 17
    • 0027105835 scopus 로고
    • Protein sequences and redox titrations indicate that the electron acceptors in reaction centers from heliobacteria are similar to Photosystem I
    • Trost, J. T., D. C. Brune R. E. Blankenship (1992) Protein sequences and redox titrations indicate that the electron acceptors in reaction centers from heliobacteria are similar to Photosystem I. Photosynth. Res. 32, 11 22.
    • (1992) Photosynth. Res. , vol.32 , pp. 11-22
    • Trost, J.T.1    Brune, D.C.2    Blankenship, R.E.3
  • 18
    • 0030783093 scopus 로고    scopus 로고
    • Fourier transform infrared study on the primary donor P798 of Heliobacterium modesticaldum: Cysteine S-H coupled to P798 and molecular interactions of carbonyl groups
    • Noguchi, T., Y. Fukami, H. Oh-oka Y. Inoue (1997) Fourier transform infrared study on the primary donor P798 of Heliobacterium modesticaldum: Cysteine S-H coupled to P798 and molecular interactions of carbonyl groups. Biochemistry 36, 12329 12336.
    • (1997) Biochemistry , vol.36 , pp. 12329-12336
    • Noguchi, T.1    Fukami, Y.2    Oh-Oka, H.3    Inoue, Y.4
  • 19
  • 20
    • 22744458890 scopus 로고    scopus 로고
    • Resolution and reconstitution of a bound Fe-S protein from the photosynthetic reaction center of Heliobacterium modesticaldum
    • Heinnickel, M., G. Shen, R. Agalarov J. H. Golbeck (2005) Resolution and reconstitution of a bound Fe-S protein from the photosynthetic reaction center of Heliobacterium modesticaldum. Biochemistry 44, 9950 9960.
    • (2005) Biochemistry , vol.44 , pp. 9950-9960
    • Heinnickel, M.1    Shen, G.2    Agalarov, R.3    Golbeck, J.H.4
  • 21
    • 2442711420 scopus 로고    scopus 로고
    • Sequence of the core antenna domain from the anoxygenic phototroph Heliophilum fasciatum: Implication for diversity of reaction center type I
    • Mix, L. J., T. L. Harmer C. M. Cavanaugh (2004) Sequence of the core antenna domain from the anoxygenic phototroph Heliophilum fasciatum: Implication for diversity of reaction center type I. Curr. Microbiol. 48, 438 440.
    • (2004) Curr. Microbiol. , vol.48 , pp. 438-440
    • Mix, L.J.1    Harmer, T.L.2    Cavanaugh, C.M.3
  • 22
    • 0032504023 scopus 로고    scopus 로고
    • A common ancestor for oxygenic and anoxygenic photosynthetic systems: A comparison based on the structural model of photosystem I
    • Schubert, W.-D., O. Klukas, W. Saenger, H. T. Witt, P. Fromme N. Krauss (1998) A common ancestor for oxygenic and anoxygenic photosynthetic systems: A comparison based on the structural model of photosystem I. J. Mol. Biol. 280, 297 314.
    • (1998) J. Mol. Biol. , vol.280 , pp. 297-314
    • Schubert, W.-D.1    Klukas, O.2    Saenger, W.3    Witt, H.T.4    Fromme, P.5    Krauss, N.6
  • 23
    • 0036469776 scopus 로고    scopus 로고
    • Reaction centres: The structure and evolution of biological solar power
    • Heathcote, P., P. K. Fyfe M. R. Jones (2002) Reaction centres: The structure and evolution of biological solar power. Trends Biochem. Sci. 27, 79 87.
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 79-87
    • Heathcote, P.1    Fyfe, P.K.2    Jones, M.R.3
  • 26
    • 0029864547 scopus 로고    scopus 로고
    • FTIR spectroscopy of primary donor photooxidation in photosystem I, Heliobacillus mobilis, and Chlorobium limicola. Comparison with purple bacteria
    • Nabedryk, E., W. Leibl J. Breton (1996) FTIR spectroscopy of primary donor photooxidation in photosystem I, Heliobacillus mobilis, and Chlorobium limicola. Comparison with purple bacteria. Photosynth. Res. 48, 301 308.
    • (1996) Photosynth. Res. , vol.48 , pp. 301-308
    • Nabedryk, E.1    Leibl, W.2    Breton, J.3
  • 27
    • 0036230812 scopus 로고    scopus 로고
    • Electron donation from membrane-bound cytochrome c to the photosynthetic reaction center in whole cells and isolated membranes of Heliobacterium gestii
    • Oh-oka, H., M. Iwaki S. Itoh (2002) Electron donation from membrane-bound cytochrome c to the photosynthetic reaction center in whole cells and isolated membranes of Heliobacterium gestii. Photosynth. Res. 71, 137 147.
    • (2002) Photosynth. Res. , vol.71 , pp. 137-147
    • Oh-Oka, H.1    Iwaki, M.2    Itoh, S.3
  • 28
    • 0000283227 scopus 로고
    • Thermodynamic properties of the photochemical reaction center of Heliobacterium chlorum
    • Prince, R. C., H. Gest R. E. Blankenship (1985) Thermodynamic properties of the photochemical reaction center of Heliobacterium chlorum. Biochim. Biophys. Acta 810, 377 384.
    • (1985) Biochim. Biophys. Acta , vol.810 , pp. 377-384
    • Prince, R.C.1    Gest, H.2    Blankenship, R.E.3
  • 29
    • 0025138328 scopus 로고
    • Photosynthetic electron transfer in Heliobacterium chlorum studied by EPR spectroscopy
    • Fischer, M. R (1990) Photosynthetic electron transfer in Heliobacterium chlorum studied by EPR spectroscopy. Biochim. Biophys. Acta 1015, 471 481.
    • (1990) Biochim. Biophys. Acta , vol.1015 , pp. 471-481
    • Fischer, M.R.1
  • 31
    • 33646868785 scopus 로고    scopus 로고
    • ESR signal of the iron-sulfur center FX and its function in the homodimeric reaction center of Heliobacterium modesticaldum
    • Miyamoto, R., M. Iwaki, H. Mino, J. Harada, S. Itoh H. Oh-oka (2006) ESR signal of the iron-sulfur center FX and its function in the homodimeric reaction center of Heliobacterium modesticaldum. Biochemistry 45, 6306 6316.
    • (2006) Biochemistry , vol.45 , pp. 6306-6316
    • Miyamoto, R.1    Iwaki, M.2    Mino, H.3    Harada, J.4    Itoh, S.5    Oh-Oka, H.6
  • 33
    • 0029824759 scopus 로고    scopus 로고
    • Function of the reacion center of green sulfur bacteria
    • Sakurai, H., N. Kusumoto K. Inoue (1996) Function of the reacion center of green sulfur bacteria. Photochem. Photobiol. 64, 5 13.
    • (1996) Photochem. Photobiol. , vol.64 , pp. 5-13
    • Sakurai, H.1    Kusumoto, N.2    Inoue, K.3
  • 35
    • 0021826509 scopus 로고
    • A unique photosynthetic reaction center from Heliobacterium chlorum
    • Fuller, R. C., S. G. Sprague, H. Gest R. E. Blankenship (1985) A unique photosynthetic reaction center from Heliobacterium chlorum. FEBS Lett. 182, 345 349.
    • (1985) FEBS Lett. , vol.182 , pp. 345-349
    • Fuller, R.C.1    Sprague, S.G.2    Gest, H.3    Blankenship, R.E.4
  • 36
    • 0015115081 scopus 로고
    • The isolation and characterization of a photochemically active complex from Chloropseudomonas ethylica
    • Fowler, C. F., N. A. Nugent R. C. Fuller (1971) The isolation and characterization of a photochemically active complex from Chloropseudomonas ethylica. Proc. Natl. Acad. Sci. USA 68, 2278 2282.
    • (1971) Proc. Natl. Acad. Sci. USA , vol.68 , pp. 2278-2282
    • Fowler, C.F.1    Nugent, N.A.2    Fuller, R.C.3
  • 37
    • 0035976015 scopus 로고    scopus 로고
    • Electron nuclear double resonance (ENDOR) spectroscopy of radicals in photosystem I and related Type 1 photosynthetic reaction centres
    • Rigby, S. E. J., M. C. W. Evans P. Heathcote (2001) Electron nuclear double resonance (ENDOR) spectroscopy of radicals in photosystem I and related Type 1 photosynthetic reaction centres. Biochim. Biophys. Acta 1507, 247 259.
    • (2001) Biochim. Biophys. Acta , vol.1507 , pp. 247-259
    • Rigby, S.E.J.1    Evans, M.C.W.2    Heathcote, P.3
  • 38
    • 0027253705 scopus 로고
    • Stoichiometries and rates of electron transfer and charge recombination in Heliobacterium chlorum
    • Kleinherenbrink, F. A. M. J. Amesz (1993) Stoichiometries and rates of electron transfer and charge recombination in Heliobacterium chlorum. Biochim. Biophys. Acta 1143, 77 83.
    • (1993) Biochim. Biophys. Acta , vol.1143 , pp. 77-83
    • Kleinherenbrink, F.A.M.1    Amesz, J.2
  • 39
    • 0028474518 scopus 로고
    • Spectroscopic evidence for the presence of an iron-sulfur center similar to FX of Photosystem I in Heliobacillus mobilis
    • Kleinherenbrink, F. A. M., H. C. Chiou, R. LoBrutto R. E. Blankenship (1994a) Spectroscopic evidence for the presence of an iron-sulfur center similar to FX of Photosystem I in Heliobacillus mobilis. Photosynth. Res. 41, 115 123.
    • (1994) Photosynth. Res. , vol.41 , pp. 115-123
    • Kleinherenbrink, F.A.M.1    Chiou, H.C.2    LoBrutto, R.3    Blankenship, R.E.4
  • 40
    • 0027958068 scopus 로고
    • Time-resolved spectroscopy of energy and electron transfer processes in the photosynthetic bacterium Heliobacillus mobilis
    • Lin, S., H. C. Chiou, F. A. M. Kleinherenbrink R. E. Blankenship (1994) Time-resolved spectroscopy of energy and electron transfer processes in the photosynthetic bacterium Heliobacillus mobilis. Biophys. J. 66, 437 445.
    • (1994) Biophys. J. , vol.66 , pp. 437-445
    • Lin, S.1    Chiou, H.C.2    Kleinherenbrink, F.A.M.3    Blankenship, R.E.4
  • 41
    • 21244455227 scopus 로고    scopus 로고
    • Determination of stereochemistry of bacteriochlorophyll gF and 81-hydroxy-chlorophyll aF from Heliobacterium modesticaldum
    • Mizoguchi, T., H. Oh-oka H. Tamiaki (2005) Determination of stereochemistry of bacteriochlorophyll gF and 81-hydroxy-chlorophyll aF from Heliobacterium modesticaldum. Photochem. Photobiol. 81, 666 673.
    • (2005) Photochem. Photobiol. , vol.81 , pp. 666-673
    • Mizoguchi, T.1    Oh-Oka, H.2    Tamiaki, H.3
  • 42
    • 0002595922 scopus 로고    scopus 로고
    • Photosystem I electron transfer reactions - Components and kinetics
    • In. Edited by. D. R. Ort. C. F. Yocum. pp. Kluwer Academic Publishers, Dordrecht, The Netherlands.
    • Malkin, R. (1996) Photosystem I electron transfer reactions - components and kinetics. In Oxygenic Photosynthesis: The Light Reactions (Edited by D. R. Ort C. F. Yocum pp. 313 332. Kluwer Academic Publishers, Dordrecht, The Netherlands.
    • (1996) Oxygenic Photosynthesis: The Light Reactions , pp. 313-332
    • Malkin, R.1
  • 44
    • 0000070127 scopus 로고
    • Excited states and primary photochemical reactions in the photosynthetic bacterium Heliobacterium chlorum
    • Nuijs, A. M., R. J. van Dorssen, L. N. M. Duysens J. Amesz (1985) Excited states and primary photochemical reactions in the photosynthetic bacterium Heliobacterium chlorum. Proc. Natl. Acad. Sci. USA 82, 6865 6868.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 6865-6868
    • Nuijs, A.M.1    Van Dorssen, R.J.2    Duysens, L.N.M.3    Amesz, J.4
  • 45
    • 0025752939 scopus 로고
    • Charge separation and formation of bacteriochlorophyll triplets in Heliobacterium chlorum
    • Kleinherenbrink, F. A. M., T. J. Aartsma J. Amesz (1991) Charge separation and formation of bacteriochlorophyll triplets in Heliobacterium chlorum. Biochim. Biophys. Acta 1057, 346 352.
    • (1991) Biochim. Biophys. Acta , vol.1057 , pp. 346-352
    • Kleinherenbrink, F.A.M.1    Aartsma, T.J.2    Amesz, J.3
  • 46
    • 0028346037 scopus 로고
    • Delayed fluorescence from Fe-S type photosynthetic reaction centers at low redox potential
    • Kleinherenbrink, F. A., G. Hastings, B. P. Wittmerhaus R. E. Blankenship (1994b) Delayed fluorescence from Fe-S type photosynthetic reaction centers at low redox potential. Biochemistry 33, 3096 3105.
    • (1994) Biochemistry , vol.33 , pp. 3096-3105
    • Kleinherenbrink, F.A.1    Hastings, G.2    Wittmerhaus, B.P.3    Blankenship, R.E.4
  • 47
    • 0000535614 scopus 로고
    • Electron transport and triplet formation in membranes of the photosynthetic bacterium Heliobacterium chlorum
    • Smit, H. W. J., J. Amesz M. F. R. van der Hoeven (1987) Electron transport and triplet formation in membranes of the photosynthetic bacterium Heliobacterium chlorum. Biochim. Biophys. Acta 893, 232 240.
    • (1987) Biochim. Biophys. Acta , vol.893 , pp. 232-240
    • Smit, H.W.J.1    Amesz, J.2    Van Der Hoeven, M.F.R.3
  • 49
    • 0028846527 scopus 로고
    • Secondary electron transfer processes in membranes of Heliobacillus mobilis
    • Lin, S., H.-C. Chiou R. E. Blankenship (1995) Secondary electron transfer processes in membranes of Heliobacillus mobilis. Biochemistry 34, 12761 12767.
    • (1995) Biochemistry , vol.34 , pp. 12761-12767
    • Lin, S.1    Chiou, H.-C.2    Blankenship, R.E.3
  • 50
    • 0032565105 scopus 로고    scopus 로고
    • Electron transfer in the heliobacterial reaction center: Evidence against a quinone-type electron acceptor functioning analogous to A1 in photosystem I
    • Brettel, K., W. Leibl U. Liebl (1998) Electron transfer in the heliobacterial reaction center: Evidence against a quinone-type electron acceptor functioning analogous to A1 in photosystem I. Biochim. Biophys. Acta 1363, 175 181.
    • (1998) Biochim. Biophys. Acta , vol.1363 , pp. 175-181
    • Brettel, K.1    Leibl, W.2    Liebl, U.3
  • 51
    • 0033152572 scopus 로고    scopus 로고
    • ENDOR and special TRIPLE resonance spectroscopy of photoaccumulated semiquinone electron acceptors in the reaction centers of green sulfur bacteria and heliobacteria
    • Muhiuddin, I. P., S. E. J. Rigby, M. C. W. Evans, J. Amesz P. Heathcote (1999) ENDOR and special TRIPLE resonance spectroscopy of photoaccumulated semiquinone electron acceptors in the reaction centers of green sulfur bacteria and heliobacteria. Biochemistry 38, 7159 7167.
    • (1999) Biochemistry , vol.38 , pp. 7159-7167
    • Muhiuddin, I.P.1    Rigby, S.E.J.2    Evans, M.C.W.3    Amesz, J.4    Heathcote, P.5
  • 52
    • 0017083870 scopus 로고
    • The properties of the primary electron acceptor in the Photosystem I reaction centre of spinach chloroplasts and its interaction with P700 and the bound ferredoxin in various oxidation-reduction states
    • Evans, M. C., C. K. Sihra R. Cammack (1976) The properties of the primary electron acceptor in the Photosystem I reaction centre of spinach chloroplasts and its interaction with P700 and the bound ferredoxin in various oxidation-reduction states. Biochem. J. 158, 71 77.
    • (1976) Biochem. J. , vol.158 , pp. 71-77
    • Evans, M.C.1    Sihra, C.K.2    Cammack, R.3
  • 54
    • 33744717871 scopus 로고    scopus 로고
    • Identification of FX in the heliobacterial reaction center as a [4Fe-4S] cluster with an S = 3/2 ground spin state
    • Heinnickel, M., R. Agalarov, N. Svensen, C. Krebs J. H. Golbeck (2006) Identification of FX in the heliobacterial reaction center as a [4Fe-4S] cluster with an S = 3/2 ground spin state. Biochemistry 45, 6756 6764.
    • (2006) Biochemistry , vol.45 , pp. 6756-6764
    • Heinnickel, M.1    Agalarov, R.2    Svensen, N.3    Krebs, C.4    Golbeck, J.H.5
  • 55
    • 0029802455 scopus 로고    scopus 로고
    • Temperature dependence of charge recombination in Heliobacillus mobilis
    • Chiou, H.-C. R. E. Blankenship (1996) Temperature dependence of charge recombination in Heliobacillus mobilis. Photochem. Photobiol. 64, 32 37.
    • (1996) Photochem. Photobiol. , vol.64 , pp. 32-37
    • Chiou, H.-C.1    Blankenship, R.E.2
  • 56
    • 0031743870 scopus 로고    scopus 로고
    • Transient electron paramagnetic resonance spectroscopy on green-sulfur bacteria and heliobacteria at two microwave frequencies
    • van der Est, A., C. Hager-Braun, W. Leibl, G. Hauska D. Stehlik (1998) Transient electron paramagnetic resonance spectroscopy on green-sulfur bacteria and heliobacteria at two microwave frequencies. Biochim. Biophys. Acta 1409, 87 98.
    • (1998) Biochim. Biophys. Acta , vol.1409 , pp. 87-98
    • Van Der Est, A.1    Hager-Braun, C.2    Leibl, W.3    Hauska, G.4    Stehlik, D.5
  • 57
    • 33646857763 scopus 로고    scopus 로고
    • Spectroscopic studies of the two different reaction center preparations from Heliobacterium modesticaldum
    • In. Edited by. A. van der Est. D. Bruce. pp. Allen Press, Lawrence, KA, USA.
    • Oh-oka, H., M. Iwaki, R. Miyamoto, H. Mino S. Itoh (2005) Spectroscopic studies of the two different reaction center preparations from Heliobacterium modesticaldum. In Photosynthesis: Fundamental Aspects to Global Perspectives (Edited by A. van der Est D. Bruce pp. 50 52. Allen Press, Lawrence, KA, USA.
    • (2005) Photosynthesis: Fundamental Aspects to Global Perspectives , pp. 50-52
    • Oh-oka, H.1    Iwaki, M.2    Miyamoto, R.3    Mino, H.4    Itoh, S.5
  • 58
    • 0000789263 scopus 로고
    • Electron transport in Heliobacterium chlorum whole cells studied by electroluminescence and absorbance difference spectroscopy
    • Vos, M. H., H. E. Klaassen H. J. van Gorkom (1989) Electron transport in Heliobacterium chlorum whole cells studied by electroluminescence and absorbance difference spectroscopy. Biochim. Biophys. Acta 973, 163 169.
    • (1989) Biochim. Biophys. Acta , vol.973 , pp. 163-169
    • Vos, M.H.1    Klaassen, H.E.2    Van Gorkom, H.J.3
  • 59
    • 0029085888 scopus 로고
    • Membrane-bound c-type cytochromes in Heliobacillus mobilis. In vivo study of the hemes involved in electron donation to the photosynthetic reaction center
    • Nitschke, W., U. Liebl, K. Matsuura D. M. Kramer (1995) Membrane-bound c-type cytochromes in Heliobacillus mobilis. In vivo study of the hemes involved in electron donation to the photosynthetic reaction center. Biochemistry 34, 11831 11839.
    • (1995) Biochemistry , vol.34 , pp. 11831-11839
    • Nitschke, W.1    Liebl, U.2    Matsuura, K.3    Kramer, D.M.4
  • 60
    • 0008851322 scopus 로고
    • Isolation of a reaction center particle and a small c-type cytochrome from Heliobacillus mobilis
    • In. Edited by. M. Baltscheffsky. pp. Kluwer, Dordrecht, The Netherlands.
    • Trost, J. T. R. E. Blankenship (1990) Isolation of a reaction center particle and a small c-type cytochrome from Heliobacillus mobilis. In Current Research in Photosynthesis (Edited by M. Baltscheffsky pp. 703 706. Kluwer, Dordrecht, The Netherlands.
    • (1990) Current Research in Photosynthesis , pp. 703-706
    • Trost, J.T.1    Blankenship, R.E.2
  • 61
    • 0030436197 scopus 로고    scopus 로고
    • Memebrane-bound c-type cytochromes in Heliobacillus mobilis. Characterisation by EPR and optical spectroscopy in membranes and detergent-solubilised material
    • Nitschke, W., B. Schoepp, B. Floss, A. Schricker, A. W. Rutherford U. Liebl (1996) Memebrane-bound c-type cytochromes in Heliobacillus mobilis. Characterisation by EPR and optical spectroscopy in membranes and detergent-solubilised material. Eur. J. Biochem. 242, 695 702.
    • (1996) Eur. J. Biochem. , vol.242 , pp. 695-702
    • Nitschke, W.1    Schoepp, B.2    Floss, B.3    Schricker, A.4    Rutherford, A.W.5    Liebl, U.6
  • 62
    • 0032560627 scopus 로고    scopus 로고
    • The 18 kDa cytochrome c553 from Heliobacterium gestii: Gene sequence and characterization of the mature protein
    • Albert, I., A. W. Rutherford, H. Grav, J. Kellermann H. Michel (1998) The 18 kDa cytochrome c553 from Heliobacterium gestii: Gene sequence and characterization of the mature protein. Biochemistry 37, 9001 9008.
    • (1998) Biochemistry , vol.37 , pp. 9001-9008
    • Albert, I.1    Rutherford, A.W.2    Grav, H.3    Kellermann, J.4    Michel, H.5
  • 63
    • 0027535989 scopus 로고
    • Electron transfer from the tetraheme cytochrome to the special pair in isolated reaction centers of Rhodopseudomonas viridis
    • Ortega, J. M. P. Mathis (1993) Electron transfer from the tetraheme cytochrome to the special pair in isolated reaction centers of Rhodopseudomonas viridis. Biochemistry 32, 1141 1151.
    • (1993) Biochemistry , vol.32 , pp. 1141-1151
    • Ortega, J.M.1    Mathis, P.2
  • 64
    • 0027754117 scopus 로고
    • Electron transfer from cytochrome c2 to the primary donor of Rhodobacter sphaeroides reaction centers. A temperature dependence study
    • Venturoli, G., A. Mallardi P. Mathis (1993) Electron transfer from cytochrome c2 to the primary donor of Rhodobacter sphaeroides reaction centers. A temperature dependence study. Biochemistry 32, 13245 13253.
    • (1993) Biochemistry , vol.32 , pp. 13245-13253
    • Venturoli, G.1    Mallardi, A.2    Mathis, P.3
  • 65
    • 0032169698 scopus 로고    scopus 로고
    • Membrane-bound cytochrome cz couples quinol oxidoreductase to the P840 reaction center complex in isolated membranes of the green sulfur bacterium Chlorobium tepidum
    • Oh-oka, H., M. Iwaki S. Itoh (1998) Membrane-bound cytochrome cz couples quinol oxidoreductase to the P840 reaction center complex in isolated membranes of the green sulfur bacterium Chlorobium tepidum. Biochemistry 37, 12293 12300.
    • (1998) Biochemistry , vol.37 , pp. 12293-12300
    • Oh-Oka, H.1    Iwaki, M.2    Itoh, S.3
  • 66
    • 0018783467 scopus 로고
    • Surface potential and reaction of membrane-bound electron transfer components. I. Reaction of P-700 in sonicated chloroplasts with redox reagents
    • Itoh, S. (1979) Surface potential and reaction of membrane-bound electron transfer components. I. Reaction of P-700 in sonicated chloroplasts with redox reagents. Biochim. Biophys. Acta 548, 579 595.
    • (1979) Biochim. Biophys. Acta , vol.548 , pp. 579-595
    • Itoh, S.1
  • 67
    • 0008844525 scopus 로고
    • Effects of net and local charges on the interaction between chemically-modified horse heart cytochrome c and P700 in photosystem 1-enriched subchloroplast particles
    • Tamura, N., S. Itoh M. Nishimura (1983) Effects of net and local charges on the interaction between chemically-modified horse heart cytochrome c and P700 in photosystem 1-enriched subchloroplast particles. Plant Cell Physiol. 24, 215 223.
    • (1983) Plant Cell Physiol. , vol.24 , pp. 215-223
    • Tamura, N.1    Itoh, S.2    Nishimura, M.3
  • 68
    • 0026517620 scopus 로고
    • A comparative laser-flash absorption spectroscopy study of algal plastocyanin and cytochrome c552 photooxidation by photosystem I particles from spinach
    • Hervás, M., M. A. De la Rosa G. Tollin (1992) A comparative laser-flash absorption spectroscopy study of algal plastocyanin and cytochrome c552 photooxidation by photosystem I particles from spinach. Eur. J. Biochem. 203, 115 120.
    • (1992) Eur. J. Biochem. , vol.203 , pp. 115-120
    • Hervás, M.1    De La Rosa, M.A.2    Tollin, G.3
  • 69
    • 0034598395 scopus 로고    scopus 로고
    • Electron transfers amongst cytochrome f, plastocyanin and photosystem I: Kinetics and mechanisms
    • Hope, A. B (2000) Electron transfers amongst cytochrome f, plastocyanin and photosystem I: Kinetics and mechanisms. Biochim. Biophys. Acta 1456, 5 26.
    • (2000) Biochim. Biophys. Acta , vol.1456 , pp. 5-26
    • Hope, A.B.1
  • 70
    • 0030899010 scopus 로고    scopus 로고
    • Cyclic electron transfer in Heliobacillus mobilis involving a menaquinol-oxidizing cytochrome bc complex and an RCI-type reaction center
    • Kramer, D. M., B. Schoepp, U. Liebl W. Nitschke (1997) Cyclic electron transfer in Heliobacillus mobilis involving a menaquinol-oxidizing cytochrome bc complex and an RCI-type reaction center. Biochemistry 36, 4203 4211.
    • (1997) Biochemistry , vol.36 , pp. 4203-4211
    • Kramer, D.M.1    Schoepp, B.2    Liebl, U.3    Nitschke, W.4
  • 71
    • 0032424309 scopus 로고    scopus 로고
    • Tracking molecular evolution of photosynthesis by characterization of a major photosynthetic gene cluster from Heliobacillus mobilis
    • Xiong, J., K. Inoue C. E. Bauer (1998) Tracking molecular evolution of photosynthesis by characterization of a major photosynthetic gene cluster from Heliobacillus mobilis. Proc. Natl. Acad. Sci. USA 95, 14851 14856.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 14851-14856
    • Xiong, J.1    Inoue, K.2    Bauer, C.E.3
  • 72
    • 0022554084 scopus 로고
    • Use of specific inhibitors on the mitochondrial bc1 complex
    • von Jagow, G. T. A. Linik (1986) Use of specific inhibitors on the mitochondrial bc1 complex. Methods Enzymol. 126, 253 271.
    • (1986) Methods Enzymol. , vol.126 , pp. 253-271
    • Von Jagow, G.1    Linik, T.A.2
  • 73
    • 0035910667 scopus 로고    scopus 로고
    • A novel hydrophobic diheme c-type cytochrome. Purification from Corynebacterium glutamicum and analysis of the QcrCBA operon encoding three subunit proteins of a putative cytochrome reductase complex
    • Sone, N., K. Nagata, H. Kojima, J. Tajima, Y. Kodera, T. Kanamaru, S. Noguchi J. Sakamoto (2001) A novel hydrophobic diheme c-type cytochrome. Purification from Corynebacterium glutamicum and analysis of the QcrCBA operon encoding three subunit proteins of a putative cytochrome reductase complex. Biochim. Biophys. Acta 1503, 279 290.
    • (2001) Biochim. Biophys. Acta , vol.1503 , pp. 279-290
    • Sone, N.1    Nagata, K.2    Kojima, H.3    Tajima, J.4    Kodera, Y.5    Kanamaru, T.6    Noguchi, S.7    Sakamoto, J.8
  • 74
    • 0037423264 scopus 로고    scopus 로고
    • Purification of a cytochrome bc-aa3 supercomplex with quinol oxidase activity from Corynebacterium glutamicum. Identification of a fourth subunity of cytochrome aa3 oxidase and mutational analysis of diheme cytochrome c1
    • Niebisch, A. M. Bott (2003) Purification of a cytochrome bc-aa3 supercomplex with quinol oxidase activity from Corynebacterium glutamicum. Identification of a fourth subunity of cytochrome aa3 oxidase and mutational analysis of diheme cytochrome c1. J. Biol. Chem. 278, 4339 4346.
    • (2003) J. Biol. Chem. , vol.278 , pp. 4339-4346
    • Niebisch, A.1    Bott, M.2
  • 75
    • 34247845533 scopus 로고    scopus 로고
    • Isolation and partial characterization of two ferredoxins from the photosynthetic bacterium Heliobacillus mobilis
    • Hatano, A., K. Inoue, D. Seo H. Sakurai (2002) Isolation and partial characterization of two ferredoxins from the photosynthetic bacterium Heliobacillus mobilis. J. Photoscience 9, 388 390.
    • (2002) J. Photoscience , vol.9 , pp. 388-390
    • Hatano, A.1    Inoue, K.2    Seo, D.3    Sakurai, H.4
  • 76
    • 0029059910 scopus 로고
    • The proton-pumping respiratory complex I of bacteria and mitochondria and its homologue in chloroplasts
    • Friedrich, T., K. Steinmuller H. Weiss (1995) The proton-pumping respiratory complex I of bacteria and mitochondria and its homologue in chloroplasts. FEBS Lett 367, 107 111.
    • (1995) FEBS Lett , vol.367 , pp. 107-111
    • Friedrich, T.1    Steinmuller, K.2    Weiss, H.3
  • 77
    • 0028231734 scopus 로고
    • Roles of the soluble cytochrome c2 and membrane-associated cytochrome cy of Rhodobacter capsulatus in photosynthetic electron transfer
    • Jenney, F. E., R.C. Prince F. Daldal (1994) Roles of the soluble cytochrome c2 and membrane-associated cytochrome cy of Rhodobacter capsulatus in photosynthetic electron transfer. Biochemistry 33, 2496 2502.
    • (1994) Biochemistry , vol.33 , pp. 2496-2502
    • Jenney, F.E.1    Prince, R.C.2    Daldal, F.3
  • 79
    • 0030746384 scopus 로고    scopus 로고
    • Viscosity dependence of the electron transfer rate from bound cytochrome c to P840 in the photosynthetic reaction center of the green sulfur bacterium Chlorobium tepidum
    • Oh-oka, H., M. Iwaki S. Itoh (1997) Viscosity dependence of the electron transfer rate from bound cytochrome c to P840 in the photosynthetic reaction center of the green sulfur bacterium Chlorobium tepidum. Biochemistry 36, 9267 9272.
    • (1997) Biochemistry , vol.36 , pp. 9267-9272
    • Oh-Oka, H.1    Iwaki, M.2    Itoh, S.3
  • 80
    • 0036230811 scopus 로고    scopus 로고
    • Kinetics of electron transfer between soluble cytochrome c-554 and purified reaction center complex from the green sulfur bacterium Chlorobium tepidum
    • Itoh, M., D. Seo, H. Sakurai P. Setif (2002) Kinetics of electron transfer between soluble cytochrome c-554 and purified reaction center complex from the green sulfur bacterium Chlorobium tepidum. Photosynth. Res. 71, 125 135.
    • (2002) Photosynth. Res. , vol.71 , pp. 125-135
    • Itoh, M.1    Seo, D.2    Sakurai, H.3    Setif, P.4
  • 81
    • 33645958935 scopus 로고    scopus 로고
    • Soluble cytochrome c-554, CycA, is not essential for the photosynthetic electron transfer in Chlorobium tepidum
    • 2194.
    • Tsukatani, Y., R. Miyamoto, S. Itoh H. Oh-oka (2006) Soluble cytochrome c-554, CycA, is not essential for the photosynthetic electron transfer in Chlorobium tepidum. FEBS Lett. 580, 2191 2194.
    • (2006) FEBS Lett. , vol.580 , pp. 2191
    • Tsukatani, Y.1    Miyamoto, R.2    Itoh, S.3    Oh-Oka, H.4
  • 82
    • 0023395661 scopus 로고
    • Structure of the reaction center from Rhodobacter sphaeroides R-26: The cofactors
    • Allen, J. P., G. Feher, T. O. Yeates, H. Komiya D. C. Rees (1987) Structure of the reaction center from Rhodobacter sphaeroides R-26: The cofactors. 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
  • 83
    • 0001337010 scopus 로고
    • The pathway, kinetics and thermodynamics of electron transfer in wild type and mutant reaction centers of purple nonsulfur bacteria
    • In. Edited by. R. E. Blankenship, M. T. Madigan. C. E. Bauer. pp. Kluwer Academic Publishers, Dordrecht, The Netherlands.
    • Woodbury, N. W. J. P. Allen (1995) The pathway, kinetics and thermodynamics of electron transfer in wild type and mutant reaction centers of purple nonsulfur bacteria. In Anoxygenic Photosynthetic Bacteria (Edited by R. E. Blankenship, M. T. Madigan C. E. Bauer pp. 527 557. Kluwer Academic Publishers, Dordrecht, The Netherlands.
    • (1995) Anoxygenic Photosynthetic Bacteria , pp. 527-557
    • Woodbury, N.W.1    Allen, J.P.2
  • 84
    • 0037422557 scopus 로고    scopus 로고
    • Crystal structure of oxygen-evolving photosystem II from Thermosynechococcus vulcanus at 3.7-A resolution
    • Kamiya, N. J. R. Shen (2003) Crystal structure of oxygen-evolving photosystem II from Thermosynechococcus vulcanus at 3.7-A resolution. Proc. Natl. Acad. Sci. USA 100, 98 103.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 98-103
    • Kamiya, N.1    Shen, J.R.2
  • 85
    • 0002281681 scopus 로고
    • Proton-coupled electron transfer reactions of QB in reaction centers from photosynthetic bacteria
    • In. Edited by. R. E. Blankenship, M. T. Madigan. C. E. Bauer. pp. Kluwer Academic Publishers, Dordrecht, The Netherlands.
    • Okamura, M. Y. G. Feher (1995) Proton-coupled electron transfer reactions of QB in reaction centers from photosynthetic bacteria. In Anoxygenic Photosynthetic Bacteria (Edited by R. E. Blankenship, M. T. Madigan C. E. Bauer pp. 577 594. Kluwer Academic Publishers, Dordrecht, The Netherlands.
    • (1995) Anoxygenic Photosynthetic Bacteria , pp. 577-594
    • Okamura, M.Y.1    Feher, G.2
  • 87
    • 0142042969 scopus 로고    scopus 로고
    • Bidirectional electron transfer in photosystem I: Electron transfer on the PsaA side is not essential for phototrophic growth in Chlamydomonas
    • Fairclough, W. V., A. Forsyth, M. C. Evans, S. E. Rigby, S. Purton P. Heathcote (2003) Bidirectional electron transfer in photosystem I: Electron transfer on the PsaA side is not essential for phototrophic growth in Chlamydomonas. Biochim. Biophys. Acta 1606, 43 55.
    • (2003) Biochim. Biophys. Acta , vol.1606 , pp. 43-55
    • Fairclough, W.V.1    Forsyth, A.2    Evans, M.C.3    Rigby, S.E.4    Purton, S.5    Heathcote, P.6
  • 88
    • 0842304732 scopus 로고    scopus 로고
    • Bidirectional electron transfer in photosystem I: Accumulation of A0- in A-side or B-side mutants of the axial ligand to chlorophyll A0
    • Ramesh, V. M., K. Gibasiewicz, S. Lin, S. E. Bingham A. N. Webber (2004) Bidirectional electron transfer in photosystem I: Accumulation of A0- in A-side or B-side mutants of the axial ligand to chlorophyll A0. Biochemistry 43, 1369 1375.
    • (2004) Biochemistry , vol.43 , pp. 1369-1375
    • Ramesh, V.M.1    Gibasiewicz, K.2    Lin, S.3    Bingham, S.E.4    Webber, A.N.5
  • 89
    • 1942534616 scopus 로고    scopus 로고
    • Evidence for asymmetric electron transfer in cyanobacterial photosystem I: Analysis of a methionine-to-leucine mutation of the ligand to the primary electron acceptor A0
    • Cohen, R. O., G. Shen, J. H. Golbeck, W. Xu, P. R. Chitnis, A. I. Valieva, A. van der Est, Y. Pushkar D. Stehlik (2004) Evidence for asymmetric electron transfer in cyanobacterial photosystem I: Analysis of a methionine-to-leucine mutation of the ligand to the primary electron acceptor A0. Biochemistry 43, 4741 4754.
    • (2004) Biochemistry , vol.43 , pp. 4741-4754
    • Cohen, R.O.1    Shen, G.2    Golbeck, J.H.3    Xu, W.4    Chitnis, P.R.5    Valieva, A.I.6    Van Der Est, A.7    Pushkar, Y.8    Stehlik, D.9
  • 90
    • 13544261421 scopus 로고    scopus 로고
    • Bidirectional electron transfer in photosystem I: Determination of two distances between P700+ and A1- in spin-correlated radical pairs
    • Santabarbara, S., I. Kuprov, W. V. Fairclough, S. Purton, P. J. Hore, P. Heathcote M. C. Evans (2005) Bidirectional electron transfer in photosystem I: Determination of two distances between P700+ and A1- in spin-correlated radical pairs. Biochemistry 44, 2119 2128.
    • (2005) Biochemistry , vol.44 , pp. 2119-2128
    • Santabarbara, S.1    Kuprov, I.2    Fairclough, W.V.3    Purton, S.4    Hore, P.J.5    Heathcote, P.6    Evans, M.C.7
  • 91
    • 0028048016 scopus 로고
    • The electronic structure of P840+: The primary donor of the Chlorobium limicola f. sp. thiosulphatophilum photosynthetic reaction centre
    • Rigby, S. E. J., R. Thapar, M. C. W. Evans P. Heathcote (1994) The electronic structure of P840+: The primary donor of the Chlorobium limicola f. sp. thiosulphatophilum photosynthetic reaction centre. FEBS Lett. 350, 24 28.
    • (1994) FEBS Lett. , vol.350 , pp. 24-28
    • Rigby, S.E.J.1    Thapar, R.2    Evans, M.C.W.3    Heathcote, P.4
  • 92
    • 0035377523 scopus 로고    scopus 로고
    • Chromosomal gene inactivation in the green sulfur bacterium Chlorobium tepidum by natural transformation
    • Frigaard, N. U. D. A. Bryant (2001) Chromosomal gene inactivation in the green sulfur bacterium Chlorobium tepidum by natural transformation. Appl. Environ. Microbiol. 67, 2538 2544.
    • (2001) Appl. Environ. Microbiol. , vol.67 , pp. 2538-2544
    • Frigaard, N.U.1    Bryant, D.A.2
  • 93
    • 10944268718 scopus 로고    scopus 로고
    • Function of a PscD subunit in a homodimeric reaction center complex of the photosynthetic green sulfur bacterium Chlorobium tepidum studied by insertional gene inactivation. Regulation of energy transfer and ferredoxin-mediated NADP+ reduction on the cytoplasmic side
    • Tsukatani, Y., R. Miyamoto, S. Itoh H. Oh-Oka (2004) Function of a PscD subunit in a homodimeric reaction center complex of the photosynthetic green sulfur bacterium Chlorobium tepidum studied by insertional gene inactivation. Regulation of energy transfer and ferredoxin-mediated NADP+ reduction on the cytoplasmic side. J. Biol. Chem. 279, 51122 51130.
    • (2004) J. Biol. Chem. , vol.279 , pp. 51122-51130
    • Tsukatani, Y.1    Miyamoto, R.2    Itoh, S.3    Oh-Oka, H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.