메뉴 건너뛰기




Volumn 46, Issue 23, 2007, Pages 6784-6794

Diazene (HN=NH) is a substrate for nitrogenase: Insights into the pathway of N2 reduction

Author keywords

[No Author keywords available]

Indexed keywords

ADDITION REACTIONS; ELECTRONS; HYDRAZINE; MOLECULAR STRUCTURE; NITROGEN; PROTONS; REDUCTION;

EID: 34250158429     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi062294s     Document Type: Article
Times cited : (98)

References (59)
  • 1
    • 0000703950 scopus 로고    scopus 로고
    • The mechanism of molybdenum nitrogenase
    • Burgess, B. K., and Lowe, D. J. (1996) The mechanism of molybdenum nitrogenase, Chem. Rev. 96, 2983-3011.
    • (1996) Chem. Rev , vol.96 , pp. 2983-3011
    • Burgess, B.K.1    Lowe, D.J.2
  • 2
    • 7744224797 scopus 로고    scopus 로고
    • Structural basis of biological nitrogen fixation
    • Howard, J. B., and Rees, D. C. (1996) Structural basis of biological nitrogen fixation, Chem. Rev. 96, 2965-2982.
    • (1996) Chem. Rev , vol.96 , pp. 2965-2982
    • Howard, J.B.1    Rees, D.C.2
  • 4
    • 0026662162 scopus 로고
    • Crystallographic structure of the nitrogenase iron protein from Azotobacter vinelandii
    • Georgiadis, M. M., Komiya, H., Chakrabarti, P., Woo, D., Kornuc, J. J., and Rees, D. C. (1992) Crystallographic structure of the nitrogenase iron protein from Azotobacter vinelandii, Science 257, 1653-1659.
    • (1992) Science , vol.257 , pp. 1653-1659
    • Georgiadis, M.M.1    Komiya, H.2    Chakrabarti, P.3    Woo, D.4    Kornuc, J.J.5    Rees, D.C.6
  • 5
    • 0001304376 scopus 로고    scopus 로고
    • Role of nucleotides in nitrogenase catalysis
    • Seefeldt, L. C., and Dean, D. R. (1997) Role of nucleotides in nitrogenase catalysis, Acc. Chem. Res. 30, 260-266.
    • (1997) Acc. Chem. Res , vol.30 , pp. 260-266
    • Seefeldt, L.C.1    Dean, D.R.2
  • 6
    • 0028289514 scopus 로고
    • Nitrogenase: A nucleotide-dependent molecular switch
    • Howard, J. B., and Rees, D. C. (1994) Nitrogenase: A nucleotide-dependent molecular switch, Annu. Rev. Biochem. 63, 235-264.
    • (1994) Annu. Rev. Biochem , vol.63 , pp. 235-264
    • Howard, J.B.1    Rees, D.C.2
  • 7
    • 0040412793 scopus 로고
    • Nitrogenase and nitrogenase reductase associate and dissociate with each catalytic cycle
    • Hageman, R. V., and Burris, R. H. (1978) Nitrogenase and nitrogenase reductase associate and dissociate with each catalytic cycle, Proc. Natl. Acad. Sci. U.S.A. 75, 2699-2702.
    • (1978) Proc. Natl. Acad. Sci. U.S.A , vol.75 , pp. 2699-2702
    • Hageman, R.V.1    Burris, R.H.2
  • 8
    • 0003859753 scopus 로고
    • On the prosthetic groups of nitrogenase
    • Coughlan, M. P, Ed, pp, Pergamon Press, Oxford
    • Orme-Johnson, W. H., and Münck, E. (1980) On the prosthetic groups of nitrogenase, in Molybdenum and molybdenum containing enzymes (Coughlan, M. P., Ed.) pp 427-438, Pergamon Press, Oxford.
    • (1980) Molybdenum and molybdenum containing enzymes , pp. 427-438
    • Orme-Johnson, W.H.1    Münck, E.2
  • 9
    • 1142275465 scopus 로고    scopus 로고
    • Substrate interactions with nitrogenase: Fe versus Mo
    • Seefeldt, L. C., Dance, I., and Dean, D. R. (2004) Substrate interactions with nitrogenase: Fe versus Mo, Biochemists 43, 1401-1409.
    • (2004) Biochemists , vol.43 , pp. 1401-1409
    • Seefeldt, L.C.1    Dance, I.2    Dean, D.R.3
  • 10
    • 15244343409 scopus 로고    scopus 로고
    • Dos, Santos, P. C., Igarashi, R. Y., Lee, H. I., Hoffman, B. M., Seefeldt, L. C., and Dean, D. R. (2005) Substrate Interactions with the nitrogenase active site, Acc. Chem. Res. 38, 208-214.
    • Dos, Santos, P. C., Igarashi, R. Y., Lee, H. I., Hoffman, B. M., Seefeldt, L. C., and Dean, D. R. (2005) Substrate Interactions with the nitrogenase active site, Acc. Chem. Res. 38, 208-214.
  • 11
    • 0017807020 scopus 로고
    • Biological nitrogen fixation by way of an enzyme-bound dinitrogen-hydride intermediate
    • Thorneley, R. N. F., Eady, R. R., and Lowe, D. J. (1978) Biological nitrogen fixation by way of an enzyme-bound dinitrogen-hydride intermediate, Nature 272, 557-558.
    • (1978) Nature , vol.272 , pp. 557-558
    • Thorneley, R.N.F.1    Eady, R.R.2    Lowe, D.J.3
  • 12
    • 0001203088 scopus 로고    scopus 로고
    • Theoretical investigations of the mechanism of biological nitrogen fixation at the FeMo cluster site
    • Dance, I. (1996) Theoretical investigations of the mechanism of biological nitrogen fixation at the FeMo cluster site, J. Biol. Inorg. Chem. 1, 581-586.
    • (1996) J. Biol. Inorg. Chem , vol.1 , pp. 581-586
    • Dance, I.1
  • 13
    • 1642351472 scopus 로고    scopus 로고
    • Chemical activity of the nitrogenase FeMo cofactor with a central nitrogen ligand: Density functional study
    • Hinnemann, B., and Nørskov, J. K. (2004) Chemical activity of the nitrogenase FeMo cofactor with a central nitrogen ligand: Density functional study, J. Am. Chem. Soc. 126, 3920-3927.
    • (2004) J. Am. Chem. Soc , vol.126 , pp. 3920-3927
    • Hinnemann, B.1    Nørskov, J.K.2
  • 15
    • 0001313303 scopus 로고    scopus 로고
    • Studies on the hydrogenation steps of the nitrogen molecule at the Azotobacter vinelandii nitrogenase site
    • Stavrev, K. K., and Zerner, M. C. (1998) Studies on the hydrogenation steps of the nitrogen molecule at the Azotobacter vinelandii nitrogenase site, Int. J. Quant. Chem. 70, 1159-1168.
    • (1998) Int. J. Quant. Chem , vol.70 , pp. 1159-1168
    • Stavrev, K.K.1    Zerner, M.C.2
  • 16
    • 33750497852 scopus 로고
    • 2 might be activated by the FeMo-cofactor in nitrogenase
    • 2 might be activated by the FeMo-cofactor in nitrogenase, Angew. Chem., Int. Ed. Engl. 32, 1062-1065.
    • (1993) Angew. Chem., Int. Ed. Engl , vol.32 , pp. 1062-1065
    • Deng, H.1    Hoffmann, R.2
  • 17
    • 34547926374 scopus 로고    scopus 로고
    • Activation and protonation of dinitrogen at the FeMo cofactor of nitrogenase
    • Kastner, J., Hemmen, S., and Blochl, P. E. (2005) Activation and protonation of dinitrogen at the FeMo cofactor of nitrogenase, J. Chem. Phys. 123, 074306.
    • (2005) J. Chem. Phys , vol.123 , pp. 074306
    • Kastner, J.1    Hemmen, S.2    Blochl, P.E.3
  • 18
    • 0037180372 scopus 로고    scopus 로고
    • An atomic-level mechanism for molybdenum nitrogenase. Part 1. Reduction of dinitrogen
    • Dunant, M. C. (2002) An atomic-level mechanism for molybdenum nitrogenase. Part 1. Reduction of dinitrogen, Biochemistry 41, 13934-13945.
    • (2002) Biochemistry , vol.41 , pp. 13934-13945
    • Dunant, M.C.1
  • 20
    • 1542318898 scopus 로고    scopus 로고
    • Dinitrogen coordination chemistry: On the biomimetic borderlands
    • Fryzuk, M. D., and MacKay, B. A. (2004) Dinitrogen coordination chemistry: On the biomimetic borderlands, Chem. Rev. 104, 385-401.
    • (2004) Chem. Rev , vol.104 , pp. 385-401
    • Fryzuk, M.D.1    MacKay, B.A.2
  • 21
    • 0014685882 scopus 로고
    • Chemical evidence concerning the function of molybdenum in nitrogenase
    • Chatt, J., Dilworth, J. R., Richards, R. L., and Sanders, J. R. (1969) Chemical evidence concerning the function of molybdenum in nitrogenase, Nature 224, 1201-1202.
    • (1969) Nature , vol.224 , pp. 1201-1202
    • Chatt, J.1    Dilworth, J.R.2    Richards, R.L.3    Sanders, J.R.4
  • 22
    • 33947092184 scopus 로고
    • Recent advances in the chemistry of nitrogen fixation
    • Chatt, J., Dilworth, J. R., and Richards, R. L. (1978) Recent advances in the chemistry of nitrogen fixation, Chem. Rev. 78, 589-625.
    • (1978) Chem. Rev , vol.78 , pp. 589-625
    • Chatt, J.1    Dilworth, J.R.2    Richards, R.L.3
  • 23
    • 3042990613 scopus 로고    scopus 로고
    • The Chatt cycle and the mechanism of enzymic reduction of molecular nitrogen
    • Pickett, C. J. (1996) The Chatt cycle and the mechanism of enzymic reduction of molecular nitrogen, J. Biol. Inorg. Chem. 1, 601-606.
    • (1996) J. Biol. Inorg. Chem , vol.1 , pp. 601-606
    • Pickett, C.J.1
  • 24
    • 0038054274 scopus 로고    scopus 로고
    • Catalytic reduction of dinitrogen to ammonia at a single molybdenum center
    • Yandulov, D. V., and Schrock, R. R. (2003) Catalytic reduction of dinitrogen to ammonia at a single molybdenum center, Science 301, 76-78.
    • (2003) Science , vol.301 , pp. 76-78
    • Yandulov, D.V.1    Schrock, R.R.2
  • 25
    • 0142248953 scopus 로고    scopus 로고
    • Catalytic reduction of dinitrogen under mild conditions
    • Schrock, R. R. (2003) Catalytic reduction of dinitrogen under mild conditions, Chem. Commun. 2389-2391.
    • (2003) Chem. Commun , pp. 2389-2391
    • Schrock, R.R.1
  • 26
    • 20744444496 scopus 로고    scopus 로고
    • Catalytic reduction of dinitrogen to ammonia at well defined single metal sites
    • Schrock, R. R. (2005) Catalytic reduction of dinitrogen to ammonia at well defined single metal sites, Phil. Trans. R. Soc. A 363, 959-969.
    • (2005) Phil. Trans. R. Soc. A , vol.363 , pp. 959-969
    • Schrock, R.R.1
  • 28
    • 0019135266 scopus 로고
    • Hydrazine as a substrate and inhibitor of Azotobacter vinelandii nitrogenase
    • Davis, L. C. (1980) Hydrazine as a substrate and inhibitor of Azotobacter vinelandii nitrogenase, Arch. Biochem. Biophys. 204, 270-276.
    • (1980) Arch. Biochem. Biophys , vol.204 , pp. 270-276
    • Davis, L.C.1
  • 29
    • 0030909004 scopus 로고    scopus 로고
    • (3+) clusters. The four-electron reduction of a N=N bond by a nitrogenase-relevant cluster and implications for the function of nitrogenase
    • (3+) clusters. The four-electron reduction of a N=N bond by a nitrogenase-relevant cluster and implications for the function of nitrogenase, J. Am. Chem. Soc. 119, 1662-1667.
    • (1997) J. Am. Chem. Soc , vol.119 , pp. 1662-1667
    • Malinak, S.M.1    Simeonov, A.M.2    Mosier, P.E.3    McKenna, C.E.4    Coucouvanis, D.5
  • 30
    • 0029961535 scopus 로고    scopus 로고
    • Reduction of cyclic and acyclic diazene derivatives by Azotobacter vinelandii nitrogenase: Diazirine and trans-dimethyldiazene
    • McKenna, C. E., Simeonov, A. M., Eran, H., and Bravo-Leerahhandh, M. (1996) Reduction of cyclic and acyclic diazene derivatives by Azotobacter vinelandii nitrogenase: diazirine and trans-dimethyldiazene, Biochemistry 35, 4502-4514.
    • (1996) Biochemistry , vol.35 , pp. 4502-4514
    • McKenna, C.E.1    Simeonov, A.M.2    Eran, H.3    Bravo-Leerahhandh, M.4
  • 31
    • 0032497358 scopus 로고    scopus 로고
    • Catalytic and biophysical properties of a nitrogenase apo-MoFe protein produced by a nifB-deletion mutant of Azotobacter vinelandii
    • Christiansen, J., Goodwin, P. J., Lanzilotta, W. N., Seefeldt, L. C., and Dean, D. R. (1998) Catalytic and biophysical properties of a nitrogenase apo-MoFe protein produced by a nifB-deletion mutant of Azotobacter vinelandii, Biochemistry 37, 12611-12623.
    • (1998) Biochemistry , vol.37 , pp. 12611-12623
    • Christiansen, J.1    Goodwin, P.J.2    Lanzilotta, W.N.3    Seefeldt, L.C.4    Dean, D.R.5
  • 32
    • 0032480797 scopus 로고    scopus 로고
    • Diazene - a not so innocent ligand for the binuclear center in cytochrome c oxidase
    • Liao, G. L., and Palmer, G. (1998) Diazene - a not so innocent ligand for the binuclear center in cytochrome c oxidase, Biochemistry 37, 15583-15592.
    • (1998) Biochemistry , vol.37 , pp. 15583-15592
    • Liao, G.L.1    Palmer, G.2
  • 33
    • 34250205225 scopus 로고    scopus 로고
    • Audrieth, D. C., and Mohr, E. B. (1953) Biurea, Inorg. Syntheses 4, 26-28.
    • Audrieth, D. C., and Mohr, E. B. (1953) Biurea, Inorg. Syntheses 4, 26-28.
  • 35
    • 11144229617 scopus 로고    scopus 로고
    • J. Biol. Chem. 279
    • Barney, B. M., Igarashi, R. Y., Dos, Santos, P. C., Dean, D. R., and Seefeldt, L. C. (2004) Substrate interaction at an iron-sulfur face of the FeMo-cofactor during nitrogenase catalysis, J. Biol. Chem. 279, 53621-53624.
    • (2004) , pp. 53621-53624
    • Barney, B.M.1    Igarashi, R.2    Dos, Y.3    Santos, P.C.4    Dean, D.R.5    Seefeldt, L.C.6
  • 37
    • 0002826498 scopus 로고    scopus 로고
    • Q-band pulsed electron spin-echo spectrometer and its application to ENDOR and ESEEM
    • Davoust, C. E., Doan, P. E., and Hoffman, B. M. (1996) Q-band pulsed electron spin-echo spectrometer and its application to ENDOR and ESEEM, J. Magn. Reson. 119, 38-44.
    • (1996) J. Magn. Reson , vol.119 , pp. 38-44
    • Davoust, C.E.1    Doan, P.E.2    Hoffman, B.M.3
  • 38
    • 0000465369 scopus 로고
    • Pulsed ENDOR experiments
    • Mims, W. B. (1965) Pulsed ENDOR experiments, Proc. R. Soc. London 238, 452-457.
    • (1965) Proc. R. Soc. London , vol.238 , pp. 452-457
    • Mims, W.B.1
  • 39
    • 0000389187 scopus 로고
    • Metalloenzyme active-site structure and function through multifrequency CW and pulsed ENDOR
    • Berliner, L. J, and Reuben, J, Eds, pp, Plenum Press, New York
    • Hoffman, B. M., DeRose, V. J., Doan, P. E., Gurbiel, R. J., Houseman, A. L. P., and Telser, J. (1993) Metalloenzyme active-site structure and function through multifrequency CW and pulsed ENDOR, in Biol. Magn. Reson. (Berliner, L. J., and Reuben, J., Eds.) pp 151-218, Plenum Press, New York.
    • (1993) Biol. Magn. Reson , pp. 151-218
    • Hoffman, B.M.1    DeRose, V.J.2    Doan, P.E.3    Gurbiel, R.J.4    Houseman, A.L.P.5    Telser, J.6
  • 40
    • 0031547577 scopus 로고    scopus 로고
    • Making hyperfine selection in Mims ENDOR independent of deadtime
    • Doan, P. E., and Hoffman, B. M. (1997) Making hyperfine selection in Mims ENDOR independent of deadtime, Chem. Phys. Lett. 269, 208-214.
    • (1997) Chem. Phys. Lett , vol.269 , pp. 208-214
    • Doan, P.E.1    Hoffman, B.M.2
  • 41
    • 0001759536 scopus 로고
    • Kinetic behavior of diazene in aqueous solutions
    • Stanbury, D. M. (1991) Kinetic behavior of diazene in aqueous solutions, Inorg. Chem. 30, 1293-1296.
    • (1991) Inorg. Chem , vol.30 , pp. 1293-1296
    • Stanbury, D.M.1
  • 43
    • 0001442098 scopus 로고
    • Kinetics and mechanisms of the nitrogenase enzyme system
    • Spiro, T. G, Ed, pp, Wiley, New York
    • Thorneley, R. N. F., and Lowe, D. J. (1985) Kinetics and mechanisms of the nitrogenase enzyme system, in Molybdenum Enzymes (Spiro, T. G., Ed.) pp 221-284, Wiley, New York.
    • (1985) Molybdenum Enzymes , pp. 221-284
    • Thorneley, R.N.F.1    Lowe, D.J.2
  • 44
    • 0043167784 scopus 로고    scopus 로고
    • Localization of a substrate binding site on FeMo-cofactor in nitrogenase: Trapping propargyl alcohol with an α-70-substituted MoFe protein
    • Benton, P. M. C., Laryukhin, M., Mayer, S. M., Hoffman, B. M., Dean, D. R., and Seefeldt, L. C. (2003) Localization of a substrate binding site on FeMo-cofactor in nitrogenase: trapping propargyl alcohol with an α-70-substituted MoFe protein, Biochemistry 42, 9102-9109.
    • (2003) Biochemistry , vol.42 , pp. 9102-9109
    • Benton, P.M.C.1    Laryukhin, M.2    Mayer, S.M.3    Hoffman, B.M.4    Dean, D.R.5    Seefeldt, L.C.6
  • 45
    • 0018805367 scopus 로고
    • Iron-sulfur clusters in the molybdenum-iron protein component of nitrogenase. Electron paramagnetic resonance of the carbon monoxide inhibited state
    • Davis, L. C., Henzl, M. T., Burris, R. H., and Orme-Johnson, W. H. (1979) Iron-sulfur clusters in the molybdenum-iron protein component of nitrogenase. Electron paramagnetic resonance of the carbon monoxide inhibited state, Biochemistry 18, 4860-4869.
    • (1979) Biochemistry , vol.18 , pp. 4860-4869
    • Davis, L.C.1    Henzl, M.T.2    Burris, R.H.3    Orme-Johnson, W.H.4
  • 47
    • 0033552236 scopus 로고    scopus 로고
    • Detection of a new radical and FeMo-cofactor EPR signal during acetylene reduction by the α-HI95Q mutant of nitrogenase
    • Sørlie, M., Christiansen, J., Dean, D. R., and Hales, B. J. (1999) Detection of a new radical and FeMo-cofactor EPR signal during acetylene reduction by the α-HI95Q mutant of nitrogenase, J. Am. Chem. Soc. 121, 9457-9458.
    • (1999) J. Am. Chem. Soc , vol.121 , pp. 9457-9458
    • Sørlie, M.1    Christiansen, J.2    Dean, D.R.3    Hales, B.J.4
  • 49
    • 27544492629 scopus 로고    scopus 로고
    • 2, J. Am. Chem. Soc. 127, 14960-14961.
    • 2, J. Am. Chem. Soc. 127, 14960-14961.
  • 50
    • 0015429312 scopus 로고
    • Nitrogenase of Klebsiella pneumoniae: Electron-paramagnetic-resonance studies on the catalytic mechanism
    • Smith, B. E., Lowe, D. J., and Bray, R. C. (1972) Nitrogenase of Klebsiella pneumoniae: Electron-paramagnetic-resonance studies on the catalytic mechanism, Biochem. J. 130, 641-643.
    • (1972) Biochem. J , vol.130 , pp. 641-643
    • Smith, B.E.1    Lowe, D.J.2    Bray, R.C.3
  • 51
    • 0015893751 scopus 로고
    • Studies by electron paramagnetic resonance on the catalytic mechanism of nitrogenase of Klebsiella pneumoniae
    • Smith, B. E., Lowe, D. J., and Bray, R. C. (1973) Studies by electron paramagnetic resonance on the catalytic mechanism of nitrogenase of Klebsiella pneumoniae, Biochem. J. 135, 331-341.
    • (1973) Biochem. J , vol.135 , pp. 331-341
    • Smith, B.E.1    Lowe, D.J.2    Bray, R.C.3
  • 52
    • 0028944336 scopus 로고
    • Role of the MoFe protein alpha-subunit histidine-195 residue in FeMo-cofactor binding and nitrogenase catalysis
    • Kim, C. H., Newton, W. E., and Dean, D. R. (1995) Role of the MoFe protein alpha-subunit histidine-195 residue in FeMo-cofactor binding and nitrogenase catalysis, Biochemistry 34, 2798-2808.
    • (1995) Biochemistry , vol.34 , pp. 2798-2808
    • Kim, C.H.1    Newton, W.E.2    Dean, D.R.3
  • 53
    • 0034687761 scopus 로고    scopus 로고
    • 2 binding and reduction, HD formation, and azide reduction with alpha-195His- and alpha-191Gln-substituted MoFe proteins of Azotobacter vinelandii nitrogenase
    • 2 binding and reduction, HD formation, and azide reduction with alpha-195His- and alpha-191Gln-substituted MoFe proteins of Azotobacter vinelandii nitrogenase, Biochemistry 39, 15570-15577.
    • (2000) Biochemistry , vol.39 , pp. 15570-15577
    • Fisher, K.1    Dilworth, M.J.2    Newton, W.E.3
  • 54
    • 0036026573 scopus 로고    scopus 로고
    • Reduction of short chain alkynes by a nitrogenase alpha-70Ala-substituted MoFe protein
    • Mayer, S. M., Niehaus, W. G., and Dean, D. R. (2002) Reduction of short chain alkynes by a nitrogenase alpha-70Ala-substituted MoFe protein, J. Chem. Soc., Dalton Trans. 5, 802-807.
    • (2002) J. Chem. Soc., Dalton Trans , vol.5 , pp. 802-807
    • Mayer, S.M.1    Niehaus, W.G.2    Dean, D.R.3
  • 55
    • 0023046623 scopus 로고
    • 2O as a substrate and as a competitive inhibitor of nitrogenase
    • 2O as a substrate and as a competitive inhibitor of nitrogenase, Biochemistry 25, 1083-1088.
    • (1986) Biochemistry , vol.25 , pp. 1083-1088
    • Jensen, B.B.1    Burris, R.H.2
  • 56
    • 0021757851 scopus 로고
    • A nitrogen pressure of 50 atmoshperes does not prevent evolution of hydrogen by nitrogenase
    • Simpson, F. B., and Burris, R. H. (1984) A nitrogen pressure of 50 atmoshperes does not prevent evolution of hydrogen by nitrogenase, Science 224, 1095-1097.
    • (1984) Science , vol.224 , pp. 1095-1097
    • Simpson, F.B.1    Burris, R.H.2
  • 57
    • 0021102426 scopus 로고
    • 2 on HD formation by various nitrogenases
    • 2 on HD formation by various nitrogenases, Biochemistry 22, 4472-4480.
    • (1983) Biochemistry , vol.22 , pp. 4472-4480
    • Li, J.1    Burris, R.H.2
  • 58
    • 4644322013 scopus 로고    scopus 로고
    • The mechanism of nitrogenase. Computed details of the site and geometry of binding of alkyne and alkene substrates and intermediates
    • Dance, I. (2004) The mechanism of nitrogenase. Computed details of the site and geometry of binding of alkyne and alkene substrates and intermediates, J. Am. Chem. Soc. 126, 11852-11863.
    • (2004) J. Am. Chem. Soc , vol.126 , pp. 11852-11863
    • Dance, I.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.