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Volumn 269, Issue 24, 2002, Pages 6101-6111

The membrane-bound [NiFe]-hydrogenase (Ech) from Methanosarcina barkeri: Unusual properties of the iron-sulphur clusters

Author keywords

Ech; Hydrogenase; Iron sulphur; pH dependence; Redox properties

Indexed keywords

HYDROGENASE; IRON SULFUR PROTEIN;

EID: 18744408736     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2002.03328.x     Document Type: Article
Times cited : (24)

References (50)
  • 1
    • 0021194792 scopus 로고
    • The physical and catalytic properties of hydrogenase II of Clostridium pasteurianum. A comparison with hydrogenase I
    • Adams, M.W.W. & Mortenson, L.E. (1984) The physical and catalytic properties of hydrogenase II of Clostridium pasteurianum. A comparison with hydrogenase I. J. Biol. Chem. 259, 7045-7055.
    • (1984) J. Biol. Chem. , vol.259 , pp. 7045-7055
    • Adams, M.W.W.1    Mortenson, L.E.2
  • 2
    • 0025000128 scopus 로고
    • The structure and mechanism of iron-hydrogenases
    • Adams, M.W.W. (1990) The structure and mechanism of iron-hydrogenases. Biochim. Biophys. Acta 1020, 115-145.
    • (1990) Biochim. Biophys. Acta , vol.1020 , pp. 115-145
    • Adams, M.W.W.1
  • 3
    • 0034886919 scopus 로고    scopus 로고
    • Classification and phylogeny of hydrogenases
    • Vignais, P.M., Billoud, B. & Meyer, J. (2001) Classification and phylogeny of hydrogenases. FEMS Microb. Rev. 25, 455-501.
    • (2001) FEMS Microb. Rev. , vol.25 , pp. 455-501
    • Vignais, P.M.1    Billoud, B.2    Meyer, J.3
  • 5
    • 0028568063 scopus 로고
    • Nickel hydrogenases: In search of the active site
    • Albracht, S.P.J. (1994) Nickel hydrogenases: In search of the active site. Biochim. Biophys. Acta 1188, 167-204.
    • (1994) Biochim. Biophys. Acta , vol.1188 , pp. 167-204
    • Albracht, S.P.J.1
  • 6
    • 0035340936 scopus 로고    scopus 로고
    • Maturation of the [NiFe] hydrogenases
    • Casalot, L. & Rousset, M. (2001) Maturation of the [NiFe] hydrogenases. Trends. Microbiol. 9, 228-237.
    • (2001) Trends. Microbiol. , vol.9 , pp. 228-237
    • Casalot, L.1    Rousset, M.2
  • 9
    • 0029869181 scopus 로고    scopus 로고
    • 10 - Methylenetetrahydromethanopterin dehydrogenase from Methanococcus thermolithotrophicus
    • 10 - Methylenetetrahydromethanopterin dehydrogenase from Methanococcus thermolithotrophicus. Arch. Microbiol. 165, 187-193.
    • (1996) Arch. Microbiol. , vol.165 , pp. 187-193
    • Hartmann, G.C.1    Klein, A.R.2    Linder, M.3    Thauer, R.K.4
  • 10
    • 0034711484 scopus 로고    scopus 로고
    • The metal-free hydrogenase from methanogenic archaea: Evidence for a bound cofactor
    • Buurman, G., Shima, S. & Thauer, R.K. (2000) The metal-free hydrogenase from methanogenic archaea: Evidence for a bound cofactor. FEBS Lett. 485, 200-204.
    • (2000) FEBS Lett. , vol.485 , pp. 200-204
    • Buurman, G.1    Shima, S.2    Thauer, R.K.3
  • 11
    • 0035478121 scopus 로고    scopus 로고
    • Activation of dihydrogen without transition metals
    • Berkessel, A. (2001) Activation of dihydrogen without transition metals. Curr. Opin. Chem. Biol. 5, 486-490.
    • (2001) Curr. Opin. Chem. Biol. , vol.5 , pp. 486-490
    • Berkessel, A.1
  • 12
    • 0031685510 scopus 로고    scopus 로고
    • Biochemistry of methanogenesis: A tribute to Marjory Stephenson
    • Thauer, R.K. (1998) Biochemistry of methanogenesis: A tribute to Marjory Stephenson. Microbiology 144, 2377-2406.
    • (1998) Microbiology , vol.144 , pp. 2377-2406
    • Thauer, R.K.1
  • 13
    • 0021720861 scopus 로고
    • Coenzymes of methanogenesis from hydrogen and carbon dioxide
    • Keltjens, J.T. (1984) Coenzymes of methanogenesis from hydrogen and carbon dioxide. Antonie Van Leeuwenhoek 50, 383-396.
    • (1984) Antonie Van Leeuwenhoek , vol.50 , pp. 383-396
    • Keltjens, J.T.1
  • 14
    • 0032521598 scopus 로고    scopus 로고
    • An Escherichia coli hydrogenase-3-type hydrogenase in metha-nogenic archaea
    • Kunkel, A., Vorholt, J.A., Thauer, R.K. & Hedderich, R. (1998) An Escherichia coli hydrogenase-3-type hydrogenase in methanogenic archaea. Eur. J. Biochem. 252, 467-476.
    • (1998) Eur. J. Biochem. , vol.252 , pp. 467-476
    • Kunkel, A.1    Vorholt, J.A.2    Thauer, R.K.3    Hedderich, R.4
  • 15
    • 0025157053 scopus 로고
    • Nucleotide sequence and expression of an operon in Escherichia coli coding for formate hydrogenlyase components
    • Böhm, R., Sauter, M. & Böck, A. (1990) Nucleotide sequence and expression of an operon in Escherichia coli coding for formate hydrogenlyase components. Mol. Microbiol. 4, 231-243.
    • (1990) Mol. Microbiol. , vol.4 , pp. 231-243
    • Böhm, R.1    Sauter, M.2    Böck, A.3
  • 16
    • 10344238576 scopus 로고    scopus 로고
    • Characterization of the region encoding the CO-induced hydrogenase of Rhodospirillum rubrum
    • Fox, J.D., He, Y., Shelver, D., Roberts, G.P. & Ludden, P.W. (1996) Characterization of the region encoding the CO-induced hydrogenase of Rhodospirillum rubrum. J. Bacteriol. 178, 6200-6208.
    • (1996) J. Bacteriol. , vol.178 , pp. 6200-6208
    • Fox, J.D.1    He, Y.2    Shelver, D.3    Roberts, G.P.4    Ludden, P.W.5
  • 17
    • 0029915837 scopus 로고    scopus 로고
    • Characterization of the CO-induced, CO-tolerant hydrogenase from Rhodospirillum rubrum and the gene encoding the large subunit of the enzyme
    • Fox, J.D., Kerby, R.L., Roberts, G.P. & Ludden, P.W. (1996) Characterization of the CO-induced, CO-tolerant hydrogenase from Rhodospirillum rubrum and the gene encoding the large subunit of the enzyme. J. Bacteriol. 178, 1515-1524.
    • (1996) J. Bacteriol. , vol.178 , pp. 1515-1524
    • Fox, J.D.1    Kerby, R.L.2    Roberts, G.P.3    Ludden, P.W.4
  • 18
    • 0033214609 scopus 로고    scopus 로고
    • Purification and catalytic properties of Ech hydrogenase from Methanosarcina barkeri
    • Meuer, J., Bartoschek, S., Koch, J., Kunkel, A. & Hedderich, R. (1999) Purification and catalytic properties of Ech hydrogenase from Methanosarcina barkeri. Eur. J. Biochem. 265, 325-335.
    • (1999) Eur. J. Biochem. , vol.265 , pp. 325-335
    • Meuer, J.1    Bartoschek, S.2    Koch, J.3    Kunkel, A.4    Hedderich, R.5
  • 20
    • 0037117505 scopus 로고    scopus 로고
    • Genetic analysis of the archaeon Methanosarcina barkeri Fusaro reveals a central role for Ech hydrogenase and ferredoxin in methanogenesis and carbon fixation
    • Meuer, J., Kuettner, H.C., Zhang, J.K., Hedderich, R. & Metcalf, W.W. (2002) Genetic analysis of the archaeon Methanosarcina barkeri Fusaro reveals a central role for Ech hydrogenase and ferredoxin in methanogenesis and carbon fixation. Proc. Natl Acad. Sci. USA 99, 5632-5637.
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 5632-5637
    • Meuer, J.1    Kuettner, H.C.2    Zhang, J.K.3    Hedderich, R.4    Metcalf, W.W.5
  • 21
    • 0031027369 scopus 로고    scopus 로고
    • Bovine-heart NADH: Ubiquinone oxidoreductase is a monomer with 8 Fe-S clusters and 2 FMN groups
    • Albracht, S.P.J., Mariette, A. & de Jong, P. (1997) Bovine-heart NADH: Ubiquinone oxidoreductase is a monomer with 8 Fe-S clusters and 2 FMN groups. Biochim. Biophys. Acta 1318, 92-106.
    • (1997) Biochim. Biophys. Acta , vol.1318 , pp. 92-106
    • Albracht, S.P.J.1    Mariette, A.2    De Jong, P.3
  • 22
    • 0019324533 scopus 로고
    • An analysis of some thermodynamic properties of iron-sulphur centres in site I of mitochondria
    • Ingledew, W.J. & Ohnishi, T. (1980) An analysis of some thermodynamic properties of iron-sulphur centres in site I of mitochondria. Biochem. J. 186, 111-117.
    • (1980) Biochem. J. , vol.186 , pp. 111-117
    • Ingledew, W.J.1    Ohnishi, T.2
  • 23
    • 0034680865 scopus 로고    scopus 로고
    • Learning from hydrogenases: Location of a proton pump and of a second FMN in bovine NADH-ubiquinone oxidoreductase (Complex I)
    • Albracht, S.P.J. & Hedderich, R. (2000) Learning from hydrogenases: Location of a proton pump and of a second FMN in bovine NADH-ubiquinone oxidoreductase (Complex I). FEBS Lett. 485, 1-6.
    • (2000) FEBS Lett. , vol.485 , pp. 1-6
    • Albracht, S.P.J.1    Hedderich, R.2
  • 24
    • 0025045750 scopus 로고
    • Ferredoxin-dependent methane formation from acetate in cell extracts of Methanosarcina barkeri (strain MS)
    • Fischer, R. & Thauer, R.K. (1990) Ferredoxin-dependent methane formation from acetate in cell extracts of Methanosarcina barkeri (strain MS). FEBS Lett. 269, 368-372.
    • (1990) FEBS Lett. , vol.269 , pp. 368-372
    • Fischer, R.1    Thauer, R.K.2
  • 25
    • 0015220486 scopus 로고
    • Oxidation-reduction potential dependence of the interaction of cytochromes, bacteriochlorophyll and carotenoids at 77 degrees K in chromatophores of Chromatium D and Rhodopseudomonas gelatinosa
    • Dutton, P.L. (1971) Oxidation-reduction potential dependence of the interaction of cytochromes, bacteriochlorophyll and carotenoids at 77 degrees K in chromatophores of Chromatium D and Rhodopseudomonas gelatinosa. Biochim. Biophys. Acta 226, 63-80.
    • (1971) Biochim. Biophys. Acta , vol.226 , pp. 63-80
    • Dutton, P.L.1
  • 28
    • 0020494651 scopus 로고
    • New insights, ideas and unanswered questions concerning iron-sulfur clusters in mitochondria
    • Beinert, H. & Albracht, S.P.J. (1982) New insights, ideas and unanswered questions concerning iron-sulfur clusters in mitochondria. Biochim. Biophys. Acta 683, 245-277.
    • (1982) Biochim. Biophys. Acta , vol.683 , pp. 245-277
    • Beinert, H.1    Albracht, S.P.J.2
  • 29
    • 85012573469 scopus 로고
    • Applications of electron paramagnetic resonance in the study of iron-sulfur clusters in energy-transducing membranes
    • Academic Press, New York, USA
    • Albracht, S.P.J. (1984) Applications of electron paramagnetic resonance in the study of iron-sulfur clusters in energy-transducing membranes. Current Topics in Bioenergetics, pp. 79-106. Academic Press, New York, USA.
    • (1984) Current Topics in Bioenergetics , pp. 79-106
    • Albracht, S.P.J.1
  • 30
    • 49649145902 scopus 로고
    • EPR signal intensity and powder shapes: A reexamination
    • Aasa, R. & Vänngård, T. (1975) EPR signal intensity and powder shapes: A reexamination. J. Magn. Reson. 19, 308-315.
    • (1975) J. Magn. Reson. , vol.19 , pp. 308-315
    • Aasa, R.1    Vänngård, T.2
  • 31
    • 0023958731 scopus 로고
    • Purification and some properties of the corrinoid-containing membrane protein from Methanobacterium thermoautotrophicum
    • Schulz, H., Albracht, S.P.J., Coremans, J.M.C.C. & Fuchs, G. (1988) Purification and some properties of the corrinoid-containing membrane protein from Methanobacterium thermoautotrophicum. Eur. J. Biochem. 171, 589-597.
    • (1988) Eur. J. Biochem. , vol.171 , pp. 589-597
    • Schulz, H.1    Albracht, S.P.J.2    Coremans, J.M.C.C.3    Fuchs, G.4
  • 32
    • 0020486176 scopus 로고
    • Analysis of strain-induced EPR-line shapes and anisotropic spin-lattice relaxation in a [2Fe-2S] ferredoxin
    • Hagen, W.R. & Albracht, S.P.J. (1982) Analysis of strain-induced EPR-line shapes and anisotropic spin-lattice relaxation in a [2Fe-2S] ferredoxin. Biochim. Biophys. Acta 702, 61-71.
    • (1982) Biochim. Biophys. Acta , vol.702 , pp. 61-71
    • Hagen, W.R.1    Albracht, S.P.J.2
  • 33
    • 0032490089 scopus 로고    scopus 로고
    • Iron-sulfur clusters/semiquinones in complex I
    • Ohnishi, T. (1998) Iron-sulfur clusters/semiquinones in complex I. Biochim. Biophys. Acta 1364, 186-206.
    • (1998) Biochim. Biophys. Acta , vol.1364 , pp. 186-206
    • Ohnishi, T.1
  • 34
    • 0022420292 scopus 로고
    • Monovalent nickel in hydrogenase from Chromatium vinosum. Light sensitivity and evidence for direct interaction with hydrogen
    • van der Zwaan, J.W., Albracht, S.P.J., Fontijn, R.D. & Slater, E.C. (1985) Monovalent nickel in hydrogenase from Chromatium vinosum. Light sensitivity and evidence for direct interaction with hydrogen. FEBS Lett. 179, 271-277.
    • (1985) FEBS Lett. , vol.179 , pp. 271-277
    • Van der Zwaan, J.W.1    Albracht, S.P.J.2    Fontijn, R.D.3    Slater, E.C.4
  • 35
    • 0021826804 scopus 로고
    • Electron paramagnetic resonance studies on the mechanism of activation and the catalytic cycle of the nickel-containing hydrogenase from Desulfovibrio gigas
    • Teixeira, M., Moura, I., Xavier, A.V., Huynh, B.H., Der Vartanian, D.V., Peck, H.D. Jr, Le Gall, J. & Moura, J.J. (1985) Electron paramagnetic resonance studies on the mechanism of activation and the catalytic cycle of the nickel-containing hydrogenase from Desulfovibrio gigas. J. Biol. Chem. 260, 8942-8950.
    • (1985) J. Biol. Chem. , vol.260 , pp. 8942-8950
    • Teixeira, M.1    Moura, I.2    Xavier, A.V.3    Huynh, B.H.4    Der Vartanian, D.V.5    Peck H.D., Jr.6    Le Gall, J.7    Moura, J.J.8
  • 36
    • 0022071390 scopus 로고
    • Electron-spin-resonance/electron-paramagnetic-resonance spectroscopy of iron-sulphur enzymes
    • Cammack, R., Patil, D.S. & Fernandez, V.M. (1985) Electron-spin-resonance/electron-paramagnetic-resonance spectroscopy of iron-sulphur enzymes. Biochem. Soc. Trans. 13, 572-578.
    • (1985) Biochem. Soc. Trans. , vol.13 , pp. 572-578
    • Cammack, R.1    Patil, D.S.2    Fernandez, V.M.3
  • 37
    • 0023504946 scopus 로고
    • On the anomalous temperature behaviour of the EPR signal of monovalent nickel in hydrogenase
    • Van der Zwaan, J.W., Albracht, S.P.J., Fontijn, R.D. & Mul, P. (1987) On the anomalous temperature behaviour of the EPR signal of monovalent nickel in hydrogenase. Eur. J. Biochem. 169, 377-384.
    • (1987) Eur. J. Biochem. , vol.169 , pp. 377-384
    • Van der Zwaan, J.W.1    Albracht, S.P.J.2    Fontijn, R.D.3    Mul, P.4
  • 38
    • 0034858150 scopus 로고    scopus 로고
    • A paramagnetic species with unique EPR characteristics in the active site of heterodisulfide reductase from methanogenic archaea
    • Madadi-Kahkesh, S., Duin, E.C., Heim, S., Albracht, S.P.J., Johnson, M.K. & Hedderich, R. (2001) A paramagnetic species with unique EPR characteristics in the active site of heterodisulfide reductase from methanogenic archaea. Eur. J. Biochem. 268, 2566-2577.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 2566-2577
    • Madadi-Kahkesh, S.1    Duin, E.C.2    Heim, S.3    Albracht, S.P.J.4    Johnson, M.K.5    Hedderich, R.6
  • 39
    • 0033555715 scopus 로고    scopus 로고
    • Inhibition of membrane-bound electron transport of the methanogenic archaeon Methanosarcina mazei Go1 by diphenyleneiodonium
    • Brodersen, J., Baumer, S., Abken, H.J., Gottschalk, G. & Deppenmeier, U. (1999) Inhibition of membrane-bound electron transport of the methanogenic archaeon Methanosarcina mazei Go1 by diphenyleneiodonium. Eur. J. Biochem. 259, 218-224.
    • (1999) Eur. J. Biochem. , vol.259 , pp. 218-224
    • Brodersen, J.1    Baumer, S.2    Abken, H.J.3    Gottschalk, G.4    Deppenmeier, U.5
  • 40
    • 0028890441 scopus 로고
    • Analysis of the vhoGAC and vhtGAC operons from Methanosarcina mazei strain Gö1, both encoding a membrane-bound hydrogenase and a cytochrome b
    • Deppenmeier, U., Blaut, M., Lentes, S., Herzberg, C. & Gottschalk, G. (1995) Analysis of the vhoGAC and vhtGAC operons from Methanosarcina mazei strain Gö1, both encoding a membrane-bound hydrogenase and a cytochrome b. Eur. J. Biochem. 227, 261-269.
    • (1995) Eur. J. Biochem. , vol.227 , pp. 261-269
    • Deppenmeier, U.1    Blaut, M.2    Lentes, S.3    Herzberg, C.4    Gottschalk, G.5
  • 41
    • 0026588473 scopus 로고
    • Distinct redox behaviour of prosthetic groups in ready and unready hydrogenase from Chromatium vinosum
    • Coremans, J.M.C.C., van der Zwaan, J.W. & Albracht, S.P.J. (1992) Distinct redox behaviour of prosthetic groups in ready and unready hydrogenase from Chromatium vinosum. Biochim. Biophys. Acta 1119, 157-168.
    • (1992) Biochim. Biophys. Acta , vol.1119 , pp. 157-168
    • Coremans, J.M.C.C.1    Van der Zwaan, J.W.2    Albracht, S.P.J.3
  • 43
    • 0025857741 scopus 로고
    • Electron spin echo envelope modulation spectroscopy supports the suggested coordination of two histidine ligands to the Rieske Fe-S centers of the cytochrome b6f complex of spinach and the cytochrome bc1 complexes of Rhodospirillum rubrum, Rhodobacter sphaeroides R.-26, and bovine heart mitochondria
    • Britt, R.D., Sauer, K., Klein, M.P., Knaff, D.B., Kriauciunas, A., Yu & C.A., Yu, L. & Malkin, R. (1991) Electron spin echo envelope modulation spectroscopy supports the suggested coordination of two histidine ligands to the Rieske Fe-S centers of the cytochrome b6f complex of spinach and the cytochrome bc1 complexes of Rhodospirillum rubrum, Rhodobacter sphaero-ides R.-26, and bovine heart mitochondria. Biochemistry 30, 1892-1901.
    • (1991) Biochemistry , vol.30 , pp. 1892-1901
    • Britt, R.D.1    Sauer, K.2    Klein, M.P.3    Knaff, D.B.4    Kriauciunas, A.5    Yu, C.A.6    Yu, L.7    Malkin, R.8
  • 44
    • 0029962504 scopus 로고    scopus 로고
    • Characterization and crystallization of the lumen side domain of the chloroplast Rieske iron-sulfur protein
    • Zhang, H., Carrell, C.J., Huang, D., Sled, V., Ohnishi, T., Smith, J.L. & Cramer, W.A. (1996) Characterization and crystallization of the lumen side domain of the chloroplast Rieske iron-sulfur protein. J. Biol. Chem. 271, 31360-31366.
    • (1996) J. Biol. Chem. , vol.271 , pp. 31360-31366
    • Zhang, H.1    Carrell, C.J.2    Huang, D.3    Sled, V.4    Ohnishi, T.5    Smith, J.L.6    Cramer, W.A.7
  • 45
    • 0025323166 scopus 로고
    • Spectroscopic characterization of the novel iron-sulfur cluster in Pyrococcus furiosus ferredoxin
    • Conover, R.C., Kowal, A.T., Fu, W.G., Park, J.B., Aono, S., Adams, M.W.W. & Johnson, M.K. (1990) Spectroscopic characterization of the novel iron-sulfur cluster in Pyrococcus furiosus ferredoxin. J. Biol. Chem. 265, 8533-8541.
    • (1990) J. Biol. Chem. , vol.265 , pp. 8533-8541
    • Conover, R.C.1    Kowal, A.T.2    Fu, W.G.3    Park, J.B.4    Aono, S.5    Adams, M.W.W.6    Johnson, M.K.7
  • 46
    • 0032547089 scopus 로고    scopus 로고
    • The two [4Fe-4S] clusters in Chromatium vinosum ferredoxin have largely different reduction potentials. Structural origin and functional consequences
    • Kyritsis, P., Hatzfeld, O.M., Link, T.A. & Moulis, J.M. (1998) The two [4Fe-4S] clusters in Chromatium vinosum ferredoxin have largely different reduction potentials. Structural origin and functional consequences. J. Biol. Chem. 273, 15404-15411.
    • (1998) J. Biol. Chem. , vol.273 , pp. 15404-15411
    • Kyritsis, P.1    Hatzfeld, O.M.2    Link, T.A.3    Moulis, J.M.4
  • 47
    • 0025854234 scopus 로고
    • A homologue of a nuclear-coded iron-sulfur protein subunit of bovine mitochondrial complex I is encoded in chloroplast genomes
    • Dupuis, A., Skehel, J.M. & Walker, J.E. (1991) A homologue of a nuclear-coded iron-sulfur protein subunit of bovine mitochondrial complex I is encoded in chloroplast genomes. Biochemistry 30, 2954-2960.
    • (1991) Biochemistry , vol.30 , pp. 2954-2960
    • Dupuis, A.1    Skehel, J.M.2    Walker, J.E.3
  • 49
    • 0035968167 scopus 로고    scopus 로고
    • A central functional role for the 49-kDa subunit within the catalytic core of mitochondrial Complex I
    • Kashani-Poor, N., Zwicker, K., Kerscher, S. & Brandt, U. (2001) A central functional role for the 49-kDa subunit within the catalytic core of mitochondrial Complex I. J. Biol. Chem 276, 24082-24087.
    • (2001) J. Biol. Chem. , vol.276 , pp. 24082-24087
    • Kashani-Poor, N.1    Zwicker, K.2    Kerscher, S.3    Brandt, U.4
  • 50
    • 0037096980 scopus 로고    scopus 로고
    • Disruption of iron-sulphur cluster N2 from NADH: Ubiquinone oxidoreductase by site-directed mutagenesis
    • Duarte, M., Populo, H., Videira, A., Friedrich, T. & Schulte, U. (2002) Disruption of iron-sulphur cluster N2 from NADH: Ubiquinone oxidoreductase by site-directed mutagenesis. Biochem. J. 364, 833-839.
    • (2002) Biochem. J. , vol.364 , pp. 833-839
    • Duarte, M.1    Populo, H.2    Videira, A.3    Friedrich, T.4    Schulte, U.5


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