메뉴 건너뛰기




Volumn , Issue , 2013, Pages 33-103

Electrochemistry of hydrogenases

Author keywords

[No Author keywords available]

Indexed keywords

ALGAE; AMMONIA;

EID: 85054682733     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1201/b15576     Document Type: Chapter
Times cited : (1)

References (107)
  • 1
    • 0000828805 scopus 로고
    • A hydrogen economy
    • Bockris, J.O.M. A hydrogen economy. Science, 1972, 176(4041): 1323.
    • (1972) Science , vol.176 , Issue.4041 , pp. 1323
    • Bockris, J.O.M.1
  • 3
    • 33751406977 scopus 로고    scopus 로고
    • Development of algal systems for hydrogen photoproduction: Addressing the hydrogenase oxygen-sensitivity problem
    • ed. A.F. Collings and C. Critchley, Berlin: Wiley Verlag
    • Ghirardi, M.L., et al. Development of algal systems for hydrogen photoproduction: Addressing the hydrogenase oxygen-sensitivity problem, in Artificial Photosynthesis, ed. A.F. Collings and C. Critchley. 2005, Berlin: Wiley Verlag.
    • (2005) Artificial Photosynthesis
    • Ghirardi, M.L.1
  • 4
    • 57649188186 scopus 로고    scopus 로고
    • Photobiological hydrogen-producing systems
    • Ghirardi, M.L., et al. Photobiological hydrogen-producing systems. Chemical Society Reviews, 2009, 38(1): 52-61.
    • (2009) Chemical Society Reviews , vol.38 , Issue.1 , pp. 52-61
    • Ghirardi, M.L.1
  • 5
    • 0036618091 scopus 로고    scopus 로고
    • Hydrogenases in green algae: Do they save the algae’s life and solve our energy problems?
    • Happe, T., et al. Hydrogenases in green algae: Do they save the algae’s life and solve our energy problems? Trends in Plant Science, 2002, 7(6): 246-250.
    • (2002) Trends in Plant Science , vol.7 , Issue.6 , pp. 246-250
    • Happe, T.1
  • 6
    • 67649283572 scopus 로고    scopus 로고
    • Structural and functional analogues of the active sites of the [Fe]-, [NiFe]-, and [FeFe]-hydrogenases
    • Tard, C., and C.J. Pickett. Structural and functional analogues of the active sites of the [Fe]-, [NiFe]-, and [FeFe]-hydrogenases. Chemical Reviews, 2009, 109(6): 2245-2274.
    • (2009) Chemical Reviews , vol.109 , Issue.6 , pp. 2245-2274
    • Tard, C.1    Pickett, C.J.2
  • 7
    • 57649243216 scopus 로고    scopus 로고
    • Small molecule mimics of hydrogenases: Hydrides and redox
    • Gloaguen, F., and T.B. Rauchfuss. Small molecule mimics of hydrogenases: Hydrides and redox. Chemical Society Reviews, 2009, 38(1): 100-108.
    • (2009) Chemical Society Reviews , vol.38 , Issue.1 , pp. 100-108
    • Gloaguen, F.1    Rauchfuss, T.B.2
  • 8
    • 49049115593 scopus 로고    scopus 로고
    • Direct electrochemistry of redox enzymes as a tool for mechanistic studies
    • Léger, C., and P. Bertrand. Direct electrochemistry of redox enzymes as a tool for mechanistic studies. Chemical Reviews, 2008, 108(7): 2379-2438.
    • (2008) Chemical Reviews , vol.108 , Issue.7 , pp. 2379-2438
    • Léger, C.1    Bertrand, P.2
  • 9
    • 35748933836 scopus 로고    scopus 로고
    • Investigating and exploiting the electrocatalytic properties of hydrogenases
    • Vincent, K.A., A. Parkin, and F.A. Armstrong. Investigating and exploiting the electrocatalytic properties of hydrogenases. Chemical Reviews, 2007, 107(10): 4366-4413.
    • (2007) Chemical Reviews , vol.107 , Issue.10 , pp. 4366-4413
    • Vincent, K.A.1    Parkin, A.2    Armstrong, F.A.3
  • 10
    • 57649243241 scopus 로고    scopus 로고
    • Dynamic electrochemical investigations of hydrogen oxidation and production by enzymes and implications for future technology
    • Armstrong, F.A., et al. Dynamic electrochemical investigations of hydrogen oxidation and production by enzymes and implications for future technology. Chemical Society Reviews, 2009, 38(1): 36-51.
    • (2009) Chemical Society Reviews , vol.38 , Issue.1 , pp. 36-51
    • Armstrong, F.A.1
  • 12
    • 80054971344 scopus 로고    scopus 로고
    • Oxygen-tolerant NiFe -hydrogenases: The individual and collective importance of supernumerary cysteines at the proximal Fe-S cluster
    • Lukey, M.J., et al. Oxygen-tolerant NiFe -hydrogenases: The individual and collective importance of supernumerary cysteines at the proximal Fe-S cluster. Journal of the American Chemical Society, 2011, 133(42): 16881-16892.
    • (2011) Journal of the American Chemical Society , vol.133 , Issue.42 , pp. 16881-16892
    • Lukey, M.J.1
  • 13
    • 27744466859 scopus 로고    scopus 로고
    • Hydrogen cycling by enzymes: Electrocatalysis and implications for future energy technology
    • Vincent, K.A., et al. Hydrogen cycling by enzymes: Electrocatalysis and implications for future energy technology. Dalton Transactions, 2005, 21: 3397-3403.
    • (2005) Dalton Transactions , vol.21 , pp. 3397-3403
    • Vincent, K.A.1
  • 14
    • 13844275458 scopus 로고    scopus 로고
    • Investigating metalloenzyme reactions using electrochemical sweeps and steps: Fine control and measurements with reactants ranging from ions to gases
    • Vincent, K.A., and F.A. Armstrong. Investigating metalloenzyme reactions using electrochemical sweeps and steps: Fine control and measurements with reactants ranging from ions to gases. Inorganic Chemistry, 2005, 44(4): 798-809.
    • (2005) Inorganic Chemistry , vol.44 , Issue.4 , pp. 798-809
    • Vincent, K.A.1    Armstrong, F.A.2
  • 16
    • 18744432274 scopus 로고    scopus 로고
    • Enzyme electrokinetics: Using protein film voltammetry to investigate redox enzymes and their mechanisms
    • Léger, C., et al. Enzyme electrokinetics: Using protein film voltammetry to investigate redox enzymes and their mechanisms. Biochemistry, 2003, 42(29): 8653-8662.
    • (2003) Biochemistry , vol.42 , Issue.29 , pp. 8653-8662
    • Léger, C.1
  • 17
    • 0017583880 scopus 로고
    • Bioelectrocatalysis. Hydrogenase as catalyst of electrochemical hydrogen ionization
    • Varfolomeev, S.D., et al. Bioelectrocatalysis. Hydrogenase as catalyst of electrochemical hydrogen ionization. Bioelectrochem. Bioenergetics., 1977, 4(3): 314-26.
    • (1977) Bioelectrochem. Bioenergetics. , vol.4 , Issue.3 , pp. 314-326
    • Varfolomeev, S.D.1
  • 18
    • 0030896355 scopus 로고    scopus 로고
    • Direct electrochemistry of Megasphaera elsdenii iron hydrogenase. Definition of the enzyme’s catalytic operating potential and quantitation of the catalytic behavior over a continuous potential range
    • Butt, J.N., M. Filipiak, and W.R. Hagen. Direct electrochemistry of Megasphaera elsdenii iron hydrogenase. Definition of the enzyme’s catalytic operating potential and quantitation of the catalytic behavior over a continuous potential range. European Journal of Biochemistry, 1997, 245(1): 116-122.
    • (1997) European Journal of Biochemistry , vol.245 , Issue.1 , pp. 116-122
    • Butt, J.N.1    Filipiak, M.2    Hagen, W.R.3
  • 20
    • 35748930865 scopus 로고    scopus 로고
    • Structure/function relationships of [NiFe]- and [FeFe]-hydrogenases
    • Fontecilla-Camps, J.C., et al. Structure/function relationships of [NiFe]- and [FeFe]-hydrogenases. Chemical Reviews, 2007, 107(10): 4273-4303.
    • (2007) Chemical Reviews , vol.107 , Issue.10 , pp. 4273-4303
    • Fontecilla-Camps, J.C.1
  • 21
    • 0033556301 scopus 로고    scopus 로고
    • Desulfovibrio desulfuricans iron hydrogenase: The structure shows unusual coordination to an active site Fe binuclear center
    • Nicolet, Y., et al. Desulfovibrio desulfuricans iron hydrogenase: The structure shows unusual coordination to an active site Fe binuclear center. Structure, 1999, 7(1): 13-23.
    • (1999) Structure , vol.7 , Issue.1 , pp. 13-23
    • Nicolet, Y.1
  • 22
    • 77956759468 scopus 로고    scopus 로고
    • The crystal structure of the [NiFe] hydrogenase from the photosynthetic bacterium Allochromatium vinosum: Characterization of the oxidized enzyme (Ni-A State)
    • Ogata, H., P. Kellers, and W. Lubitz. The crystal structure of the [NiFe] hydrogenase from the photosynthetic bacterium Allochromatium vinosum: Characterization of the oxidized enzyme (Ni-A State). Journal of Molecular Biology, 2010, 402(2): 428-444.
    • (2010) Journal of Molecular Biology , vol.402 , Issue.2 , pp. 428-444
    • Ogata, H.1    Kellers, P.2    Lubitz, W.3
  • 23
    • 0033556301 scopus 로고    scopus 로고
    • Desulfovibrio desulfuricans iron hydrogenase: The structure shows unusual coordination to an active site Fe binuclear center
    • Nicolet, Y., et al. Desulfovibrio desulfuricans iron hydrogenase: The structure shows unusual coordination to an active site Fe binuclear center. Structure with Folding and Design, 1999, 7(1): 13-23.
    • (1999) Structure with Folding and Design , vol.7 , Issue.1 , pp. 13-23
    • Nicolet, Y.1
  • 24
    • 0032483966 scopus 로고    scopus 로고
    • X-ray crystal structure of the Fe-only hydrogenase (Cpl) from Clostridium pasteurianum to 1.8 angstrom resolution
    • Peters, J.W., et al. X-ray crystal structure of the Fe-only hydrogenase (Cpl) from Clostridium pasteurianum to 1.8 angstrom resolution. Science, 1998, 282: 1853-1858.
    • (1998) Science , vol.282 , pp. 1853-1858
    • Peters, J.W.1
  • 25
    • 0037149937 scopus 로고    scopus 로고
    • Direct comparison of the electrocatalytic oxidation of hydrogen by an enzyme and a platinum catalyst
    • Jones, A.K., et al. Direct comparison of the electrocatalytic oxidation of hydrogen by an enzyme and a platinum catalyst. Chemical Communications, 2002, 866-867.
    • (2002) Chemical Communications , pp. 866-867
    • Jones, A.K.1
  • 26
    • 14644423964 scopus 로고    scopus 로고
    • Hydrogenase electrodes for fuel cells
    • Karyakin, A.A., et al. Hydrogenase electrodes for fuel cells. Biochemical Society of Transactions, 2005, 33(1): 73-75.
    • (2005) Biochemical Society of Transactions , vol.33 , Issue.1 , pp. 73-75
    • Karyakin, A.A.1
  • 27
    • 39049132264 scopus 로고    scopus 로고
    • [FeFe]-Hydrogenase-catalyzed H2 production in a photoelectrochemical biofuel cell
    • Hambourger, M., et al. [FeFe]-Hydrogenase-catalyzed H2 production in a photoelectrochemical biofuel cell. Journal of the American Chemical Society, 2008, 130(6): 2015-2022.
    • (2008) Journal of the American Chemical Society , vol.130 , Issue.6 , pp. 2015-2022
    • Hambourger, M.1
  • 28
    • 0033551444 scopus 로고    scopus 로고
    • 2 value
    • 2 value. Biochemistry, 1999, 38(28): 8992-8999.
    • (1999) Biochemistry , vol.38 , Issue.28 , pp. 8992-8999
    • Pershad, H.R.1
  • 29
    • 80051636877 scopus 로고    scopus 로고
    • A synthetic nickel electrocatalyst with a turnover frequency above 100,000 s(-1) for H(2) production
    • Helm, M.L., et al. A synthetic nickel electrocatalyst with a turnover frequency above 100,000 s(-1) for H(2) production. Science, 2011, 333(6044): 863-866.
    • (2011) Science , vol.333 , Issue.6044 , pp. 863-866
    • Helm, M.L.1
  • 30
    • 80052565457 scopus 로고    scopus 로고
    • Moving protons with pendant amines: Proton mobility in a nickel catalyst for oxidation of hydrogen
    • O’Hagan, M., et al. Moving protons with pendant amines: Proton mobility in a nickel catalyst for oxidation of hydrogen. Journal of the American Chemical Society, 2011, 133(36): 14301-14312.
    • (2011) Journal of the American Chemical Society , vol.133 , Issue.36 , pp. 14301-14312
    • O’Hagan, M.1
  • 31
    • 35848964033 scopus 로고    scopus 로고
    • Fundamentals of H2 binding and reactivity on transition metals underlying hydrogenase function and H2 production and storage
    • Kubas, G.J. Fundamentals of H2 binding and reactivity on transition metals underlying hydrogenase function and H2 production and storage. Chemical Reviews, 2007, 107(10): 4152-4205.
    • (2007) Chemical Reviews , vol.107 , Issue.10 , pp. 4152-4205
    • Kubas, G.J.1
  • 33
    • 50249104385 scopus 로고    scopus 로고
    • Hydrogen production under aerobic conditions by membrane-bound hydrogenases from Ralstonia species
    • Goldet, G., et al. Hydrogen production under aerobic conditions by membrane-bound hydrogenases from Ralstonia species. Journal of the American Chemical Society, 2008, 130(33): 11106-11113.
    • (2008) Journal of the American Chemical Society , vol.130 , Issue.33 , pp. 11106-11113
    • Goldet, G.1
  • 34
    • 29844441433 scopus 로고    scopus 로고
    • Electrochemical definitions of O2 sensitivity and oxidative inactivation in hydrogenases
    • Vincent, K.A., et al. Electrochemical definitions of O2 sensitivity and oxidative inactivation in hydrogenases. Journal of the American Chemical Society, 2005, 127(51): 18179-18189.
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.51 , pp. 18179-18189
    • Vincent, K.A.1
  • 35
    • 77950503486 scopus 로고    scopus 로고
    • How Escherichia coli is equipped to oxidize hydrogen under different redox conditions
    • Lukey, M.J., et al. How Escherichia coli is equipped to oxidize hydrogen under different redox conditions. Journal of Biological Chemistry, 2010, 285(6): 3928-3938.
    • (2010) Journal of Biological Chemistry , vol.285 , Issue.6 , pp. 3928-3938
    • Lukey, M.J.1
  • 36
    • 79951841772 scopus 로고    scopus 로고
    • CO disrupts the reduced H-cluster of FeFe hydrogenase. A combined DFT and protein film voltammetry study
    • Baffert, C., et al. CO disrupts the reduced H-cluster of FeFe hydrogenase. A combined DFT and protein film voltammetry study. Journal of the American Chemical Society, 2011, 133(7): 2096-2099.
    • (2011) Journal of the American Chemical Society , vol.133 , Issue.7 , pp. 2096-2099
    • Baffert, C.1
  • 37
    • 33745015520 scopus 로고    scopus 로고
    • Rapid and reversible reactions of [NiFe]-hydrogenases with sulfide
    • Vincent, K.A., et al. Rapid and reversible reactions of [NiFe]-hydrogenases with sulfide. Journal of the American Chemical Society, 2006, 128(23): 7448-7449.
    • (2006) Journal of the American Chemical Society , vol.128 , Issue.23 , pp. 7448-7449
    • Vincent, K.A.1
  • 38
    • 79551702166 scopus 로고    scopus 로고
    • Formaldehyde-A rapid and reversible inhibitor of hydrogen production by FeFe-hydrogenases
    • Wait, A.F., et al. Formaldehyde-A rapid and reversible inhibitor of hydrogen production by FeFe-hydrogenases. Journal of the American Chemical Society, 2011, 133(5): 1282-1285.
    • (2011) Journal of the American Chemical Society , vol.133 , Issue.5 , pp. 1282-1285
    • Wait, A.F.1
  • 39
    • 84860806395 scopus 로고    scopus 로고
    • Inhibition of FeFe-hydrogenases by formaldehyde and wider mechanistic implications for biohydrogen activation
    • Foster, C.E., et al. Inhibition of FeFe-hydrogenases by formaldehyde and wider mechanistic implications for biohydrogen activation. Journal of the American Chemical Society, 2012, 134(17): 7553-7557.
    • (2012) Journal of the American Chemical Society , vol.134 , Issue.17 , pp. 7553-7557
    • Foster, C.E.1
  • 40
    • 35048826863 scopus 로고    scopus 로고
    • [NiFe] and [FeFe] hydrogenases studied by advanced magnetic resonance techniques
    • Lubitz, W., E. Reijerse, and M. van Gastel. [NiFe] and [FeFe] hydrogenases studied by advanced magnetic resonance techniques. Chemical Reviews, 2007, 107(10): 4331-4365.
    • (2007) Chemical Reviews , vol.107 , Issue.10 , pp. 4331-4365
    • Lubitz, W.1    Reijerse, E.2    van Gastel, M.3
  • 41
    • 77649271875 scopus 로고    scopus 로고
    • The three-dimensional structure of NiFeSe hydrogenase from Desulfovibrio vulgaris Hildenborough: A hydrogenase without a bridging ligand in the active site in its oxidised, “as-isolated” state
    • Marques, M.C., et al. The three-dimensional structure of NiFeSe hydrogenase from Desulfovibrio vulgaris Hildenborough: A hydrogenase without a bridging ligand in the active site in its oxidised, “as-isolated” state. Journal of Molecular Biology, 2010, 396(4): 893-907.
    • (2010) Journal of Molecular Biology , vol.396 , Issue.4 , pp. 893-907
    • Marques, M.C.1
  • 42
    • 35748942883 scopus 로고    scopus 로고
    • Computational studies of NiFe and FeFe hydrogenases
    • Siegbahn, P.E.M., J.W. Tye, and M.B. Hall. Computational studies of NiFe and FeFe hydrogenases. Chemical Reviews, 2007, 107(10): 4414-4435.
    • (2007) Chemical Reviews , vol.107 , Issue.10 , pp. 4414-4435
    • Siegbahn, P.E.M.1    Tye, J.W.2    Hall, M.B.3
  • 43
    • 0037009993 scopus 로고    scopus 로고
    • Structural studies of the carbon monoxide complex of [NiFe]hydrogenase from Desulfovibrio vulgaris Miyazaki F: Suggestion for the initial activation site for dihydrogen
    • Ogata, H., et al. Structural studies of the carbon monoxide complex of [NiFe]hydrogenase from Desulfovibrio vulgaris Miyazaki F: Suggestion for the initial activation site for dihydrogen. Journal of the American Chemical Society, 2002, 124(39): 11628-11635.
    • (2002) Journal of the American Chemical Society , vol.124 , Issue.39 , pp. 11628-11635
    • Ogata, H.1
  • 44
    • 68349101212 scopus 로고    scopus 로고
    • 14N HYSCORE investigation of the H-cluster of [FeFe] hydrogenase: Evidence for a nitrogen in the dithiol bridge
    • Silakov, A., et al. 14N HYSCORE investigation of the H-cluster of [FeFe] hydrogenase: Evidence for a nitrogen in the dithiol bridge. Physical Chemistry Chemical Physics, 2009, 11(31): 6592-6599.
    • (2009) Physical Chemistry Chemical Physics , vol.11 , Issue.31 , pp. 6592-6599
    • Silakov, A.1
  • 45
    • 0035961483 scopus 로고    scopus 로고
    • Crystallographic and FTIR spectroscopic evidence of changes in Fe coordination upon reduction of the active site of the Fe-only hydrogenase from Desulfovibrio desulfuricans
    • Nicolet, Y., et al. Crystallographic and FTIR spectroscopic evidence of changes in Fe coordination upon reduction of the active site of the Fe-only hydrogenase from Desulfovibrio desulfuricans. Journal of the American Chemical Society, 2001, 123(8): 1596-1601.
    • (2001) Journal of the American Chemical Society , vol.123 , Issue.8 , pp. 1596-1601
    • Nicolet, Y.1
  • 46
    • 35048857033 scopus 로고    scopus 로고
    • The electronic structure of the H-cluster in the [FeFe]-hydrogenase from Desulfovibrio desulfuricans: A Q-band Fe-57-ENDOR and HYSCORE study
    • Silakov, A., et al. The electronic structure of the H-cluster in the [FeFe]-hydrogenase from Desulfovibrio desulfuricans: A Q-band Fe-57-ENDOR and HYSCORE study. Journal of the American Chemical Society, 2007, 129: 11447-11458.
    • (2007) Journal of the American Chemical Society , vol.129 , pp. 11447-11458
    • Silakov, A.1
  • 47
    • 0039182024 scopus 로고    scopus 로고
    • Binding of exogenously added carbon monoxide at the active site of the iron-only hydrogenase (CpI) from Clostridium pasteurianum
    • Lemon, B.J., and J.W. Peters. Binding of exogenously added carbon monoxide at the active site of the iron-only hydrogenase (CpI) from Clostridium pasteurianum. Biochemistry, 1999, 38(40): 12969-12973.
    • (1999) Biochemistry , vol.38 , Issue.40 , pp. 12969-12973
    • Lemon, B.J.1    Peters, J.W.2
  • 48
    • 34547269611 scopus 로고    scopus 로고
    • Hydrogenase-coated carbon nanotubes for efficient H2 oxidation
    • Alonso-Lomillo, M.A., et al. Hydrogenase-coated carbon nanotubes for efficient H2 oxidation. Nano Letters, 2007, 7(6): 1603-1608.
    • (2007) Nano Letters , vol.7 , Issue.6 , pp. 1603-1608
    • Alonso-Lomillo, M.A.1
  • 49
    • 70449529430 scopus 로고    scopus 로고
    • Immobilization of the hyperthermophilic hydrogenase from Aquifex aeolicus bacterium onto gold and carbon nanotube electrodes for efficient H-2 oxidation
    • Luo, X.J., et al. Immobilization of the hyperthermophilic hydrogenase from Aquifex aeolicus bacterium onto gold and carbon nanotube electrodes for efficient H-2 oxidation. Journal of Biological Inorganic Chemistry, 2009, 14(8): 1275-1288.
    • (2009) Journal of Biological Inorganic Chemistry , vol.14 , Issue.8 , pp. 1275-1288
    • Luo, X.J.1
  • 50
    • 84858052739 scopus 로고    scopus 로고
    • Order-of-magnitude enhancement of an enzymatic hydrogen-air fuel cell based on pyrenyl carbon nanostructures
    • Krishnan, S., and F.A. Armstrong. Order-of-magnitude enhancement of an enzymatic hydrogen-air fuel cell based on pyrenyl carbon nanostructures. Chemical Science, 2012, 3(4): 1015-1023.
    • (2012) Chemical Science , vol.3 , Issue.4 , pp. 1015-1023
    • Krishnan, S.1    Armstrong, F.A.2
  • 51
    • 81355161716 scopus 로고    scopus 로고
    • Electrically conducting particle networks in polymer electrolyte as three-dimensional electrodes for hydrogenase electrocatalysis
    • Healy, A.J., et al. Electrically conducting particle networks in polymer electrolyte as three-dimensional electrodes for hydrogenase electrocatalysis. Electrochimica Acta, 2011, 56(28): 10786-10790.
    • (2011) Electrochimica Acta , vol.56 , Issue.28 , pp. 10786-10790
    • Healy, A.J.1
  • 52
    • 36749036654 scopus 로고    scopus 로고
    • Wiring-up hydrogenase with single-walled carbon nanotubes
    • McDonald, T.J., et al. Wiring-up hydrogenase with single-walled carbon nanotubes. Nano Letters, 2007, 7(11): 3528-3534.
    • (2007) Nano Letters , vol.7 , Issue.11 , pp. 3528-3534
    • McDonald, T.J.1
  • 53
    • 79953066770 scopus 로고    scopus 로고
    • High-performance hydrogen production and oxidation electrodes with hydrogenase supported on metallic single-wall carbon nanotube networks
    • Svedruzic, D., et al. High-performance hydrogen production and oxidation electrodes with hydrogenase supported on metallic single-wall carbon nanotube networks. Journal of the American Chemical Society, 2011, 133(12): 4299-4306.
    • (2011) Journal of the American Chemical Society , vol.133 , Issue.12 , pp. 4299-4306
    • Svedruzic, D.1
  • 54
    • 84856261361 scopus 로고    scopus 로고
    • Catalytic turnover of FeFe-hydrogenase based on single-molecule imaging
    • Madden, C., et al. Catalytic turnover of FeFe-hydrogenase based on single-molecule imaging. Journal of the American Chemical Society, 2012, 134(3): 1577-1582.
    • (2012) Journal of the American Chemical Society , vol.134 , Issue.3 , pp. 1577-1582
    • Madden, C.1
  • 55
    • 84859119897 scopus 로고    scopus 로고
    • Characterization of photochemical processes for H-2 production by CdS nanorod-FeFe hydrogenase complexes
    • Brown, K.A., et al. Characterization of photochemical processes for H-2 production by CdS nanorod-FeFe hydrogenase complexes. Journal of the American Chemical Society, 2012, 134(12): 5627-5636.
    • (2012) Journal of the American Chemical Society , vol.134 , Issue.12 , pp. 5627-5636
    • Brown, K.A.1
  • 56
    • 80052235153 scopus 로고    scopus 로고
    • Role of the HoxZ subunit in the electron transfer pathway of the membrane-bound NiFe-hydrogenase from Ralstonia eutropha immobilized on electrodes
    • Sezer, M., et al. Role of the HoxZ subunit in the electron transfer pathway of the membrane-bound NiFe-hydrogenase from Ralstonia eutropha immobilized on electrodes. Journal of Physical Chemistry B, 2011, 115(34): 10368-10374.
    • (2011) Journal of Physical Chemistry B , vol.115 , Issue.34 , pp. 10368-10374
    • Sezer, M.1
  • 57
    • 79952270949 scopus 로고    scopus 로고
    • SEIRA spectroscopy of the electrochemical activation of an immobilized NiFe hydrogenase under turnover and non-turnover conditions
    • Millo, D., et al. SEIRA spectroscopy of the electrochemical activation of an immobilized NiFe hydrogenase under turnover and non-turnover conditions. Angewandte Chemie-International Edition, 2011, 50(11): 2632-2634.
    • (2011) Angewandte Chemie-International Edition , vol.50 , Issue.11 , pp. 2632-2634
    • Millo, D.1
  • 58
    • 68549123548 scopus 로고    scopus 로고
    • SOAS: A free program to analyze electrochemical data and other one-dimensional signals
    • Fourmond, V., et al. SOAS: A free program to analyze electrochemical data and other one-dimensional signals. Bioelectrochemistry, 2009, 76(1-2): 141-147.
    • (2009) Bioelectrochemistry , vol.76 , Issue.1-2 , pp. 141-147
    • Fourmond, V.1
  • 59
    • 0037207118 scopus 로고    scopus 로고
    • Enzyme electrokinetics: Hydrogen evolution and oxidation by Allochromatium vinosum [NiFe]-hydrogenase
    • Léger, C., et al. Enzyme electrokinetics: Hydrogen evolution and oxidation by Allochromatium vinosum [NiFe]-hydrogenase. Biochemistry, 2002, 41(52): 15736-15746.
    • (2002) Biochemistry , vol.41 , Issue.52 , pp. 15736-15746
    • Léger, C.1
  • 60
    • 77958607481 scopus 로고    scopus 로고
    • Mechanistic studies of the ‘blue’ Cu enzyme, bilirubin oxidase, as a highly efficient electrocatalyst for the oxygen reduction reaction
    • dos Santos, L., et al. Mechanistic studies of the ‘blue’ Cu enzyme, bilirubin oxidase, as a highly efficient electrocatalyst for the oxygen reduction reaction. Physical Chemistry Chemical Physics, 2010, 12(42): 13962-13974.
    • (2010) Physical Chemistry Chemical Physics , vol.12 , Issue.42 , pp. 13962-13974
    • dos Santos, L.1
  • 61
    • 0037137649 scopus 로고    scopus 로고
    • Effect of a dispersion of interfacial electron transfer rates on steady state catalytic electron transport in NiFe-hydrogenase and other enzymes
    • Leger, C., et al. Effect of a dispersion of interfacial electron transfer rates on steady state catalytic electron transport in NiFe-hydrogenase and other enzymes. Journal of Physical Chemistry B, 2002, 106(50): 13058-13063.
    • (2002) Journal of Physical Chemistry B , vol.106 , Issue.50 , pp. 13058-13063
    • Leger, C.1
  • 62
    • 65249104535 scopus 로고    scopus 로고
    • Correcting for electrocatalyst desorption and inactivation in chronoamperometry experiments
    • Fourmond, V., et al. Correcting for electrocatalyst desorption and inactivation in chronoamperometry experiments. Analytical Chemistry, 2009, 81(8): 2962-2968.
    • (2009) Analytical Chemistry , vol.81 , Issue.8 , pp. 2962-2968
    • Fourmond, V.1
  • 63
    • 4644245238 scopus 로고    scopus 로고
    • Inhibition and aerobic inactivation kinetics of Desulfovibrio fructosovorans NiFe hydrogenase studied by protein film voltammetry
    • Léger, C., et al. Inhibition and aerobic inactivation kinetics of Desulfovibrio fructosovorans NiFe hydrogenase studied by protein film voltammetry. Journal of the American Chemical Society, 2004, 126(38): 12162-12172.
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.38 , pp. 12162-12172
    • Léger, C.1
  • 64
    • 58649121731 scopus 로고    scopus 로고
    • Oxygen-tolerant H-2 oxidation by membrane-bound [NiFe] hydrogenases of Ralstonia species
    • Ludwig, M., et al. Oxygen-tolerant H-2 oxidation by membrane-bound [NiFe] hydrogenases of Ralstonia species. Journal of Biological Chemistry, 2009, 284(1): 465-477.
    • (2009) Journal of Biological Chemistry , vol.284 , Issue.1 , pp. 465-477
    • Ludwig, M.1
  • 65
    • 33749184515 scopus 로고    scopus 로고
    • Electron tunneling chains of mitochondria
    • Moser, C.C., et al. Electron tunneling chains of mitochondria. Biochimica et Biophysica Acta-Bioenergetics, 2006, 1757(9-10): 1096-1109.
    • (2006) Biochimica et Biophysica Acta-Bioenergetics , vol.1757 , Issue.9-10 , pp. 1096-1109
    • Moser, C.C.1
  • 66
    • 79959881257 scopus 로고    scopus 로고
    • Rates of intra- and intermolecular electron transfers in hydrogenase deduced from steady-state activity measurements
    • Dementin, S., et al. Rates of intra- and intermolecular electron transfers in hydrogenase deduced from steady-state activity measurements. Journal of the American Chemical Society, 2011, 133(26): 10211-10221.
    • (2011) Journal of the American Chemical Society , vol.133 , Issue.26 , pp. 10211-10221
    • Dementin, S.1
  • 67
    • 33646161964 scopus 로고    scopus 로고
    • Changing the ligation of the distal 4Fe4S cluster in NiFe hydrogenase impairs inter- and intramolecular electron transfers
    • Dementin, S., et al. Changing the ligation of the distal 4Fe4S cluster in NiFe hydrogenase impairs inter- and intramolecular electron transfers. Journal of the American Chemical Society, 2006, 128(15): 5209-5218.
    • (2006) Journal of the American Chemical Society , vol.128 , Issue.15 , pp. 5209-5218
    • Dementin, S.1
  • 68
    • 30744452491 scopus 로고    scopus 로고
    • Electron flow in multicenter enzymes: Theory, applications, and consequences on the natural design of redox chains
    • Léger, C., et al. Electron flow in multicenter enzymes: Theory, applications, and consequences on the natural design of redox chains. Journal of the American Chemical Society, 2006, 128(1): 180-187.
    • (2006) Journal of the American Chemical Society , vol.128 , Issue.1 , pp. 180-187
    • Léger, C.1
  • 69
    • 84863899218 scopus 로고    scopus 로고
    • Electrocatalytic mechanism of reversible hydrogen cycling by enzymes and distinctions between the major classes of hydrogenases
    • Hexter, S.V., et al. Electrocatalytic mechanism of reversible hydrogen cycling by enzymes and distinctions between the major classes of hydrogenases. Proceedings of the National Academy of Sciences of the United States of America, 2012, 109(29): 11516-21.
    • (2012) Proceedings of the National Academy of Sciences of the United States of America , vol.109 , Issue.29 , pp. 11516-11521
    • Hexter, S.V.1
  • 70
    • 70350234815 scopus 로고    scopus 로고
    • Electrochemical kinetic investigations of the reactions of FeFe-hydrogenases with carbon monoxide and oxygen: Comparing the importance of gas tunnels and active-site electronic/redox effects
    • Goldet, G., et al. Electrochemical kinetic investigations of the reactions of FeFe-hydrogenases with carbon monoxide and oxygen: Comparing the importance of gas tunnels and active-site electronic/redox effects. Journal of the American Chemical Society, 2009, 131(41): 14979-14989.
    • (2009) Journal of the American Chemical Society , vol.131 , Issue.41 , pp. 14979-14989
    • Goldet, G.1
  • 71
    • 79960588023 scopus 로고    scopus 로고
    • The NiFe-hydrogenase of the Cyanobacterium synechocystis sp PCC 6803 works bidirectionally with a bias to H(2) production
    • McIntosh, C.L., et al. The NiFe-hydrogenase of the Cyanobacterium synechocystis sp PCC 6803 works bidirectionally with a bias to H(2) production. Journal of the American Chemical Society, 2011, 133(29): 11308-11319.
    • (2011) Journal of the American Chemical Society , vol.133 , Issue.29 , pp. 11308-11319
    • McIntosh, C.L.1
  • 72
    • 84861402614 scopus 로고    scopus 로고
    • Understanding and tuning the catalytic bias of hydrogenase
    • Hamdan, A.A., et al. Understanding and tuning the catalytic bias of hydrogenase. Journal of the American Chemical Society, 2012, 134(23): 9828.
    • (2012) Journal of the American Chemical Society , vol.134 , Issue.23 , pp. 9828
    • Hamdan, A.A.1
  • 73
    • 35748956722 scopus 로고    scopus 로고
    • Activation and inactivation of hydrogenase function and the catalytic cycle: Spectroelectrochemical studies
    • De Lacey, A.L., et al. Activation and inactivation of hydrogenase function and the catalytic cycle: Spectroelectrochemical studies. Chemical Reviews, 2007, 107(10): 4304-4330.
    • (2007) Chemical Reviews , vol.107 , Issue.10 , pp. 4304-4330
    • De Lacey, A.L.1
  • 74
    • 20044370126 scopus 로고    scopus 로고
    • Structural differences between the ready and unready oxidized states of [NiFe] hydrogenases
    • Volbeda, A., et al. Structural differences between the ready and unready oxidized states of [NiFe] hydrogenases. Journal of Biological Inorganic Chemistry, 2005, 10: 239-249.
    • (2005) Journal of Biological Inorganic Chemistry , vol.10 , pp. 239-249
    • Volbeda, A.1
  • 75
    • 27644552110 scopus 로고    scopus 로고
    • Activation process of [NiFe] hydrogenase elucidated by high-resolution x-ray analyses: Conversion of the ready to the unready state
    • Ogata, H., et al. Activation process of [NiFe] hydrogenase elucidated by high-resolution x-ray analyses: Conversion of the ready to the unready state. Structure, 2005, 13(11): 1635-1642.
    • (2005) Structure , vol.13 , Issue.11 , pp. 1635-1642
    • Ogata, H.1
  • 76
    • 0038375489 scopus 로고    scopus 로고
    • Enzyme electrokinetics: Electrochemical studies of the anaerobic interconversions between active and inactive states of Allochromatium vinosum [NiFe]-hydrogenase
    • Jones, A.K., et al. Enzyme electrokinetics: Electrochemical studies of the anaerobic interconversions between active and inactive states of Allochromatium vinosum [NiFe]-hydrogenase. Journal of the American Chemical Society, 2003, 125(28): 8505-8514.
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.28 , pp. 8505-8514
    • Jones, A.K.1
  • 77
    • 77950795503 scopus 로고    scopus 로고
    • “Two-step” chronoamperometric method for studying the anaerobic inactivation of an oxygen tolerant NiFe hydrogenase
    • Fourmond, V., et al. “Two-step” chronoamperometric method for studying the anaerobic inactivation of an oxygen tolerant NiFe hydrogenase. Journal of the American Chemical Society, 2010, 132(13): 4848-4857.
    • (2010) Journal of the American Chemical Society , vol.132 , Issue.13 , pp. 4848-4857
    • Fourmond, V.1
  • 78
    • 0034685468 scopus 로고    scopus 로고
    • Photochemistry at the active site of the carbon monoxide inhibited form of the iron-only hydrogenase (CpI)
    • Lemon, B.J., and J.W. Peters. Photochemistry at the active site of the carbon monoxide inhibited form of the iron-only hydrogenase (CpI). Journal of the American Chemical Society, 2000, 122(15): 3793-3794.
    • (2000) Journal of the American Chemical Society , vol.122 , Issue.15 , pp. 3793-3794
    • Lemon, B.J.1    Peters, J.W.2
  • 79
    • 58849115344 scopus 로고    scopus 로고
    • Spin distribution of the H-cluster in the H-ox-CO state of the FeFe hydrogenase from Desulfovibrio desulfuricans: HYSCORE and ENDOR study of N-14 and C-13 nuclear interactions
    • Silakov, A., et al. Spin distribution of the H-cluster in the H-ox-CO state of the FeFe hydrogenase from Desulfovibrio desulfuricans: HYSCORE and ENDOR study of N-14 and C-13 nuclear interactions. Journal of Biological Inorganic Chemistry, 2009, 14(2): 301-313.
    • (2009) Journal of Biological Inorganic Chemistry , vol.14 , Issue.2 , pp. 301-313
    • Silakov, A.1
  • 80
    • 41949131441 scopus 로고    scopus 로고
    • Hydrogen-activating enzymes: Activity does not correlate with oxygen sensitivity
    • Baffert, C., et al. Hydrogen-activating enzymes: Activity does not correlate with oxygen sensitivity. Angewandte Chemie-International Edition, 2008, 47(11): 2052-2054.
    • (2008) Angewandte Chemie-International Edition , vol.47 , Issue.11 , pp. 2052-2054
    • Baffert, C.1
  • 81
    • 8844220418 scopus 로고    scopus 로고
    • Electrochemical potential-step investigations of the aerobic interconversions of [NiFe]-hydrogenase from Allochromatium vinosum: New insights into the puzzling difference between unready and ready oxidized inactive states
    • Lamle, S.E., S.P.J. Albracht, and F.A. Armstrong. Electrochemical potential-step investigations of the aerobic interconversions of [NiFe]-hydrogenase from Allochromatium vinosum: New insights into the puzzling difference between unready and ready oxidized inactive states. Journal of the American Chemical Society, 2004, 126(45): 14899-14909.
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.45 , pp. 14899-14909
    • Lamle, S.E.1    Albracht, S.P.J.2    Armstrong, F.A.3
  • 82
  • 83
    • 33845270211 scopus 로고    scopus 로고
    • 2 in still air-An ultimate test for an oxygen tolerant hydrogenase
    • 2 in still air-An ultimate test for an oxygen tolerant hydrogenase. Chemical Communications, 2006(48): 5033-5035.
    • (2006) Chemical Communications , Issue.48 , pp. 5033-5035
    • Vincent, K.A.1
  • 85
    • 18644373177 scopus 로고    scopus 로고
    • The mechanism of activation of a [NiFe]-hydrogenase by electrons, hydrogen, and carbon monoxide
    • Lamle, S.E., S.P.J. Albracht, and F.A. Armstrong. The mechanism of activation of a [NiFe]-hydrogenase by electrons, hydrogen, and carbon monoxide. Journal of the American Chemical Society, 2005, 127(18): 6595-6604.
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.18 , pp. 6595-6604
    • Lamle, S.E.1    Albracht, S.P.J.2    Armstrong, F.A.3
  • 86
    • 27644552110 scopus 로고    scopus 로고
    • Activation process of [NiFe] hydrogenase elucidated by high-resolution x-ray analyses: Conversion of the ready to the unready state
    • Ogata, H., et al. Activation process of [NiFe] hydrogenase elucidated by high-resolution x-ray analyses: Conversion of the ready to the unready state. Structure, 2005, 13(11): 1635-1642.
    • (2005) Structure , vol.13 , Issue.11 , pp. 1635-1642
    • Ogata, H.1
  • 88
    • 80855156729 scopus 로고    scopus 로고
    • Structural basis for a 4Fe-3S cluster in the oxygen-tolerant membrane-bound NiFe-hydrogenase
    • Shomura, Y., et al. Structural basis for a 4Fe-3S cluster in the oxygen-tolerant membrane-bound NiFe-hydrogenase. Nature, 2011, 479(7372): 253-U143.
    • (2011) Nature , vol.479 , Issue.7372 , pp. 253-343
    • Shomura, Y.1
  • 89
    • 79955072473 scopus 로고    scopus 로고
    • A unique iron-sulfur cluster is crucial for oxygen tolerance of a [NiFe]-hydrogenase
    • Goris, T., et al. A unique iron-sulfur cluster is crucial for oxygen tolerance of a [NiFe]-hydrogenase. Nature Chemical Biology, 2011, 7(5): 310-318.
    • (2011) Nature Chemical Biology , vol.7 , Issue.5 , pp. 310-318
    • Goris, T.1
  • 90
    • 79955027963 scopus 로고    scopus 로고
    • Characterization of a unique [FeS] cluster in the electron transfer chain of the oxygen tolerant [NiFe] hydrogenase from Aquifex aeolicus
    • Pandelia, M.-E., et al. Characterization of a unique [FeS] cluster in the electron transfer chain of the oxygen tolerant [NiFe] hydrogenase from Aquifex aeolicus. Proceedings of the National Academy of Sciences of the United States of America, 2011, 108(15): 6097-6102.
    • (2011) Proceedings of the National Academy of Sciences of the United States of America , vol.108 , Issue.15 , pp. 6097-6102
    • Pandelia, M.-E.1
  • 91
    • 84859464540 scopus 로고    scopus 로고
    • X-ray crystallographic and computational studies of the O-2-tolerant NiFe-hydrogenase 1 from Escherichia coli
    • Volbeda, A., et al. X-ray crystallographic and computational studies of the O-2-tolerant NiFe-hydrogenase 1 from Escherichia coli. Proceedings of the National Academy of Sciences of the United States of America, 2012, 109(14): 5305-5310.
    • (2012) Proceedings of the National Academy of Sciences of the United States of America , vol.109 , Issue.14 , pp. 5305-5310
    • Volbeda, A.1
  • 92
    • 84857911690 scopus 로고    scopus 로고
    • How Salmonella oxidises H-2 under aerobic conditions
    • Parkin, A., et al. How Salmonella oxidises H-2 under aerobic conditions. FEBS Letters, 2012, 586(5): 536-544.
    • (2012) FEBS Letters , vol.586 , Issue.5 , pp. 536-544
    • Parkin, A.1
  • 93
    • 53549119985 scopus 로고    scopus 로고
    • The difference a Se makes? Oxygen-tolerant hydrogen production by the [NiFeSe]-hydrogenase from Desulfomicrobium baculatum
    • Parkin, A., et al. The difference a Se makes? Oxygen-tolerant hydrogen production by the [NiFeSe]-hydrogenase from Desulfomicrobium baculatum. Journal of the American Chemical Society, 2008, 130(40): 13410-13416.
    • (2008) Journal of the American Chemical Society , vol.130 , Issue.40 , pp. 13410-13416
    • Parkin, A.1
  • 94
    • 79851504099 scopus 로고    scopus 로고
    • Original design of an oxygen-tolerant [NiFe] hydrogenase: Major effect of a valine-to-cysteine mutation near the active site
    • Liebgott, P.-P., et al. Original design of an oxygen-tolerant [NiFe] hydrogenase: Major effect of a valine-to-cysteine mutation near the active site. Journal of the American Chemical Society, 2011, 133(4): 986-997.
    • (2011) Journal of the American Chemical Society , vol.133 , Issue.4 , pp. 986-997
    • Liebgott, P.-P.1
  • 96
    • 0033134667 scopus 로고    scopus 로고
    • Removal of the bridging ligand atom at the Ni-Fe active site of [NiFe] hydrogenase upon reduction with H-2, as revealed by X-ray structure analysis at 1.4 A resolution
    • Higuchi, Y., et al. Removal of the bridging ligand atom at the Ni-Fe active site of [NiFe] hydrogenase upon reduction with H-2, as revealed by X-ray structure analysis at 1.4 A resolution. Structure, 1999, 7: 549-556.
    • (1999) Structure , vol.7 , pp. 549-556
    • Higuchi, Y.1
  • 97
    • 0031574022 scopus 로고    scopus 로고
    • Unusual ligand structure in Ni-Fe active center and an additional Mg site in hydrogenase revealed by high resolution x-ray structure analysis
    • Higuchi, Y., T. Yagi, and N. Yasuoka. Unusual ligand structure in Ni-Fe active center and an additional Mg site in hydrogenase revealed by high resolution x-ray structure analysis. Structure, 1997, 5(12): 1671-1680.
    • (1997) Structure , vol.5 , Issue.12 , pp. 1671-1680
    • Higuchi, Y.1    Yagi, T.2    Yasuoka, N.3
  • 98
    • 0002123299 scopus 로고    scopus 로고
    • Asymmetric transfer hydrogenation catalyzed by chiral ruthenium complexes
    • Noyori, R., and S. Hashiguchi. Asymmetric transfer hydrogenation catalyzed by chiral ruthenium complexes. Accounts of Chemical Research, 1997, 30(2): 97-102.
    • (1997) Accounts of Chemical Research , vol.30 , Issue.2 , pp. 97-102
    • Noyori, R.1    Hashiguchi, S.2
  • 99
    • 77955336661 scopus 로고    scopus 로고
    • Characteristics of enzyme-based hydrogen fuel cells using an oxygen-tolerant hydrogenase as the anodic catalyst
    • Wait, A.F., et al. Characteristics of enzyme-based hydrogen fuel cells using an oxygen-tolerant hydrogenase as the anodic catalyst. Journal of Physical Chemistry C, 2010, 114(27): 12003-12009.
    • (2010) Journal of Physical Chemistry C , vol.114 , Issue.27 , pp. 12003-12009
    • Wait, A.F.1
  • 100
    • 36248931018 scopus 로고    scopus 로고
    • Enzymatic catalysis on conducting graphite particles
    • Vincent, K.A., et al. Enzymatic catalysis on conducting graphite particles. Nature Chemical Biology, 2007, 3(12): 761-762.
    • (2007) Nature Chemical Biology , vol.3 , Issue.12 , pp. 761-762
    • Vincent, K.A.1
  • 101
    • 70349919653 scopus 로고    scopus 로고
    • Water-gas shift reaction catalyzed by redox enzymes on conducting graphite platelets
    • Lazarus, O., et al. Water-gas shift reaction catalyzed by redox enzymes on conducting graphite platelets. Journal of the American Chemical Society, 2009, 131(40): 14154.
    • (2009) Journal of the American Chemical Society , vol.131 , Issue.40 , pp. 14154
    • Lazarus, O.1
  • 102
    • 84855668583 scopus 로고    scopus 로고
    • A modular system for regeneration of NAD cofactors using graphite particles modified with hydrogenase and diaphorase moieties
    • Reeve, H.A., et al. A modular system for regeneration of NAD cofactors using graphite particles modified with hydrogenase and diaphorase moieties. Chemical Communications, 2012, 48(10): 1589-1591.
    • (2012) Chemical Communications , vol.48 , Issue.10 , pp. 1589-1591
    • Reeve, H.A.1
  • 103
    • 84864195656 scopus 로고    scopus 로고
    • Enzymes and bio-inspired electrocatalysts in solar fuel devices
    • Woolerton, T.W., et al. Enzymes and bio-inspired electrocatalysts in solar fuel devices. Energy and Environmental Science, 2012, 5(6): 7470-7490.
    • (2012) Energy and Environmental Science , vol.5 , Issue.6 , pp. 7470-7490
    • Woolerton, T.W.1
  • 104
    • 58649123792 scopus 로고    scopus 로고
    • Catalytic electrochemistry of a NiFeSe-hydrogenase on TiO2 and demonstration of its suitability for visible-light driven H-2 production
    • Reisner, E., J.C. Fontecilla-Camps, and F.A. Armstrong. Catalytic electrochemistry of a NiFeSe-hydrogenase on TiO2 and demonstration of its suitability for visible-light driven H-2 production. Chemical Communications, 2009, 5: 550-552.
    • (2009) Chemical Communications , vol.5 , pp. 550-552
    • Reisner, E.1    Fontecilla-Camps, J.C.2    Armstrong, F.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.