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Volumn 43, Issue 34, 2004, Pages 11109-11117

Investigations of photolysis and rebinding kinetics in myoglobin using proximal ligand replacements

Author keywords

[No Author keywords available]

Indexed keywords

CARBON MONOXIDE; ENZYME KINETICS; MUTAGENS; PROTEINS; RAMAN SPECTROSCOPY; VIBRATIONS (MECHANICAL);

EID: 4644288083     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi049077g     Document Type: Article
Times cited : (22)

References (65)
  • 2
    • 1842618422 scopus 로고    scopus 로고
    • Hemoglobins: O2 Uptake and Transport
    • (Atwood, J. L., and Steed, J. W., Eds.), Marcel Dekker, New York
    • Sage, J. T. (2004) Hemoglobins: O2 Uptake and Transport, in Encyclopedia of Supramolecular Chemistry (Atwood, J. L., and Steed, J. W., Eds.) pp 636-644, Marcel Dekker, New York.
    • (2004) Encyclopedia of Supramolecular Chemistry , pp. 636-644
    • Sage, J.T.1
  • 3
    • 0014958182 scopus 로고
    • Stereochemistry of cooperative effects in haemoglobin
    • Perutz, M. F. (1970) Stereochemistry of cooperative effects in haemoglobin, Nature 228, 726-739.
    • (1970) Nature , vol.228 , pp. 726-739
    • Perutz, M.F.1
  • 4
    • 0018654083 scopus 로고
    • Regulation of oxygen affinity of hemoglobin: Influence of structure of the globin on the heme iron
    • Perutz, M. F. (1979) Regulation of oxygen affinity of hemoglobin: influence of structure of the globin on the heme iron, Annu. Rev. Biochem. 48, 327-386.
    • (1979) Annu. Rev. Biochem. , vol.48 , pp. 327-386
    • Perutz, M.F.1
  • 6
    • 0025344693 scopus 로고
    • Mechanisms regulating the reactions of human hemoglobin with oxygen and carbon monoxide
    • Perutz, M. F. (1990) Mechanisms regulating the reactions of human hemoglobin with oxygen and carbon monoxide, Annu. Rev. Physiol. 52, 1-25.
    • (1990) Annu. Rev. Physiol. , vol.52 , pp. 1-25
    • Perutz, M.F.1
  • 7
    • 0344730727 scopus 로고
    • Protein fluctuations, distributed coupling, and the binding of ligands to heme-proteins
    • Šrajer, V., Reinisch, L., and Champion, P. M. (1988) Protein fluctuations, distributed coupling, and the binding of ligands to heme-proteins, J. Am. Chem. Soc. 110, 6656-6670.
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 6656-6670
    • Šrajer, V.1    Reinisch, L.2    Champion, P.M.3
  • 8
    • 0025718720 scopus 로고
    • Investigations of optical-line shapes and kinetic hole burning in myoglobin
    • Šrajer, V., and Champion, P. M. (1991) Investigations of optical-line shapes and kinetic hole burning in myoglobin, Biochemistry 30, 7390-7402.
    • (1991) Biochemistry , vol.30 , pp. 7390-7402
    • Šrajer, V.1    Champion, P.M.2
  • 9
    • 0023640468 scopus 로고
    • Linkage of functional and structural heterogeneity in proteins-dynamic hole burning in carboxymyoglobin
    • Campbell, B. F., Chance, M. R., and Friedman, J. M. (1987) Linkage of functional and structural heterogeneity in proteins-dynamic hole burning in carboxymyoglobin, Science 238, 373-376.
    • (1987) Science , vol.238 , pp. 373-376
    • Campbell, B.F.1    Chance, M.R.2    Friedman, J.M.3
  • 10
    • 0000040147 scopus 로고
    • Evidence for proximal control of ligand specificity in hemeproteins-absorption and Raman studies of cryogenically trapped photoproducts of ligand bound myoglobins
    • Ahmed, A. M., Campbell, B. F., Caruso, D., Chance, M. R., Chavez, M. D., Courtney, S. H., Friedman, J. M., Iben, I. E. T., Ondrias, M. R., and Yang, M. (1991) Evidence for proximal control of ligand specificity in hemeproteins-absorption and Raman studies of cryogenically trapped photoproducts of ligand bound myoglobins, Chem. Phys. 158, 329-351.
    • (1991) Chem. Phys. , vol.158 , pp. 329-351
    • Ahmed, A.M.1    Campbell, B.F.2    Caruso, D.3    Chance, M.R.4    Chavez, M.D.5    Courtney, S.H.6    Friedman, J.M.7    Iben, I.E.T.8    Ondrias, M.R.9    Yang, M.10
  • 12
    • 0013129690 scopus 로고
    • Far infrared magnetic resonance of deoxyhemoglobin and deoxymyoglobin
    • Champion, P. M. and Sievers, A. J. (1980) Far infrared magnetic resonance of deoxyhemoglobin and deoxymyoglobin, J. Chem. Phys. 72, 1569-1582.
    • (1980) J. Chem. Phys. , vol.72 , pp. 1569-1582
    • Champion, P.M.1    Sievers, A.J.2
  • 15
    • 0025216601 scopus 로고
    • The effects of amino acid substitution at position E7 (residue 64) on the kinetics of ligand binding to sperm whale myoglobin
    • Rohlfs, R. J., Mathews, A. J., Carver, T. E., Olson, J. S., Springer, B. A., Egeberg, K. D., and Sligar, S. G. (1990) The effects of amino acid substitution at position E7 (residue 64) on the kinetics of ligand binding to sperm whale myoglobin, J. Biol. Chem. 265, 3168-3176.
    • (1990) J. Biol. Chem. , vol.265 , pp. 3168-3176
    • Rohlfs, R.J.1    Mathews, A.J.2    Carver, T.E.3    Olson, J.S.4    Springer, B.A.5    Egeberg, K.D.6    Sligar, S.G.7
  • 16
    • 0025243607 scopus 로고
    • Analysis of the kinetic barriers for ligand-binding to sperm whale myoglobin using site-directed mutagenesis and laser photolysis techniques
    • Carver, T. E., Rohlfs, R. J., Olson, J. S., Gibson, Q. H., Blackmore, R. S., Springer, B. A., and Sligar, S. G. (1990) Analysis of the kinetic barriers for ligand-binding to sperm whale myoglobin using site-directed mutagenesis and laser photolysis techniques, J. Biol. Chem. 265, 20007-20020.
    • (1990) J. Biol. Chem. , vol.265 , pp. 20007-20020
    • Carver, T.E.1    Rohlfs, R.J.2    Olson, J.S.3    Gibson, Q.H.4    Blackmore, R.S.5    Springer, B.A.6    Sligar, S.G.7
  • 17
    • 0027368854 scopus 로고
    • High-resolution crystal structures of distal histidine mutants of sperm whale myoglobin
    • Quillin, M. L., Arduini, R. M., Olson, J. S., and Phillips, G. N., Jr. (1993) High-resolution crystal structures of distal histidine mutants of sperm whale myoglobin, J. Mol. Biol. 234, 140-155.
    • (1993) J. Mol. Biol. , vol.234 , pp. 140-155
    • Quillin, M.L.1    Arduini, R.M.2    Olson, J.S.3    Phillips Jr., G.N.4
  • 19
    • 0029894282 scopus 로고    scopus 로고
    • Kinetic pathways and barriers for ligand binding to myoglobin
    • Olson, J. S., and Phillips, G. N., Jr. (1996) Kinetic pathways and barriers for ligand binding to myoglobin, J. Biol. Chem. 271, 17593-17596.
    • (1996) J. Biol. Chem. , vol.271 , pp. 17593-17596
    • Olson, J.S.1    Phillips Jr., G.N.2
  • 21
    • 0037054809 scopus 로고    scopus 로고
    • Myoglobin as a model system for designing heme protein based blood substitutes
    • Dou, Y., Maillett, D. H., Eich, R. F., and Olson, J. S. (2002) Myoglobin as a model system for designing heme protein based blood substitutes, Biophys. Chem. 98, 127-148.
    • (2002) Biophys. Chem. , vol.98 , pp. 127-148
    • Dou, Y.1    Maillett, D.H.2    Eich, R.F.3    Olson, J.S.4
  • 23
    • 0142242162 scopus 로고    scopus 로고
    • Structural dynamics of myoglobin: Ligand migration and binding in valine 68 mutants
    • Nienhaus, K., Deng, P., Olson, J. S., Warren, J. J., and Nienhaus, G. U. (2003) Structural dynamics of myoglobin: ligand migration and binding in valine 68 mutants, J. Biol. Chem. 278, 42532-42544.
    • (2003) J. Biol. Chem. , vol.278 , pp. 42532-42544
    • Nienhaus, K.1    Deng, P.2    Olson, J.S.3    Warren, J.J.4    Nienhaus, G.U.5
  • 25
    • 0142228327 scopus 로고    scopus 로고
    • Measurement of rate constants for reactions of O2, CO, and NO with hemoglobin
    • Olson, J. S., Foley, E. W., Maillett, D. H., and Paster, E. V. (2003) Measurement of rate constants for reactions of O2, CO, and NO with hemoglobin, Methods Mol. Med. 82, 65-91.
    • (2003) Methods Mol. Med. , vol.82 , pp. 65-91
    • Olson, J.S.1    Foley, E.W.2    Maillett, D.H.3    Paster, E.V.4
  • 26
    • 2442645409 scopus 로고    scopus 로고
    • Crystal structure of the dioxygen-bound heme oxygenase from Coryne-bacterium diphtheriae: Implications for heme oxygenase function
    • in press
    • Unno, M., Matsui, T., Chu, G. C., Couture, M., Yoshida, T., Rousseau, D. L., Olson, J. S., and Ikeda-Saito, M. (2004) Crystal structure of the dioxygen-bound heme oxygenase from Coryne-bacterium diphtheriae: Implications for heme oxygenase function, J. Biol. Chem. (in press).
    • (2004) J. Biol. Chem.
    • Unno, M.1    Matsui, T.2    Chu, G.C.3    Couture, M.4    Yoshida, T.5    Rousseau, D.L.6    Olson, J.S.7    Ikeda-Saito, M.8
  • 27
    • 0031722046 scopus 로고    scopus 로고
    • Myoglobin mutants giving the largest geminate yield in CO rebinding in the nanosecond time domain
    • Sugimoto, T., Unno, M., Shiro, Y., Dou, Y., and Ikeda-Saito, M. (1998) Myoglobin mutants giving the largest geminate yield in CO rebinding in the nanosecond time domain, Biophys. J. 75, 2188-2194.
    • (1998) Biophys. J. , vol.75 , pp. 2188-2194
    • Sugimoto, T.1    Unno, M.2    Shiro, Y.3    Dou, Y.4    Ikeda-Saito, M.5
  • 28
    • 0030009777 scopus 로고    scopus 로고
    • Modulation of protein function by exogenous ligands in protein cavities: CO binding to a myoglobin cavity mutant containing unnatural proximal ligands
    • Decatur, S. M., DePillis, G. D., and Boxer, S. G. (1996) Modulation of protein function by exogenous ligands in protein cavities: CO binding to a myoglobin cavity mutant containing unnatural proximal ligands, Biochemistry 35, 3925-3932.
    • (1996) Biochemistry , vol.35 , pp. 3925-3932
    • Decatur, S.M.1    DePillis, G.D.2    Boxer, S.G.3
  • 29
    • 0030938807 scopus 로고    scopus 로고
    • On the origin of heme absorption band shifts and associated protein structural relaxation in myoglobin following flash photolysis
    • Franzen, S., and Boxer, S. G. (1997) On the origin of heme absorption band shifts and associated protein structural relaxation in myoglobin following flash photolysis, J. Biol. Chem. 272, 9655-9660.
    • (1997) J. Biol. Chem. , vol.272 , pp. 9655-9660
    • Franzen, S.1    Boxer, S.G.2
  • 32
    • 0037007797 scopus 로고    scopus 로고
    • Carbonmonoxy rebinding kinetics in H93G myoglobin: Separation of proximal and distal side effects
    • Franzen, S. (2002) Carbonmonoxy rebinding kinetics in H93G myoglobin: Separation of proximal and distal side effects, J. Phys. Chem. B 106, 4533-4542.
    • (2002) J. Phys. Chem. B , vol.106 , pp. 4533-4542
    • Franzen, S.1
  • 33
    • 0037083579 scopus 로고    scopus 로고
    • The leghemoglobin proximal heme pocket directs oxygen dissociation and stabilizes bound heme
    • Kundu, S., Snyder, B., Das, K., Chowdhury, P., Park, J., Petrich, J. W., and Hargrove, M. S. (2002) The leghemoglobin proximal heme pocket directs oxygen dissociation and stabilizes bound heme, Proteins 46, 268-277.
    • (2002) Proteins , vol.46 , pp. 268-277
    • Kundu, S.1    Snyder, B.2    Das, K.3    Chowdhury, P.4    Park, J.5    Petrich, J.W.6    Hargrove, M.S.7
  • 34
    • 0000457728 scopus 로고    scopus 로고
    • Small substrate recognition in heme proteins
    • (Suslick, K. S., Ed.), Pergamon, Oxford, U.K.
    • Sage, J. T., and Champion, P. M. (1996) Small Substrate Recognition in Heme Proteins, in Comprehensive Supramolecular Chemistry (Suslick, K. S., Ed.) pp 171-218, Pergamon, Oxford, U.K.
    • (1996) Comprehensive Supramolecular Chemistry , pp. 171-218
    • Sage, J.T.1    Champion, P.M.2
  • 35
    • 0034645588 scopus 로고    scopus 로고
    • DFT Computation of the intrinsic barrier to CO geminate recombination with heme compounds
    • Harvey, J. N. (2000) DFT Computation of the intrinsic barrier to CO geminate recombination with heme compounds, J. Am. Chem. Soc. 122, 12401-12402.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 12401-12402
    • Harvey, J.N.1
  • 37
    • 0034623932 scopus 로고    scopus 로고
    • Dissociation and recombination between ligands and heme in a CO-sensing transcriptional activator CooA. A flash photolysis study
    • Kumazaki, S., Nakajima, H., Sakaguchi, T., Nakagawa, E., Shinohara, H., Yoshihara, K., and Aono, S. (2000) Dissociation and recombination between ligands and heme in a CO-sensing transcriptional activator CooA. A flash photolysis study, J. Biol. Chem. 275, 38378-38383.
    • (2000) J. Biol. Chem. , vol.275 , pp. 38378-38383
    • Kumazaki, S.1    Nakajima, H.2    Sakaguchi, T.3    Nakagawa, E.4    Shinohara, H.5    Yoshihara, K.6    Aono, S.7
  • 39
    • 0041417321 scopus 로고
    • Preexponential-limited solid-state chemistry-ultrafast rebinding of a heme ligand complex in a glass or protein matrix
    • Miers, J. B., Postlewaite, J. C., Cowen, B. R., Roemig, G. R., Lee, I. Y. S., and Dlott, D. D. (1991) Preexponential-limited solid-state chemistry-ultrafast rebinding of a heme ligand complex in a glass or protein matrix, J. Chem. Phys. 94, 1825-1836.
    • (1991) J. Chem. Phys. , vol.94 , pp. 1825-1836
    • Miers, J.B.1    Postlewaite, J.C.2    Cowen, B.R.3    Roemig, G.R.4    Lee, I.Y.S.5    Dlott, D.D.6
  • 41
    • 0028339218 scopus 로고
    • Replacement of the proximal ligand of sperm whale myoglobin with free imidazole in the mutant His-93 → Gly
    • Barrick, D. (1994) Replacement of the proximal ligand of sperm whale myoglobin with free imidazole in the mutant His-93 → Gly, Biochemistry 33, 6546-6554.
    • (1994) Biochemistry , vol.33 , pp. 6546-6554
    • Barrick, D.1
  • 42
    • 0028083482 scopus 로고
    • Functional cavities in proteins: A general method for proximal ligand substitution in myoglobin
    • DePillis, G. D., Decatur, S. M., Barrick, D., and Boxer, S. G. (1994) Functional cavities in proteins: A general method for proximal ligand substitution in myoglobin, J. Am. Chem. Soc. 116, 6981-6982.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 6981-6982
    • DePillis, G.D.1    Decatur, S.M.2    Barrick, D.3    Boxer, S.G.4
  • 43
    • 0029100766 scopus 로고
    • Depletion and replacement of protein metal ligands
    • Barrick, D. (1995) Depletion and replacement of protein metal ligands, Curr. Opin. Biotechnol. 6, 411-418.
    • (1995) Curr. Opin. Biotechnol. , vol.6 , pp. 411-418
    • Barrick, D.1
  • 44
    • 0031033020 scopus 로고    scopus 로고
    • A test of the role of the proximal histidines in the Perutz model for cooperativity in haemoglobin
    • Barrick, D., Ho, N. T., Simplaceanu, V., Dahlquist, F. W., and Ho, C. (1997) A test of the role of the proximal histidines in the Perutz model for cooperativity in haemoglobin, Nat. Struct. Biol. 4, 78-83.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 78-83
    • Barrick, D.1    Ho, N.T.2    Simplaceanu, V.3    Dahlquist, F.W.4    Ho, C.5
  • 45
    • 0034212857 scopus 로고    scopus 로고
    • Trans-substitution of the proximal hydrogen bond in moglobin: I. Structural consequences of hydrogen bond deletion
    • Barrick, D., and Dahlquist, F. W. (2000) Trans-substitution of the proximal hydrogen bond in moglobin: I. Structural consequences of hydrogen bond deletion, Proteins: Struct., Funct., Genet. 39, 278-290.
    • (2000) Proteins: Struct., Funct., Genet. , vol.39 , pp. 278-290
    • Barrick, D.1    Dahlquist, F.W.2
  • 46
    • 0034214224 scopus 로고    scopus 로고
    • Trans-substitution of the proximal hydrogen bond in moglobin: II. Energetics, functional consequences, and implications for hemoglobin allostery
    • Barrick, D. (2000) Trans-substitution of the proximal hydrogen bond in moglobin: II. Energetics, functional consequences, and implications for hemoglobin allostery, Proteins: Struct., Funct., Genet. 39, 291-308.
    • (2000) Proteins: Struct., Funct., Genet. , vol.39 , pp. 291-308
    • Barrick, D.1
  • 47
    • 0035799350 scopus 로고    scopus 로고
    • Distal ligand reactivity and quaternary structure studies of proximally detached hemoglobins
    • Barrick, D., Ho, N. T., Simplaceanu, V., and Ho, C. (2001) Distal ligand reactivity and quaternary structure studies of proximally detached hemoglobins, Biochemistry 40, 3780-3795.
    • (2001) Biochemistry , vol.40 , pp. 3780-3795
    • Barrick, D.1    Ho, N.T.2    Simplaceanu, V.3    Ho, C.4
  • 49
    • 0030924067 scopus 로고    scopus 로고
    • Spectroscopic effects of polarity and hydration in the distal heme pocket of deoxymyoglobin
    • Christian, J. F., Unno, M., Sage, J. T., Champion, P. M., Chien, E., and Sligar, S. G. (1997) Spectroscopic effects of polarity and hydration in the distal heme pocket of deoxymyoglobin, Biochemistry 36, 11198-11204.
    • (1997) Biochemistry , vol.36 , pp. 11198-11204
    • Christian, J.F.1    Unno, M.2    Sage, J.T.3    Champion, P.M.4    Chien, E.5    Sligar, S.G.6
  • 50
    • 0032584325 scopus 로고    scopus 로고
    • A possible allosteric communication pathway identified through a resonance Raman study of four beta 37 mutants of human hemoglobin A
    • Peterson, E. S., and Friedman, J. M. (1998) A possible allosteric communication pathway identified through a resonance Raman study of four beta 37 mutants of human hemoglobin A, Biochemistry 37, 4346-4357.
    • (1998) Biochemistry , vol.37 , pp. 4346-4357
    • Peterson, E.S.1    Friedman, J.M.2
  • 51
    • 0021111948 scopus 로고
    • Geminate recombination of carbon-monoxide to myoglobin
    • Henry, E. R., Sommer, J. H., Hofrichter, J., and Eaton, W. A. (1983) Geminate recombination of carbon-monoxide to myoglobin, J. Mol. Biol. 166, 443-451.
    • (1983) J. Mol. Biol. , vol.166 , pp. 443-451
    • Henry, E.R.1    Sommer, J.H.2    Hofrichter, J.3    Eaton, W.A.4
  • 53
    • 0035899723 scopus 로고    scopus 로고
    • On the rate distribution analysis of kinetics data using the maximum entropy method: Application to myoglobin relaxation on the nanosecond and femtosecond time scales
    • Kumar, A. T. N., Zhu, L., Christian, J. F., Demidov, A. A., and Champion, P. M. (2001) On the rate distribution analysis of kinetics data using the maximum entropy method: application to myoglobin relaxation on the nanosecond and femtosecond time scales, J. Phys. Chem. B 105, 7847-7856.
    • (2001) J. Phys. Chem. B , vol.105 , pp. 7847-7856
    • Kumar, A.T.N.1    Zhu, L.2    Christian, J.F.3    Demidov, A.A.4    Champion, P.M.5
  • 57
    • 0034323170 scopus 로고    scopus 로고
    • Resonance raman studies of heme axial ligation in H93G myoglobin
    • Franzen, S., Boxer, S. G., Dyer, R. B., and Woodruff, W. H. (2000) Resonance raman studies of heme axial ligation in H93G myoglobin, J. Phys. Chem. B 104, 10359-10367.
    • (2000) J. Phys. Chem. B , vol.104 , pp. 10359-10367
    • Franzen, S.1    Boxer, S.G.2    Dyer, R.B.3    Woodruff, W.H.4
  • 58
    • 0025855421 scopus 로고
    • Spectroscopic studies of myoglobin at low pH-heme structure and ligation
    • Sage, J. T., Morikis, D., and Champion, P. M. (1991) Spectroscopic studies of myoglobin at low pH-heme structure and ligation. Biochemistry 30, 1227-1237.
    • (1991) Biochemistry , vol.30 , pp. 1227-1237
    • Sage, J.T.1    Morikis, D.2    Champion, P.M.3
  • 59
    • 0036492316 scopus 로고    scopus 로고
    • Electronic structure and bonding in unligated and ligated Fell porphyrins
    • Liao, M.-S., and Scheiner, S. (2002) Electronic structure and bonding in unligated and ligated Fell porphyrins, J. Chem. Phys. 116, 3635-3645.
    • (2002) J. Chem. Phys. , vol.116 , pp. 3635-3645
    • Liao, M.-S.1    Scheiner, S.2
  • 60
    • 0000407005 scopus 로고
    • The iron histidine mode of myoglobin revisited-resonance Raman studies of isotopically labeled Escherichia coli expressed myoglobin
    • Wells, A. V., Sage, J. T., Morikis, D., Champion, P. M., Chiu, M. L., and Sugar, S. G. (1991) The iron histidine mode of myoglobin revisited-resonance Raman studies of isotopically labeled Escherichia coli expressed myoglobin, J. Am. Chem. Soc. 113, 9655-9660.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 9655-9660
    • Wells, A.V.1    Sage, J.T.2    Morikis, D.3    Champion, P.M.4    Chiu, M.L.5    Sugar, S.G.6
  • 61
    • 0040182564 scopus 로고    scopus 로고
    • Identification of histidine 77 as the axial heme ligand of carbonmonoxy CooA by picosecond time-resolved resonance Raman spectroscopy
    • Uchida, T., Ishikawa, H., Ishimori, K., Morishima, I., Nakajima, H., Aono, S., Mizutani, Y., and Kitagawa, T. (2000) Identification of histidine 77 as the axial heme ligand of carbonmonoxy CooA by picosecond time-resolved resonance Raman spectroscopy, Biochemistry 39, 12747-12752.
    • (2000) Biochemistry , vol.39 , pp. 12747-12752
    • Uchida, T.1    Ishikawa, H.2    Ishimori, K.3    Morishima, I.4    Nakajima, H.5    Aono, S.6    Mizutani, Y.7    Kitagawa, T.8
  • 63
    • 0025729839 scopus 로고
    • Spectroscopic studies of myoglobin at low pH-heme ligation kinetics
    • Sage, J. T., Li, P. S., and Champion, P. M. (1991) Spectroscopic studies of myoglobin at low pH-heme ligation kinetics, Biochemistry 30, 1237-1247.
    • (1991) Biochemistry , vol.30 , pp. 1237-1247
    • Sage, J.T.1    Li, P.S.2    Champion, P.M.3


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