메뉴 건너뛰기




Volumn 5, Issue 10, 2009, Pages 727-733

Redesigning dehalogenase access tunnels as a strategy for degrading an anthropogenic substrate

Author keywords

[No Author keywords available]

Indexed keywords

1,2,3 TRICHLOROPROPANE; BACTERIAL ENZYME; CARBON; DEHALOGENASE; HALOGEN; PROPANE; UNCLASSIFIED DRUG;

EID: 70349330482     PISSN: 15524450     EISSN: 15524469     Source Type: Journal    
DOI: 10.1038/nchembio.205     Document Type: Article
Times cited : (230)

References (50)
  • 1
    • 0034700242 scopus 로고    scopus 로고
    • Redesigning the substrate specifcity of an enzyme: Isocitrate dehydrogenase.
    • Doyle, S.A., Fung, S.Y. & Koshland, D.E. Jr. Redesigning the substrate specifcity of an enzyme: isocitrate dehydrogenase. Biochemistry 39, 14348-14355 (2000).
    • (2000) Biochemistry , vol.39 , pp. 14348-14355
    • Doyle, S.A.1    Fung, S.Y.2    Koshland Jr., D.E.3
  • 2
    • 0035877632 scopus 로고    scopus 로고
    • Engineering delta 9-16:0-acyl carrier protein (ACP) desaturase specifcity based on combinatorial saturation mutagenesis and logical redesign of the castor delta 9-18:0-ACP desaturase
    • Whittle, E. & Shanklin, J. Engineering delta 9-16:0-acyl carrier protein (ACP) desaturase specifcity based on combinatorial saturation mutagenesis and logical redesign of the castor delta 9-18:0-ACP desaturase. J. Biol. Chem. 276, 21500-21505 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 21500-21505
    • Whittle, E.1    Shanklin, J.2
  • 3
    • 0035148643 scopus 로고    scopus 로고
    • Directed evolution of a new catalytic site in 2-keto-3-deoxy-6- phosphogluconate aldolase from Escherichia coli.
    • Wymer, N. et al. Directed evolution of a new catalytic site in 2-keto-3-deoxy-6-phosphogluconate aldolase from Escherichia coli. Structure 9, 1-9 (2001).
    • (2001) Structure , vol.9 , pp. 1-9
    • Wymer, N.1
  • 4
    • 33744475011 scopus 로고    scopus 로고
    • Directed evolution of enantioselective enzymes: Iterative cycles of CASTing for probing protein-sequence space
    • Reetz, M.T., Wang, L.W. & Bocola, M. Directed evolution of enantioselective enzymes: iterative cycles of CASTing for probing protein-sequence space. Angew. Chem. Int. Edn Engl. 45, 1236-1241 (2006).
    • (2006) Angew. Chem. Int. Edn Engl. , vol.45 , pp. 1236-1241
    • Reetz, M.T.1    Wang, L.W.2    Bocola, M.3
  • 5
    • 33947095042 scopus 로고    scopus 로고
    • Improving catalytic function by ProSAR-driven enzyme evolution
    • Fox, R.J. et al. Improving catalytic function by ProSAR-driven enzyme evolution. Nat. Biotechnol. 25, 338-344 (2007).
    • (2007) Nat. Biotechnol. , vol.25 , pp. 338-344
    • Fox, R.J.1
  • 6
    • 39849090377 scopus 로고    scopus 로고
    • Complete inversion of enantioselectivity towards acetylated tertiary alcohols by a double mutant of a Bacillus subtilis esterase
    • Bartsch, S., Kourist, R. & Bornscheuer, U.T. Complete inversion of enantioselectivity towards acetylated tertiary alcohols by a double mutant of a Bacillus subtilis esterase. Angew. Chem. Int. Edn Engl. 47, 1508-1511 (2008).
    • (2008) Angew. Chem. Int. Edn Engl. , vol.47 , pp. 1508-1511
    • Bartsch, S.1    Kourist, R.2    Bornscheuer, U.T.3
  • 7
    • 43449098518 scopus 로고    scopus 로고
    • Kemp elimination catalysts by computational enzyme design
    • Rothlisberger, D. et al. Kemp elimination catalysts by computational enzyme design. Nature 453, 190-195 (2008).
    • (2008) Nature , vol.453 , pp. 190-195
    • Rothlisberger, D.1
  • 9
    • 18144403554 scopus 로고    scopus 로고
    • Improving enzyme properties: When are closer mutations better?
    • Morley, K.L. & Kazlauskas, R.J. Improving enzyme properties: when are closer mutations better? Trends Biotechnol. 23, 231-237 (2005).
    • (2005) Trends Biotechnol. , vol.23 , pp. 231-237
    • Morley, K.L.1    Kazlauskas, R.J.2
  • 11
    • 28644444340 scopus 로고    scopus 로고
    • Bacterial degradation of xenobiotic compounds: Evolution and distribution of novel enzyme activities
    • Janssen, D.B., Dinkla, I.J., Poelarends, G.J. & Terpstra, P. Bacterial degradation of xenobiotic compounds: evolution and distribution of novel enzyme activities. Environ. Microbiol. 7, 1868-1882 (2005).
    • (2005) Environ. Microbiol. , vol.7 , pp. 1868-1882
    • Janssen, D.B.1    Dinkla, I.J.2    Poelarends, G.J.3    Terpstra, P.4
  • 12
    • 0033179546 scopus 로고    scopus 로고
    • Dehalogenases applied to industrial-scale biocatalysis
    • Swanson, P.E. Dehalogenases applied to industrial-scale biocatalysis. Curr. Opin. Biotechnol. 10, 365-369 (1999).
    • (1999) Curr. Opin. Biotechnol. , vol.10 , pp. 365-369
    • Swanson, P.E.1
  • 13
    • 0034742615 scopus 로고    scopus 로고
    • Rate constants for the reactions of OH with chlorinated propanes
    • Yujing, M. & Mellouki, A. Rate constants for the reactions of OH with chlorinated propanes. Phys. Chem. Chem. Phys. 3, 2614-2617 (2001).
    • (2001) Phys. Chem. Chem. Phys. , vol.3 , pp. 2614-2617
    • Yujing, M.1    Mellouki, A.2
  • 14
    • 0036300748 scopus 로고    scopus 로고
    • Biodegradation of 1, 2,3-trichloropropane through directed evolution and heterologous expression of a haloalkane dehalogenase gene
    • Bosma, T., Damborsky, J., Stucki, G. & Janssen, D.B. Biodegradation of 1,2,3-trichloropropane through directed evolution and heterologous expression of a haloalkane dehalogenase gene. Appl. Environ. Microbiol. 68, 3582-3587 (2002).
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 3582-3587
    • Bosma, T.1    Damborsky, J.2    Stucki, G.3    Janssen, D.B.4
  • 15
    • 0032850679 scopus 로고    scopus 로고
    • Utilization of trihalogenated propanes by Agrobacterium radiobacter AD1 through heterologous expression of the haloalkane dehalogenase from Rhodococcus sp. strain m15-3
    • Bosma, T., Kruizinga, E., de Bruin, E.J., Poelarends, G.J. & Janssen, D.B. Utilization of trihalogenated propanes by Agrobacterium radiobacter AD1 through heterologous expression of the haloalkane dehalogenase from Rhodococcus sp. strain m15-3. Appl. Environ. Microbiol. 65, 4575-4581 (1999).
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 4575-4581
    • Bosma, T.1    Kruizinga, E.2    De Bruin, E.J.3    Poelarends, G.J.4    Janssen, D.B.5
  • 16
    • 0023404069 scopus 로고
    • Purifcation and properties of haloalkane dehalogenase from Corynebacterium sp. strain m15-3
    • Yokota, T., Omori, T. & Kodama, T. Purifcation and properties of haloalkane dehalogenase from Corynebacterium sp. strain m15-3. J. Bacteriol. 169, 4049-4054 (1987).
    • (1987) J. Bacteriol. , vol.169 , pp. 4049-4054
    • Yokota, T.1    Omori, T.2    Kodama, T.3
  • 17
    • 0023829191 scopus 로고
    • Purifcation and characterization of a bacterial dehalogenase with activity toward halogenated alkanes, alcohols and ethers
    • Janssen, D.B. et al. Purifcation and characterization of a bacterial dehalogenase with activity toward halogenated alkanes, alcohols and ethers. Eur. J. Biochem. 171, 67-72 (1988).
    • (1988) Eur. J. Biochem. , vol.171 , pp. 67-72
    • Janssen, D.B.1
  • 18
    • 0025138372 scopus 로고
    • Isolation and characterization of a haloalkane halidohydrolase from Rhodococcus erythropolis Y2
    • Sallis, P.J., Armfeld, S.J., Bull, A.T. & Hardman, D.J. Isolation and characterization of a haloalkane halidohydrolase from Rhodococcus erythropolis Y2. J. Gen. Microbiol. 136, 115-120 (1990).
    • (1990) J. Gen. Microbiol. , vol.136 , pp. 115-120
    • Sallis, P.J.1    Armfeld, S.J.2    Bull, A.T.3    Hardman, D.J.4
  • 19
    • 0031026361 scopus 로고    scopus 로고
    • The plasmid-located haloalkane dehalogenase gene from Rhodococcus rhodochrous NCIMB 13064
    • Kulakova, A.N., Larkin, M.J. & Kulakov, L.A. The plasmid-located haloalkane dehalogenase gene from Rhodococcus rhodochrous NCIMB 13064. Microbiology 143, 109-115 (1997).
    • (1997) Microbiology , vol.143 , pp. 109-115
    • Kulakova, A.N.1    Larkin, M.J.2    Kulakov, L.A.3
  • 21
    • 0033534177 scopus 로고    scopus 로고
    • Haloalkane dehalogenase: Structure of a Rhodococcus enzyme
    • Newman, J. et al. Haloalkane dehalogenase: structure of a Rhodococcus enzyme. Biochemistry 38, 16105-16114 (1999).
    • (1999) Biochemistry , vol.38 , pp. 16105-16114
    • Newman, J.1
  • 22
    • 0036226117 scopus 로고    scopus 로고
    • Functionally relevant motions of haloalkane dehalogenases occur in the specifcity-modulating cap domains
    • Otyepka, M. & Damborsky, J. Functionally relevant motions of haloalkane dehalogenases occur in the specifcity-modulating cap domains. Protein Sci. 11, 1206-1217 (2002).
    • (2002) Protein Sci. , vol.11 , pp. 1206-1217
    • Otyepka, M.1    Damborsky, J.2
  • 23
    • 0027337615 scopus 로고
    • Crystallographic analysis of the catalytic mechanism of haloalkane dehalogenase
    • Verschueren, K.H.G., Seljee, F., Rozeboom, H.J., Kalk, K.H. & Dijkstra, B.W. Crystallographic analysis of the catalytic mechanism of haloalkane dehalogenase. Nature 363, 693-698 (1993).
    • (1993) Nature , vol.363 , pp. 693-698
    • Verschueren, K.H.G.1    Seljee, F.2    Rozeboom, H.J.3    Kalk, K.H.4    Dijkstra, B.W.5
  • 24
    • 0001121864 scopus 로고    scopus 로고
    • Rapid evolution of reversible denaturation and elevated melting temperature in a microbial haloalkane dehalogenase
    • Gray, K.A. et al. Rapid evolution of reversible denaturation and elevated melting temperature in a microbial haloalkane dehalogenase. Adv. Synth. Catal. 343, 607-617 (2001).
    • (2001) Adv. Synth. Catal. , vol.343 , pp. 607-617
    • Gray, K.A.1
  • 25
    • 33947389519 scopus 로고    scopus 로고
    • Mechanism of enhanced conversion of 1,2,3-trichloropropane by mutant haloalkane dehalogenase revealed by molecular modeling
    • Banas, P., Otyepka, M., Jerabek, P., Petrek, M. & Damborsky, J. Mechanism of enhanced conversion of 1,2,3-trichloropropane by mutant haloalkane dehalogenase revealed by molecular modeling. J. Comput. Aided Mol. Des. 20, 375-383 (2006).
    • (2006) J. Comput. Aided Mol. Des. , vol.20 , pp. 375-383
    • Banas, P.1    Otyepka, M.2    Jerabek, P.3    Petrek, M.4    Damborsky, J.5
  • 26
    • 33847142225 scopus 로고    scopus 로고
    • CAVER: A new tool to explore routes from protein clefts, pockets and cavities
    • Petrek, M. et al. CAVER: A new tool to explore routes from protein clefts, pockets and cavities. BMC Bioinformatics 7, 316 (2006).
    • (2006) BMC Bioinformatics , vol.7 , pp. 316
    • Petrek, M.1
  • 27
    • 0037117562 scopus 로고    scopus 로고
    • Comparison of the dynamics of substrate access channels in three cytochrome P450s reveals different opening mechanisms and a novel functional role for a buried arginine
    • Winn, P.J., Ludemann, S.K., Gauges, R., Lounnas, V. & Wade, R.C. Comparison of the dynamics of substrate access channels in three cytochrome P450s reveals different opening mechanisms and a novel functional role for a buried arginine. Proc. Natl. Acad. Sci. USA 99, 5361-5366 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 5361-5366
    • Winn, P.J.1    Ludemann, S.K.2    Gauges, R.3    Lounnas, V.4    Wade, R.C.5
  • 28
    • 67849130559 scopus 로고    scopus 로고
    • HotSpot Wizard: A web server for identifcation of hot spots in protein engineering
    • Pavelka, A., Chovancova, E. & Damborsky, J. HotSpot Wizard: a web server for identifcation of hot spots in protein engineering. Nucleic Acids Res. 37 (web server issue): W376-W383 (2009).
    • (2009) Nucleic Acids Res. , vol.37 , Issue.WEB SERVER ISSUE
    • Pavelka, A.1    Chovancova, E.2    Damborsky, J.3
  • 30
    • 2542563521 scopus 로고    scopus 로고
    • Chemical and biochemical strategies for the randomization of protein encoding DNA sequences: Library construction methods for directed evolution
    • Neylon, C. Chemical and biochemical strategies for the randomization of protein encoding DNA sequences: library construction methods for directed evolution. Nucleic Acids Res. 32, 1448-1459 (2004).
    • (2004) Nucleic Acids Res. , vol.32 , pp. 1448-1459
    • Neylon, C.1
  • 31
    • 0038385475 scopus 로고    scopus 로고
    • Steady-state and pre-steady-state kinetic analysis of halopropane conversion by a Rhodococcus haloalkane dehalogenase
    • Bosma, T., Pikkemaat, M.G., Kingma, J., Dijk, J. & Janssen, D.B. Steady-state and pre-steady-state kinetic analysis of halopropane conversion by a Rhodococcus haloalkane dehalogenase. Biochemistry 42, 8047-8053 (2003).
    • (2003) Biochemistry , vol.42 , pp. 8047-8053
    • Bosma, T.1    Pikkemaat, M.G.2    Kingma, J.3    Dijk, J.4    Janssen, D.B.5
  • 32
    • 0029946082 scopus 로고    scopus 로고
    • Kinetics of halide release of haloalkane dehalogenase: Evidence for a slow conformational change
    • Schanstra, J.P. & Janssen, D.B. Kinetics of halide release of haloalkane dehalogenase: evidence for a slow conformational change. Biochemistry 35, 5624-5632 (1996).
    • (1996) Biochemistry , vol.35 , pp. 5624-5632
    • Schanstra, J.P.1    Janssen, D.B.2
  • 33
    • 0242413672 scopus 로고    scopus 로고
    • Catalytic mechamism of the haloalkane dehalogenase LinB from Sphingomonas paucimobilis UT26
    • Prokop, Z. et al. Catalytic mechamism of the haloalkane dehalogenase LinB from Sphingomonas paucimobilis UT26. J. Biol. Chem. 278, 45094-45100 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 45094-45100
    • Prokop, Z.1
  • 34
    • 11244281311 scopus 로고    scopus 로고
    • The "evolvability" of promiscuous protein functions
    • Aharoni, A. et al. The "evolvability" of promiscuous protein functions. Nat. Genet. 37, 73-76 (2005).
    • (2005) Nat. Genet. , vol.37 , pp. 73-76
    • Aharoni, A.1
  • 35
    • 0029124086 scopus 로고
    • Experiences of a large-scale application of 1,2-dichloroethane degrading microorganisms for groundwater treatment
    • Stucki, G. & Thuer, M. Experiences of a large-scale application of 1,2-dichloroethane degrading microorganisms for groundwater treatment. Environ. Sci. Technol. 29, 2339-2345 (1995).
    • (1995) Environ. Sci. Technol. , vol.29 , pp. 2339-2345
    • Stucki, G.1    Thuer, M.2
  • 36
    • 0037418209 scopus 로고    scopus 로고
    • Comparison of formation of reactive conformers for the SN2 displacements by CH3CO2-in water and by Asp124-CO2-in a haloalkane dehalogenase
    • Hur, S., Kahn, K. & Bruice, T.C. Comparison of formation of reactive conformers for the SN2 displacements by CH3CO2-in water and by Asp124-CO2-in a haloalkane dehalogenase. Proc. Natl. Acad. Sci. USA 100, 2215-2219 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 2215-2219
    • Hur, S.1    Kahn, K.2    Bruice, T.C.3
  • 37
    • 0037433269 scopus 로고    scopus 로고
    • Combined QM/MM study of the mechanism and kinetic isotope effect of the nucleophilic substitution reaction in haloalkane dehalogenase
    • Devi-Kesavan, L.S. & Gao, J. Combined QM/MM study of the mechanism and kinetic isotope effect of the nucleophilic substitution reaction in haloalkane dehalogenase. J. Am. Chem. Soc. 125, 1532-1540 (2003).
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 1532-1540
    • Devi-Kesavan, L.S.1    Gao, J.2
  • 38
    • 9344245168 scopus 로고    scopus 로고
    • Solute solvent dynamics and energetics in enzyme catalysis: The S(N)2 reaction of dehalogenase as a general benchmark
    • Olsson, M.H. & Warshel, A. Solute solvent dynamics and energetics in enzyme catalysis: the S(N)2 reaction of dehalogenase as a general benchmark. J. Am. Chem. Soc. 126, 15167-15179 (2004).
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 15167-15179
    • Olsson, M.H.1    Warshel, A.2
  • 39
    • 0034700262 scopus 로고    scopus 로고
    • Crystal structure of the haloalkane dehalogenase from Sphingomonas paucimobilis UT26
    • Marek, J. et al. Crystal structure of the haloalkane dehalogenase from Sphingomonas paucimobilis UT26. Biochemistry 39, 14082-14086 (2000).
    • (2000) Biochemistry , vol.39 , pp. 14082-14086
    • Marek, J.1
  • 40
    • 0346101759 scopus 로고    scopus 로고
    • Modifcation of activity and specifcity of haloalkane dehalogenase from Sphingomonas paucimobilis UT26 by engineering of its entrance tunnel
    • Chaloupkova, R. et al. Modifcation of activity and specifcity of haloalkane dehalogenase from Sphingomonas paucimobilis UT26 by engineering of its entrance tunnel. J. Biol. Chem. 278, 52622-52628 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 52622-52628
    • Chaloupkova, R.1
  • 41
    • 22144466209 scopus 로고    scopus 로고
    • Do mammalian cytochrome P450s show multiple ligand access pathways and ligand channelling?
    • Schleinkofer, K., Sudarko, Winn, P.J., Ludemann, S.K. & Wade, R.C. Do mammalian cytochrome P450s show multiple ligand access pathways and ligand channelling? EMBO Rep. 6, 584-589 (2005).
    • (2005) EMBO Rep. , vol.6 , pp. 584-589
    • Schleinkofer, K.1    Sudarko Winn, P.J.2    Ludemann, S.K.3    Wade, R.C.4
  • 43
    • 0034819837 scopus 로고    scopus 로고
    • Protein engineering of Bacillus megaterium CYP102. the oxidation of polycyclic aromatic hydrocarbons
    • Carmichael, A.B. & Wong, L.L. Protein engineering of Bacillus megaterium CYP102. The oxidation of polycyclic aromatic hydrocarbons. Eur. J. Biochem. 268, 3117-3125 (2001).
    • (2001) Eur. J. Biochem. , vol.268 , pp. 3117-3125
    • Carmichael, A.B.1    Wong, L.L.2
  • 44
    • 0036655806 scopus 로고    scopus 로고
    • Blocking the tunnel: Engineering of Candida rugosa lipase mutants with short chain length specifcity
    • Schmitt, J., Brocca, S., Schmid, R.D. & Pleiss, J. Blocking the tunnel: engineering of Candida rugosa lipase mutants with short chain length specifcity. Prot. Eng. 15, 595-601 (2002).
    • (2002) Prot. Eng. , vol.15 , pp. 595-601
    • Schmitt, J.1    Brocca, S.2    Schmid, R.D.3    Pleiss, J.4
  • 45
    • 0036136695 scopus 로고    scopus 로고
    • Structure determinants of substrate specifcity of hydroxynitrile lyase from Manihot esculenta
    • Lauble, H. et al. Structure determinants of substrate specifcity of hydroxynitrile lyase from Manihot esculenta. Protein Sci. 11, 65-71 (2002).
    • (2002) Protein Sci. , vol.11 , pp. 65-71
    • Lauble, H.1
  • 46
    • 4644252576 scopus 로고    scopus 로고
    • Protein engineering of toluene 4-monooxygenase of Pseudomonas mendocina KR1 for synthesizing 4-nitrocatechol from nitrobenzene
    • Fishman, A., Tao, Y., Bentley, W.E. & Wood, T.K. Protein engineering of toluene 4-monooxygenase of Pseudomonas mendocina KR1 for synthesizing 4-nitrocatechol from nitrobenzene. Biotechnol. Bioeng. 87, 779-790 (2004).
    • (2004) Biotechnol. Bioeng. , vol.87 , pp. 779-790
    • Fishman, A.1    Tao, Y.2    Bentley, W.E.3    Wood, T.K.4
  • 47
    • 1942469472 scopus 로고    scopus 로고
    • Structures of nitric oxide synthase isoforms complexed with the inhibitor AR-R17477 suggest a rational basis for specifcity and inhibitor design
    • Fedorov, R., Vasan, R., Ghosh, D.K. & Schlichting, I. Structures of nitric oxide synthase isoforms complexed with the inhibitor AR-R17477 suggest a rational basis for specifcity and inhibitor design. Proc. Natl. Acad. Sci. USA 101, 5892-5897 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 5892-5897
    • Fedorov, R.1    Vasan, R.2    Ghosh, D.K.3    Schlichting, I.4
  • 48
    • 34848893919 scopus 로고    scopus 로고
    • Cloning of an epoxide hydrolase-encoding gene from Aspergillus niger M200, overexpression in E. coli, and modifcation of activity and enantioselectivity of the enzyme by protein engineering
    • Kotik, M., Stepanek, V., Kyslik, P. & Maresova, H. Cloning of an epoxide hydrolase-encoding gene from Aspergillus niger M200, overexpression in E. coli, and modifcation of activity and enantioselectivity of the enzyme by protein engineering. J. Biotechnol. 132, 8-15 (2007).
    • (2007) J. Biotechnol. , vol.132 , pp. 8-15
    • Kotik, M.1    Stepanek, V.2    Kyslik, P.3    Maresova, H.4
  • 49
    • 40549093291 scopus 로고    scopus 로고
    • Protein engineering of toluene monooxygenases for synthesis of chiral sulfoxides
    • Feingersch, R., Shainsky, J., Wood, T.K. & Fishman, A. Protein engineering of toluene monooxygenases for synthesis of chiral sulfoxides. Appl. Environ. Microbiol. 74, 1555-1566 (2008).
    • (2008) Appl. Environ. Microbiol. , vol.74 , pp. 1555-1566
    • Feingersch, R.1    Shainsky, J.2    Wood, T.K.3    Fishman, A.4
  • 50
    • 0001606804 scopus 로고
    • New colorimetric determination of chloride using mercuric thiocyanate and ferric ion
    • Iwasaki, I., Utsumi, S. & Ozawa, T. New colorimetric determination of chloride using mercuric thiocyanate and ferric ion. Bull. Chem. Soc. Jpn. 25, 226 (1952).
    • (1952) Bull. Chem. Soc. Jpn. , vol.25 , pp. 226
    • Iwasaki, I.1    Utsumi, S.2    Ozawa, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.