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Volumn 44, Issue 50, 2005, Pages 16502-16512

An elementary reaction step of the proton pump is revealed by mutation of tryptophan-164 to phenylalanine in cytochrome c oxidase from Paracoccus denitrificans

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; CELL MEMBRANES; MUTAGENESIS; PROTONS; REACTION KINETICS; REDOX REACTIONS; REDUCTION;

EID: 29244472486     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0511336     Document Type: Article
Times cited : (42)

References (64)
  • 1
    • 1942472486 scopus 로고    scopus 로고
    • Cytochrome c oxidase: 25 Years of the elusive proton pump
    • Wikström, M. (2004) Cytochrome c oxidase: 25 years of the elusive proton pump, Biochim. Biophys. Acta 1655, 241-247.
    • (2004) Biochim. Biophys. Acta , vol.1655 , pp. 241-247
    • Wikström, M.1
  • 2
    • 3242763877 scopus 로고    scopus 로고
    • Redox-driven membrane-bound proton pumps
    • Brzezinski, P. (2004) Redox-driven membrane-bound proton pumps, Trends Biochem. Sci. 29, 380-387.
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 380-387
    • Brzezinski, P.1
  • 3
    • 0037716158 scopus 로고    scopus 로고
    • Understanding the mechanism of proton movement linked to oxygen reduction in cytochrome c oxidase: Lessons from other proteins
    • Mills, D. A., and Ferguson-Miller, S. (2003) Understanding the mechanism of proton movement linked to oxygen reduction in cytochrome c oxidase: lessons from other proteins, FEBS Lett. 545, 47-51.
    • (2003) FEBS Lett. , vol.545 , pp. 47-51
    • Mills, D.A.1    Ferguson-Miller, S.2
  • 4
    • 0017358508 scopus 로고
    • Proton pump coupled to cytochrome c oxidase in mitochondria
    • Wikström, M. (1977) Proton pump coupled to cytochrome c oxidase in mitochondria, Nature 266, 271-273.
    • (1977) Nature , vol.266 , pp. 271-273
    • Wikström, M.1
  • 5
    • 0032562214 scopus 로고    scopus 로고
    • Role of the Pathway through K(I-362) in Proton transfer in cytochrome c oxidase from R. sphaeroides
    • Ädelroth, P., Gennis, R. B., and Brzezinski, P. (1998) Role of the Pathway through K(I-362) in Proton transfer in cytochrome c oxidase from R. sphaeroides, Biochemistry 37, 2470-2476.
    • (1998) Biochemistry , vol.37 , pp. 2470-2476
    • Ädelroth, P.1    Gennis, R.B.2    Brzezinski, P.3
  • 6
    • 0031880698 scopus 로고    scopus 로고
    • The coupling of electron transfer and proton translocation: Electrostatic calculations on Paracoccus denitrificans cytochrome c oxidase
    • Kannt, A., Lancaster, C. R. D., and Michel, H. (1998) The coupling of electron transfer and proton translocation: electrostatic calculations on Paracoccus denitrificans cytochrome c oxidase, Biophys. J. 74, 708-721.
    • (1998) Biophys. J. , vol.74 , pp. 708-721
    • Kannt, A.1    Lancaster, C.R.D.2    Michel, H.3
  • 7
    • 0033524476 scopus 로고    scopus 로고
    • Proton exit from the heme-copper oxidase of Escherichia coli
    • Puustinen, A. and Wikström, M. (1999) Proton exit from the heme-copper oxidase of Escherichia coli, Proc. Natl. Acad. Sci. U.S.A. 96, 35-37.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 35-37
    • Puustinen, A.1    Wikström, M.2
  • 9
    • 0034673188 scopus 로고    scopus 로고
    • Functional properties of the heme propionates in cytochrome c oxidase from Paracoccus denitrificans. Evidence from FTIR difference spectroscopy and site-directed mutagenesis
    • Behr, J., Michel, H., Mäntele, W., and Hellwig, P. (2000) Functional properties of the heme propionates in cytochrome c oxidase from Paracoccus denitrificans. Evidence from FTIR difference spectroscopy and site-directed mutagenesis, Biochemistry 39, 1356-1363.
    • (2000) Biochemistry , vol.39 , pp. 1356-1363
    • Behr, J.1    Michel, H.2    Mäntele, W.3    Hellwig, P.4
  • 10
    • 0028890031 scopus 로고
    • Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans
    • Iwata, S., Ostermeier, C., Ludwig, B., and Michel, H. (1995) Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans, Nature 376, 660-669.
    • (1995) Nature , vol.376 , pp. 660-669
    • Iwata, S.1    Ostermeier, C.2    Ludwig, B.3    Michel, H.4
  • 12
    • 0030761382 scopus 로고    scopus 로고
    • Substitutions of charged amino acid residues conserved in subunit I perturb the redox metal centers of the Escherichia coli bo-type ubiquinol oxidase
    • Kawasaki, M., Mogi, T., and Anraku, Y. (1997) Substitutions of charged amino acid residues conserved in subunit I perturb the redox metal centers of the Escherichia coli bo-type ubiquinol oxidase, J. Biochem. 122, 422-429.
    • (1997) J. Biochem. , vol.122 , pp. 422-429
    • Kawasaki, M.1    Mogi, T.2    Anraku, Y.3
  • 13
    • 0037056047 scopus 로고    scopus 로고
    • Influence of structure, pH and membrane potential on proton movement in cytochrome oxidase
    • Mills, D. A. and Ferguson-Miller, S. (2002) Influence of structure, pH and membrane potential on proton movement in cytochrome oxidase, Biochim. Biophys. Acta 1555, 96-100.
    • (2002) Biochim. Biophys. Acta , vol.1555 , pp. 96-100
    • Mills, D.A.1    Ferguson-Miller, S.2
  • 15
    • 23244459036 scopus 로고    scopus 로고
    • The protonation state of a heme propionate controls electron transfer in cytochrome c oxidase
    • Brändén, G., Brändén, M., Schmidt, B., Mills, D. A., Ferguson-Miller, S., and Brzezinski, P. (2005) The protonation state of a heme propionate controls electron transfer in cytochrome c oxidase, Biochemistry 44, 10466-10474.
    • (2005) Biochemistry , vol.44 , pp. 10466-10474
    • Brändén, G.1    Brändén, M.2    Schmidt, B.3    Mills, D.A.4    Ferguson-Miller, S.5    Brzezinski, P.6
  • 16
    • 23244466489 scopus 로고    scopus 로고
    • An arginine to lysine mutation in the vicinity of the heme propionates affects the redox potentials of the hemes and associated electron and proton transfer in cytochrome c oxidase
    • Mills, D. A., Geren, L., Hiser, C., Schmidt, B., Durham, B., Millett, F., and Ferguson-Miller, S. (2005) An arginine to lysine mutation in the vicinity of the heme propionates affects the redox potentials of the hemes and associated electron and proton transfer in cytochrome c oxidase, Biochemistry 44, 10457-10465.
    • (2005) Biochemistry , vol.44 , pp. 10457-10465
    • Mills, D.A.1    Geren, L.2    Hiser, C.3    Schmidt, B.4    Durham, B.5    Millett, F.6    Ferguson-Miller, S.7
  • 18
    • 0024962043 scopus 로고
    • Cytochrome o(bo) is a Proton Pump in Paracoccus denitrificans and Escherichia coli
    • Puustinen, A., Finel, M., Virkki, M., and Wikström, M. (1989) Cytochrome o(bo) is a Proton Pump in Paracoccus denitrificans and Escherichia coli, FEBS Lett. 249, 163-167.
    • (1989) FEBS Lett. , vol.249 , pp. 163-167
    • Puustinen, A.1    Finel, M.2    Virkki, M.3    Wikström, M.4
  • 19
    • 0029101114 scopus 로고
    • Reconstitution of membrane proteins into liposomes: Application to energy-transducing membrane proteins
    • Rigaud, J. L., Pitard, B., and Levy, D. (1995) Reconstitution of membrane proteins into liposomes: application to energy-transducing membrane proteins, Biochim. Biophys. Acta 1231, 223-246.
    • (1995) Biochim. Biophys. Acta , vol.1231 , pp. 223-246
    • Rigaud, J.L.1    Pitard, B.2    Levy, D.3
  • 20
    • 0034636796 scopus 로고    scopus 로고
    • Proton translocation by cytochrome c oxidase can take place without the conserved glutamic acid in subunit I
    • Backgren, C., Hummer, G., Wikström, M., and Puustinen, A. (2000) Proton translocation by cytochrome c oxidase can take place without the conserved glutamic acid in subunit I, Biochemistry 39, 7863-7867.
    • (2000) Biochemistry , vol.39 , pp. 7863-7867
    • Backgren, C.1    Hummer, G.2    Wikström, M.3    Puustinen, A.4
  • 22
    • 0033514982 scopus 로고    scopus 로고
    • Assignment and charge translocation stoichiometries of the major electrogenic phases in the reaction of cytochrome c oxidase with dioxygen
    • Jasaitis, A., Verkhovsky, M. I., Morgan, J. E., Verkhovskaya, M. L., and Wikström, M. (1999) Assignment and charge translocation stoichiometries of the major electrogenic phases in the reaction of cytochrome c oxidase with dioxygen, Biochemistry 38, 2697-2706.
    • (1999) Biochemistry , vol.38 , pp. 2697-2706
    • Jasaitis, A.1    Verkhovsky, M.I.2    Morgan, J.E.3    Verkhovskaya, M.L.4    Wikström, M.5
  • 23
    • 0026496717 scopus 로고
    • Intramolecular electron transfer in cytochrome c oxidase: A cascade of equilibria
    • Verkhovsky, M. I., Morgan, J. E., and Wikström, M. (1992) Intramolecular electron transfer in cytochrome c oxidase: a cascade of equilibria, Biochemistry 31, 11860-11863.
    • (1992) Biochemistry , vol.31 , pp. 11860-11863
    • Verkhovsky, M.I.1    Morgan, J.E.2    Wikström, M.3
  • 24
    • 0000825077 scopus 로고
    • Reactions of cytochrome oxidase with oxygen and carbon monoxide
    • Gibson, Q. H. and Greenwood, C. (1963) Reactions of cytochrome oxidase with oxygen and carbon monoxide, Biochem. J. 86, 541-554.
    • (1963) Biochem. J. , vol.86 , pp. 541-554
    • Gibson, Q.H.1    Greenwood, C.2
  • 25
    • 0034732967 scopus 로고    scopus 로고
    • 2 and its reduction are both retarded by replacement of valine 279 by isoleucine in cytochrome c oxidase from Paracoccus denitrificans
    • 2 and its reduction are both retarded by replacement of valine 279 by isoleucine in cytochrome c oxidase from Paracoccus denitrificans, Biochemistry 39, 6365-6372.
    • (2000) Biochemistry , vol.39 , pp. 6365-6372
    • Riistama, S.1    Puustinen, A.2    Verkhovsky, M.I.3    Morgan, J.E.4    Wikström, M.5
  • 26
    • 0041846657 scopus 로고    scopus 로고
    • M and F intermediates of bovine and Paracoccus denitrificans cytochrome c oxidase
    • M and F intermediates of bovine and Paracoccus denitrificans cytochrome c oxidase, Biochemistry 42, 8809-8817.
    • (2003) Biochemistry , vol.42 , pp. 8809-8817
    • Iwaki, M.1    Puustinen, A.2    Wikström, M.3    Rich, P.R.4
  • 30
    • 0000336683 scopus 로고
    • Regularization Techniques for Inverse Problems in Molecular Biology
    • Deuflhard, P. and Hairer, E., Eds. Birkhauser, Boston
    • Provencher, S. W., and Vogel, R. H. (1983) Regularization Techniques for Inverse Problems in Molecular Biology, in Progress in Scientific Computing (Deuflhard, P. and Hairer, E., Eds.) pp 304-319, Birkhauser, Boston.
    • (1983) Progress in Scientific Computing , pp. 304-319
    • Provencher, S.W.1    Vogel, R.H.2
  • 33
    • 0344618240 scopus 로고    scopus 로고
    • Fourier transform infrared spectroscopy of enzyme systems
    • Mantsch, H. H., Chapman, D., Eds. John Wiley & Sons, Inc., Publications, New York
    • Alben, J. O. (1996) Fourier transform infrared spectroscopy of enzyme systems, in Infrared Spectroscopy of Biomolecules (Mantsch, H. H., Chapman, D., Eds.) pp 19-37, John Wiley & Sons, Inc., Publications, New York.
    • (1996) Infrared Spectroscopy of Biomolecules , pp. 19-37
    • Alben, J.O.1
  • 34
    • 0029884379 scopus 로고    scopus 로고
    • Carboxyl group protonation upon reduction of the Paracoccus denitrificans cytochrome c oxidase: Direct evidence by FTIR spectroscopy
    • Hellwig, P. (1996) Carboxyl group protonation upon reduction of the Paracoccus denitrificans cytochrome c oxidase: direct evidence by FTIR spectroscopy, FEBS 385, 53-57.
    • (1996) FEBS , vol.385 , pp. 53-57
    • Hellwig, P.1
  • 36
    • 0035519279 scopus 로고    scopus 로고
    • Ultrafast haem-haem electron transfer in cytochrome c oxidase
    • Verkhovsky, M. I., Jasaitis, A., and Wikström, M. (2001) Ultrafast haem-haem electron transfer in cytochrome c oxidase, Biochim. Biophys. Acta 1506, 143-146.
    • (2001) Biochim. Biophys. Acta , vol.1506 , pp. 143-146
    • Verkhovsky, M.I.1    Jasaitis, A.2    Wikström, M.3
  • 37
    • 9244257845 scopus 로고    scopus 로고
    • Electron transfer between hemes in mammalian cytochrome c oxidase
    • Pilet, E., Jasaitis, A., Liebl, U., and Vos, M. H. (2004) Electron transfer between hemes in mammalian cytochrome c oxidase, Proc. Natl. Acad. Sci. U.S.A. 101, 16198-16203.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 16198-16203
    • Pilet, E.1    Jasaitis, A.2    Liebl, U.3    Vos, M.H.4
  • 39
    • 0027380681 scopus 로고
    • Site-directed mutagenesis of highly conserved residues in helix VIII of subunit I of the cytochrome bo ubiquinol oxidase from Escherichia coli: An amphipathic transmembrane helix that may be important in conveying protons to the binuclear center
    • Thomas, J. W., Puustinen, A., Alben, J. O., Gennis, R. B., and Wikström, M. (1993) Site-directed mutagenesis of highly conserved residues in helix VIII of subunit I of the cytochrome bo ubiquinol oxidase from Escherichia coli: An amphipathic transmembrane helix that may be important in conveying protons to the binuclear center, Biochemistry 32, 10923-10928.
    • (1993) Biochemistry , vol.32 , pp. 10923-10928
    • Thomas, J.W.1    Puustinen, A.2    Alben, J.O.3    Gennis, R.B.4    Wikström, M.5
  • 41
    • 0039242661 scopus 로고
    • Energy-dependent reversal of the cytochrome oxidase reaction
    • Wikström, M. (1981) Energy-dependent reversal of the cytochrome oxidase reaction, Proc. Natl. Acad. Sci. U.S.A. 78, 4051-4054.
    • (1981) Proc. Natl. Acad. Sci. U.S.A. , vol.78 , pp. 4051-4054
    • Wikström, M.1
  • 42
    • 0021763113 scopus 로고
    • The reaction of fully reduced cytochrome c oxidase with oxygen studied by flow-flash spectrophotometry at room temperature
    • Hill, B. C. and Greenwood, C. (1984) The reaction of fully reduced cytochrome c oxidase with oxygen studied by flow-flash spectrophotometry at room temperature, Biochem. J. 218, 913-921.
    • (1984) Biochem. J. , vol.218 , pp. 913-921
    • Hill, B.C.1    Greenwood, C.2
  • 43
    • 0029775911 scopus 로고    scopus 로고
    • Observation and assignment of peroxy and ferryl intermediates in the reduction of dioxygen to water by cytochrome c oxidase
    • Morgan, J. E., Verkhovsky, M. I., and Wikström, M. (1996) Observation and assignment of peroxy and ferryl intermediates in the reduction of dioxygen to water by cytochrome c oxidase, Biochemistry 35, 12235-12240.
    • (1996) Biochemistry , vol.35 , pp. 12235-12240
    • Morgan, J.E.1    Verkhovsky, M.I.2    Wikström, M.3
  • 45
    • 0343580460 scopus 로고    scopus 로고
    • 3 from Rhodobacter sphaeroides is involved in proton uptake during the reaction of the fully reduced enzyme with dioxygen
    • 3 from Rhodobacter sphaeroides is involved in proton uptake during the reaction of the fully reduced enzyme with dioxygen, Biochemistry 36, 13824-13829.
    • (1997) Biochemistry , vol.36 , pp. 13824-13829
    • Ädelroth, P.1    Svensson, E.M.2    Mitchell, D.M.3    Gennis, R.B.4    Brzezinski, P.5
  • 46
    • 0001805270 scopus 로고    scopus 로고
    • The reactions of hydrogen peroxide with bovine cytochrome c oxidase
    • Junemann, S., Heathcote, P., and Rich, P. R. (2000) The reactions of hydrogen peroxide with bovine cytochrome c oxidase, Biochim. Biophys. Acta 1456, 56-66.
    • (2000) Biochim. Biophys. Acta , vol.1456 , pp. 56-66
    • Junemann, S.1    Heathcote, P.2    Rich, P.R.3
  • 47
    • 0035859920 scopus 로고    scopus 로고
    • Role of the K-channel in the pH-dependence of the reaction of cytochrome c oxidase with hydrogen peroxide
    • Pecoraro, C., Gennis, R. B., Vygodina, T. V., and Konstantinov, A. A. (2001) Role of the K-channel in the pH-dependence of the reaction of cytochrome c oxidase with hydrogen peroxide, Biochemistry 40, 9695-9708.
    • (2001) Biochemistry , vol.40 , pp. 9695-9708
    • Pecoraro, C.1    Gennis, R.B.2    Vygodina, T.V.3    Konstantinov, A.A.4
  • 48
    • 0028263983 scopus 로고
    • Cytochrome bo from Escherichia coli: Reaction of the oxidized enzyme with hydrogen peroxide
    • Watmough, N. J., Cheesman, M. R., Greenwood, C., and Thomson, A. J. (1994) Cytochrome bo from Escherichia coli: Reaction of the oxidized enzyme with hydrogen peroxide, Biochem. J. 300, 469-475.
    • (1994) Biochem. J. , vol.300 , pp. 469-475
    • Watmough, N.J.1    Cheesman, M.R.2    Greenwood, C.3    Thomson, A.J.4
  • 50
    • 0028109925 scopus 로고
    • The reaction of hydrogen peroxide with pulsed cytochrome bo from Escherichia coli
    • Moody, A. J. and Rich, P. R. (1994) The reaction of hydrogen peroxide with pulsed cytochrome bo from Escherichia coli, Eur. J. Biochem. 226, 731-737.
    • (1994) Eur. J. Biochem. , vol.226 , pp. 731-737
    • Moody, A.J.1    Rich, P.R.2
  • 51
    • 0024346661 scopus 로고
    • 2-induced conversion of cytochrome c oxidase peroxy complex to oxoferryl state
    • 2-induced conversion of cytochrome c oxidase peroxy complex to oxoferryl state, Ann. NY Acad. Sci. 550, 124-138.
    • (1988) Ann. NY Acad. Sci. , vol.550 , pp. 124-138
    • Vygodina, T.V.1    Konstantinov, A.A.2
  • 52
    • 0022966751 scopus 로고
    • Kinetic investigations of cytochrome c oxidase with hydrogen peroxide
    • Gorren, A. C. F., Dekker, H., and Wever, R. (1986) Kinetic investigations of cytochrome c oxidase with hydrogen peroxide, Biochim. Biophys. Acta 852, 1-92.
    • (1986) Biochim. Biophys. Acta , vol.852 , pp. 1-92
    • Gorren, A.C.F.1    Dekker, H.2    Wever, R.3
  • 53
    • 0025787382 scopus 로고
    • Reaction of hydrogen peroxide with the rapid form of resting cytochrome oxidase
    • Weng, L., and Baker, G. M. (1991) Reaction of hydrogen peroxide with the rapid form of resting cytochrome oxidase, Biochemistry 30, 5727-5733.
    • (1991) Biochemistry , vol.30 , pp. 5727-5733
    • Weng, L.1    Baker, G.M.2
  • 54
    • 0024515840 scopus 로고
    • Effect of pH on the spectrum of cytochrome c oxidase hydrogen peroxide complex
    • Vygodina, T., and Konstantinov, A. (1989) Effect of pH on the spectrum of cytochrome c oxidase hydrogen peroxide complex, Biochim. Biophys. Acta 973, 390-398.
    • (1989) Biochim. Biophys. Acta , vol.973 , pp. 390-398
    • Vygodina, T.1    Konstantinov, A.2
  • 55
    • 0035852827 scopus 로고    scopus 로고
    • Proton involvement in the transition from the "peroxy" to the ferryl intermediate of cytochrome c oxidase
    • Fabian, M., and Palmer, G. (2001) Proton involvement in the transition from the "peroxy" to the ferryl intermediate of cytochrome c oxidase, Biochemistry 40, 1867-1874.
    • (2001) Biochemistry , vol.40 , pp. 1867-1874
    • Fabian, M.1    Palmer, G.2
  • 56
    • 0026530174 scopus 로고
    • Oxygen activation and the conservation of energy in cell respiration
    • Babcock, G. T., and Wikström, M. (1992) Oxygen activation and the conservation of energy in cell respiration, Nature 356, 301-309.
    • (1992) Nature , vol.356 , pp. 301-309
    • Babcock, G.T.1    Wikström, M.2
  • 57
    • 0031559894 scopus 로고    scopus 로고
    • Role of water in the proton translocation mechanism of the haem-copper oxidases
    • Riistama, S., Hummer, G., Puustinen, A., Dyer, R. B., Woodruff, W. H., and Wikström, M. (1997) Role of water in the proton translocation mechanism of the haem-copper oxidases, FEBS Lett. 414, 275-280.
    • (1997) FEBS Lett. , vol.414 , pp. 275-280
    • Riistama, S.1    Hummer, G.2    Puustinen, A.3    Dyer, R.B.4    Woodruff, W.H.5    Wikström, M.6
  • 58
    • 0031973948 scopus 로고    scopus 로고
    • Oxygen and proton pathways in cytochrome c oxidase
    • Hofacker, I., and Schulten, K. (1998) Oxygen and proton pathways in cytochrome c oxidase, Proteins 30, 100-107.
    • (1998) Proteins , vol.30 , pp. 100-107
    • Hofacker, I.1    Schulten, K.2
  • 59
    • 0032311173 scopus 로고    scopus 로고
    • Structure and dynamics of a proton shuttle in cytochrome c oxidase
    • Pomes, R., Hummer, G., and Wikström, M. (1998) Structure and dynamics of a proton shuttle in cytochrome c oxidase, Biochim. Biophys. Acta 1365, 255-260.
    • (1998) Biochim. Biophys. Acta , vol.1365 , pp. 255-260
    • Pomes, R.1    Hummer, G.2    Wikström, M.3
  • 60
    • 16344363592 scopus 로고    scopus 로고
    • Simulating redox coupled proton transfer in cytochrome c oxidase: Looking for the proton bottleneck
    • Olsson, M. H. M., Sharma, P. K., and Warshel, A. (2005) Simulating redox coupled proton transfer in cytochrome c oxidase: Looking for the proton bottleneck, FEBS Lett. 579, 2026-2034.
    • (2005) FEBS Lett. , vol.579 , pp. 2026-2034
    • Olsson, M.H.M.1    Sharma, P.K.2    Warshel, A.3
  • 62
    • 0033602933 scopus 로고    scopus 로고
    • Aspartate-132 in cytochrome c oxidase from Rhodobacter sphaeroides is involved in a two-step proton transfer during oxo-ferryl formation
    • Smirnova, I., Ädelroth, P., Gennis, R. B., and Brzezinski, P. (1999) Aspartate-132 in cytochrome c oxidase from Rhodobacter sphaeroides is involved in a two-step proton transfer during oxo-ferryl formation, Biochemistry 38, 6826-6833.
    • (1999) Biochemistry , vol.38 , pp. 6826-6833
    • Smirnova, I.1    Ädelroth, P.2    Gennis, R.B.3    Brzezinski, P.4


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