메뉴 건너뛰기




Volumn 321, Issue 2, 2002, Pages 329-339

The X-ray crystal structures of wild-type and EQ(I-286) mutant cytochrome c oxidases from Rhodobacter sphaeroides

Author keywords

Cytochrome c oxidase; Membrane protein; Terminal oxidases; X ray crystallography

Indexed keywords

BACTERIAL ENZYME; CYTOCHROME C OXIDASE; OXYGEN; PROTON PUMP; WATER;

EID: 0036382724     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(02)00619-8     Document Type: Article
Times cited : (486)

References (62)
  • 1
    • 0028890031 scopus 로고
    • Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans
    • Iwata, S., Ostermeier, C., Ludwig, B. & 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
  • 2
    • 0029652024 scopus 로고
    • Structures of metal sites of oxidized bovine heart cytochrome c oxidase at 2.8 Å
    • Tsukihara, T., Aoyama, H., Yamashita, E., Tomizaki, T., Yamaguchi, H., Shinzawa-Itoh, K. et al. (1995). Structures of metal sites of oxidized bovine heart cytochrome c oxidase at 2.8 Å. Science, 269, 1069-1074.
    • (1995) Science , vol.269 , pp. 1069-1074
    • Tsukihara, T.1    Aoyama, H.2    Yamashita, E.3    Tomizaki, T.4    Yamaguchi, H.5    Shinzawa-Itoh, K.6
  • 3
    • 0030886203 scopus 로고    scopus 로고
    • Structure at 2.7 Å resolution of the Paracoccus denitrificans two-subunit cytochrome c oxidase complexed with an antibody FV fragment
    • Ostermeier, C., Harrenga, A., Ermler, U. & Michel, H. (1997). Structure at 2.7 Å resolution of the Paracoccus denitrificans two-subunit cytochrome c oxidase complexed with an antibody FV fragment. Proc. Natl Acad. Sci. USA, 94, 10547-10553.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 10547-10553
    • Ostermeier, C.1    Harrenga, A.2    Ermler, U.3    Michel, H.4
  • 4
    • 18144447465 scopus 로고    scopus 로고
    • Redox-coupled crystal structural changes in bovine heart cytochrome c oxidase
    • Yoshikawa, S., Shinzawa-Itoh, K., Nakashima, R., Yaono, R., Yamashita, E., Inoue, N. et al. (1998). Redox-coupled crystal structural changes in bovine heart cytochrome c oxidase. Science, 280, 1723-1729.
    • (1998) Science , vol.280 , pp. 1723-1729
    • Yoshikawa, S.1    Shinzawa-Itoh, K.2    Nakashima, R.3    Yaono, R.4    Yamashita, E.5    Inoue, N.6
  • 5
    • 0033585083 scopus 로고    scopus 로고
    • The cytochrome c oxidase from Paracoccus denitrificans does not change the metal center ligation upon reduction
    • Harrenga, A. & Michel, H. (1999). The cytochrome c oxidase from Paracoccus denitrificans does not change the metal center ligation upon reduction. J. Biol. Chem. 274, 33296-33299.
    • (1999) J. Biol. Chem. , vol.274 , pp. 33296-33299
    • Harrenga, A.1    Michel, H.2
  • 6
    • 0034696637 scopus 로고    scopus 로고
    • Mutations in the putative H-channel in the cytochrome c oxidase from Rhodobacter sphaeroides show that this channel is not important for proton conduction but reveal modulation of the properties of heme a
    • Lee, H. M., Das, T. K., Rousseau, D. L., Mills, D., Ferguson-Miller, S. & Gennis, R. B. (2000). Mutations in the putative H-channel in the cytochrome c oxidase from Rhodobacter sphaeroides show that this channel is not important for proton conduction but reveal modulation of the properties of heme a. Biochemistry, 39, 2989-2996.
    • (2000) Biochemistry , vol.39 , pp. 2989-2996
    • Lee, H.M.1    Das, T.K.2    Rousseau, D.L.3    Mills, D.4    Ferguson-Miller, S.5    Gennis, R.B.6
  • 7
    • 0034640504 scopus 로고    scopus 로고
    • Proton pumping by cytochrome oxidase: Progress, problems and postulates
    • Zaslavsky, D. & Gennis, R. B. (2000). Proton pumping by cytochrome oxidase: Progress, problems and postulates. Biochim. Biophys. Acta, 1458, 164-179.
    • (2000) Biochim. Biophys. Acta , vol.1458 , pp. 164-179
    • Zaslavsky, D.1    Gennis, R.B.2
  • 8
    • 0031744648 scopus 로고    scopus 로고
    • Pathways of proton transfer in cytochrome c oxidase
    • Brzezinski, P. & Adelroth, P. (1998). Pathways of proton transfer in cytochrome c oxidase. J. Bioenerg. Biomembr. 30, 99-107.
    • (1998) J. Bioenerg. Biomembr. , vol.30 , pp. 99-107
    • Brzezinski, P.1    Adelroth, P.2
  • 9
    • 0033539479 scopus 로고    scopus 로고
    • Mass spectrometric determination of dioxygen bond splitting in the "peroxy" intermediate of cytochrome c oxidase
    • Fabian, M., Wong, W. W., Gennis, R. B. & Palmer, G. (1999). Mass spectrometric determination of dioxygen bond splitting in the "peroxy" intermediate of cytochrome c oxidase. Proc. Natl Acad. Sci. USA, 96, 13114-13117.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 13114-13117
    • Fabian, M.1    Wong, W.W.2    Gennis, R.B.3    Palmer, G.4
  • 10
    • 0031744886 scopus 로고    scopus 로고
    • Time-resolved resonance Raman investigation of oxygen reduction mechanism of bovine cytochrome c oxidase
    • Kitagawa, T. & Ogura, T. (1998). Time-resolved resonance Raman investigation of oxygen reduction mechanism of bovine cytochrome c oxidase. J. Bioenerg. Biomembr. 30, 71-79.
    • (1998) J. Bioenerg. Biomembr. , vol.30 , pp. 71-79
    • Kitagawa, T.1    Ogura, T.2
  • 11
    • 0030013601 scopus 로고    scopus 로고
    • 2concentration dependence
    • Proshlyakov, D. A., Ogura, T., Shinzawa-Itoh, K., Yoshikawa, S. & Kitagawa, T. (1996). Resonance Raman/absorption characterization of the oxo intermediates of cytochrome c oxidase generated in its reaction with hydrogen peroxide: pH and H2O2 concentration dependence. Biochemistry, 35, 8580-8586.
    • (1996) Biochemistry , vol.35 , pp. 8580-8586
    • Proshlyakov, D.A.1    Ogura, T.2    Shinzawa-Itoh, K.3    Yoshikawa, S.4    Kitagawa, T.5
  • 12
    • 0032493345 scopus 로고    scopus 로고
    • Dioxygen activation and bond cleavage by mixed-valence cytochrome c oxidase
    • Proshlyakov, D. A., Pressler, M. A. & Babcock, G. T. (1998). Dioxygen activation and bond cleavage by mixed-valence cytochrome c oxidase. Proc. Natl Acad. Sci. USA, 95, 8020-8025.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 8020-8025
    • Proshlyakov, D.A.1    Pressler, M.A.2    Babcock, G.T.3
  • 13
    • 0028263983 scopus 로고
    • Cytochrome bo from Escherichia coli: Reaction of the oxidized enzyme with hydrogen peroxide
    • Watmough, N. J., Cheesman, M. R., Greenwood, C. & 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
  • 14
    • 0034711407 scopus 로고    scopus 로고
    • Oxygen activation and reduction in respiration: Involvement of redox-active tyrosine 244
    • Proshlyakov, D. A., Pressler, M. A., DeMaso, C., Leykam, J. F., DeWitt, D. L. & Babcock, G. T. (2000). Oxygen activation and reduction in respiration: involvement of redox-active tyrosine 244. Science, 290, 1588-1591.
    • (2000) Science , vol.290 , pp. 1588-1591
    • Proshlyakov, D.A.1    Pressler, M.A.2    DeMaso, C.3    Leykam, J.F.4    DeWitt, D.L.5    Babcock, G.T.6
  • 16
    • 0033576277 scopus 로고    scopus 로고
    • Cytochrome c oxidase: Catalytic cycle and mechanisms of proton pumping - A discussion
    • Michel, H. (1999). Cytochrome c oxidase: catalytic cycle and mechanisms of proton pumping-a discussion. Biochemistry, 38, 15129-15140.
    • (1999) Biochemistry , vol.38 , pp. 15129-15140
    • Michel, H.1
  • 18
    • 0034640452 scopus 로고    scopus 로고
    • Mechanism of proton translocation by cytochrome c oxidase: A new four-stroke histidine cycle
    • Wikström, M. (2000). Mechanism of proton translocation by cytochrome c oxidase: a new four-stroke histidine cycle. Biochim. Biophys. Acta, 1458, 188-198.
    • (2000) Biochim. Biophys. Acta , vol.1458 , pp. 188-198
    • Wikström, M.1
  • 19
    • 0025879301 scopus 로고
    • Subunit III of cytochrome c oxidase is not involved in proton translocation: A site-directed mutagenesis study
    • Haltia, T., Saraste, M. & Wikström, M. (1991). Subunit III of cytochrome c oxidase is not involved in proton translocation: a site-directed mutagenesis study. EMBO J. 10, 2015-2021.
    • (1991) EMBO J , vol.10 , pp. 2015-2021
    • Haltia, T.1    Saraste, M.2    Wikström, M.3
  • 20
    • 0033534165 scopus 로고    scopus 로고
    • Suicide inactivation of cytochrome c oxidase: Catalytic turnover in the absence of subunit III alters the active site
    • Bratton, M. R., Pressler, M. A. & Hosler, J. P. (1999). Suicide inactivation of cytochrome c oxidase: catalytic turnover in the absence of subunit III alters the active site. Biochemistry, 38, 16236-16245.
    • (1999) Biochemistry , vol.38 , pp. 16236-16245
    • Bratton, M.R.1    Pressler, M.A.2    Hosler, J.P.3
  • 22
    • 0034654622 scopus 로고    scopus 로고
    • Insights into the functional role of the tyrosine-histidine linkage in cytochrome c oxidase
    • McCauley, K. M., Vrtis, J. M., Dupont, J. & Donk, W. A. v. d. (2000). Insights into the functional role of the tyrosine-histidine linkage in cytochrome c oxidase. J. Am. Chem. Soc. 122, 2403-2404.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 2403-2404
    • McCauley, K.M.1    Vrtis, J.M.2    Dupont, J.3    Donk, W.A.V.D.4
  • 23
    • 0033600912 scopus 로고    scopus 로고
    • Mutants that alter the covalent structure of catalase hydroperoxidase II from Escherichia coli
    • Mate, M. J., Sevinc, M. S., Hu, B., Bujons, J., Bravo, J., Switala, J. et al. (1999). Mutants that alter the covalent structure of catalase hydroperoxidase II from Escherichia coli. J. Biol. Chem. 274, 27717-27725.
    • (1999) J. Biol. Chem. , vol.274 , pp. 27717-27725
    • Mate, M.J.1    Sevinc, M.S.2    Hu, B.3    Bujons, J.4    Bravo, J.5    Switala, J.6
  • 26
    • 0033019674 scopus 로고    scopus 로고
    • Structural dynamics of ligand diffusion in the protein matrix: A study on a new myoglobin mutant Y(B10) Q(E7) R(E10)
    • Brunori, M., Cutruzzola, F., Savino, C., Travaglini-Allocatelli, C., Vallone, B. & Gibson, Q. H. (1999). Structural dynamics of ligand diffusion in the protein matrix: a study on a new myoglobin mutant Y(B10) Q(E7) R(E10). Biophys. J. 76, 1259-1269.
    • (1999) Biophys. J. , vol.76 , pp. 1259-1269
    • Brunori, M.1    Cutruzzola, F.2    Savino, C.3    Travaglini-Allocatelli, C.4    Vallone, B.5    Gibson, Q.H.6
  • 28
    • 0031973948 scopus 로고    scopus 로고
    • Oxygen and proton pathways in cytochrome c oxidase
    • Hofacker, I. & Schulten, K. (1998). Oxygen and proton pathways in cytochrome c oxidase. Proteins: Struct. Funct. Genet. 30, 100-107.
    • (1998) Proteins: Struct. Funct. Genet. , vol.30 , pp. 100-107
    • Hofacker, I.1    Schulten, K.2
  • 31
    • 0033524476 scopus 로고    scopus 로고
    • Proton exit from the heme-copper oxidase of Escherichia coli
    • Puustinen, A. & Wikström, M. (1999). Proton exit from the heme-copper oxidase of Escherichia coli. Proc. Natl Acad. Sci. USA, 96, 35-37.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 35-37
    • Puustinen, A.1    Wikström, M.2
  • 32
    • 0034640332 scopus 로고    scopus 로고
    • Where is "outside" in cytochrome c oxidase and how and when do protons get there?
    • Mills, D. A., Florens, L., Hiser, C., Qian, J. & Ferguson-Miller, S. (2000). Where is "outside" in cytochrome c oxidase and how and when do protons get there? Biochim. Biophys. Acta, 1458, 180-187.
    • (2000) Biochim. Biophys. Acta , vol.1458 , pp. 180-187
    • Mills, D.A.1    Florens, L.2    Hiser, C.3    Qian, J.4    Ferguson-Miller, S.5
  • 34
    • 0032562214 scopus 로고    scopus 로고
    • Role of the pathway through K(I-362) in proton transfer in cytochrome c oxidase from R. sphaeroides
    • Adelroth, P., Gennis, R. B. & 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
    • Adelroth, P.1    Gennis, R.B.2    Brzezinski, P.3
  • 36
    • 0031880698 scopus 로고    scopus 로고
    • The coupling of electron transfer and proton translocation: Electrostatic calculations on Paracoccus denitrificans cytochrome c oxidase
    • Kannt, A., Roy, C., Lancaster, D. & 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    Roy, C.2    Lancaster, D.3    Michel, H.4
  • 38
    • 0034643829 scopus 로고    scopus 로고
    • Localized control of proton transfer through the D-pathway in cytochrome c oxidase: Application of the proton-inventory technique
    • Karpefors, M., Adelroth, P. & Brzezinski, P. (2000). Localized control of proton transfer through the D-pathway in cytochrome c oxidase: application of the proton-inventory technique. Biochemistry, 39, 6850-6856.
    • (2000) Biochemistry , vol.39 , pp. 6850-6856
    • Karpefors, M.1    Adelroth, P.2    Brzezinski, P.3
  • 39
    • 0032311173 scopus 로고    scopus 로고
    • Structure and dynamics of a proton shuttle in cytochrome c oxidase
    • Pomes, R., Hummer, G. & 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
  • 40
    • 0034663494 scopus 로고    scopus 로고
    • The role of the D-and K-pathways of proton transfer in the function of the haem-copper oxidases
    • Wikström, M., Jasaitis, A., Backgren, C., Puustinen, A. & Verkhovsky, M. I. (2000). The role of the D-and K-pathways of proton transfer in the function of the haem-copper oxidases. Biochim. Biophys. Acta, 1459, 514-520.
    • (2000) Biochim. Biophys. Acta , vol.1459 , pp. 514-520
    • Wikström, M.1    Jasaitis, A.2    Backgren, C.3    Puustinen, A.4    Verkhovsky, M.I.5
  • 41
    • 0034663652 scopus 로고    scopus 로고
    • Proton transfer from glutamate 286 determines the transition rates between oxygen intermediates in cytochrome c oxidase
    • Ådelroth, P., Karpefors, M., Gilderson, G., Tomson, F. L., Gennis, R. B. & Brzezinski, P. (2000). Proton transfer from glutamate 286 determines the transition rates between oxygen intermediates in cytochrome c oxidase. Biochim. Biophys. Acta, 1459, 533-539.
    • (2000) Biochim. Biophys. Acta , vol.1459 , pp. 533-539
    • Ådelroth, P.1    Karpefors, M.2    Gilderson, G.3    Tomson, F.L.4    Gennis, R.B.5    Brzezinski, P.6
  • 42
    • 0029884379 scopus 로고    scopus 로고
    • Carboxyl group protonation upon reduction of the Paracoccus denitrificans cytochrome c oxidase: Direct evidence by FTIR spectroscopy
    • Hellwig, P., Rost, B., Kaiser, U., Ostermeier, C., Michel, H. & Mantele, W. (1996). Carboxyl group protonation upon reduction of the Paracoccus denitrificans cytochrome c oxidase: direct evidence by FTIR spectroscopy. FEBS Letters, 385, 53-57.
    • (1996) FEBS Letters , vol.385 , pp. 53-57
    • Hellwig, P.1    Rost, B.2    Kaiser, U.3    Ostermeier, C.4    Michel, H.5    Mantele, W.6
  • 45
    • 0343580460 scopus 로고    scopus 로고
    • 3from Rhodobacter sphaeroides is involved in proton uptake during the reaction of the fully-reduced enzyme with dioxygen
    • 3from 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
    • Ådelroth, P.1    Ek, M.S.2    Mitchell, D.M.3    Gennis, R.B.4    Brzezinski, P.5
  • 46
    • 0001357106 scopus 로고    scopus 로고
    • 3from Escherichia coli: Kinetics of electron and proton transfer
    • 3from Escherichia coli: kinetics of electron and proton transfer. Biochemistry, 36, 5425-5431.
    • (1997) Biochemistry , vol.36 , pp. 5425-5431
    • Svensson-Ek, M.1    Brzezinski, P.2
  • 47
    • 0034732967 scopus 로고    scopus 로고
    • 2and its reduction are both retarded by replacement of valine 279 by isoleucine in cytochrome c oxidase from Paracoccus denitrificans
    • 2and 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
  • 48
    • 0032143387 scopus 로고    scopus 로고
    • Proton translocation by bacteriorhodopsin and heme-copper oxidases
    • Wikström, M. (1998). Proton translocation by bacteriorhodopsin and heme-copper oxidases. Curr. Opin. Struct. Biol. 8, 480-488.
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 480-488
    • Wikström, M.1
  • 49
    • 0034719162 scopus 로고    scopus 로고
    • Redesign of the proton-pumping machinery of cytochrome c oxidase: Proton pumping does not require Glu(I-286)
    • Aagaard, A., Gilderson, G., Mills, D. A., Ferguson-Miller, S. & Brzezinski, P. (2000). Redesign of the proton-pumping machinery of cytochrome c oxidase: proton pumping does not require Glu(I-286). Biochemistry, 39, 15847-15850.
    • (2000) Biochemistry , vol.39 , pp. 15847-15850
    • Aagaard, A.1    Gilderson, G.2    Mills, D.A.3    Ferguson-Miller, S.4    Brzezinski, P.5
  • 50
    • 0035371783 scopus 로고    scopus 로고
    • A novel scenario for the evolution of haem-copper oxygen reductases
    • Pereira, M. M., Santana, M. & Teixeira, M. (2001). A novel scenario for the evolution of haem-copper oxygen reductases. Biochim. Biophys. Acta Bioenerg. 1505, 185-208.
    • (2001) Biochim. Biophys. Acta Bioenerg. , vol.1505 , pp. 185-208
    • Pereira, M.M.1    Santana, M.2    Teixeira, M.3
  • 51
    • 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. & 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
  • 52
    • 0026583053 scopus 로고
    • 3-type cytochrome c oxidase of Rhodobacter sphaeroides
    • 3-type cytochrome c oxidase of Rhodobacter sphaeroides. Mol. Microbiol. 6, 635-642.
    • (1992) Mol. Microbiol. , vol.6 , pp. 635-642
    • Shapleigh, J.P.1    Gennis, R.B.2
  • 54
    • 0032146125 scopus 로고    scopus 로고
    • Overexpression and purification of cytochrome c oxidase from Rhodobacter sphaeroides
    • Zhen, Y., Qian, J., Follmann, K., Hayward, T., Nilsson, T., Dahn, M. et al. (1998). Overexpression and purification of cytochrome c oxidase from Rhodobacter sphaeroides. Protein Expr. Purif. 13, 326-336.
    • (1998) Protein Expr. Purif. , vol.13 , pp. 326-336
    • Zhen, Y.1    Qian, J.2    Follmann, K.3    Hayward, T.4    Nilsson, T.5    Dahn, M.6
  • 56
    • 0028103275 scopus 로고
    • The CPP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, N. (1994). The CPP4 suite: programs for protein crystallography. Acta Crystallog. sect. D, 50, 760-763.
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 760-763
  • 60
    • 85001622940 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., MacArthur, M. W., Moss, D. S. & Thornton, J. M. (1993). PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallog. 26, 283-291.
    • (1993) J. Appl. Crystallog , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 61
    • 0030729838 scopus 로고    scopus 로고
    • An extensively modified version of MolScript that includes greatly enhanced coloring capabilities
    • Esnouf, R. M. (1997). An extensively modified version of MolScript that includes greatly enhanced coloring capabilities. J. Mol. Graph. Model, 15, 132-134.
    • (1997) J. Mol. Graph. Model , vol.15 , pp. 132-134
    • Esnouf, R.M.1
  • 62
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photo-realistic molecular graphics
    • Merritt, E. A. & Bacon, D. J. (1997). Raster3D: photo-realistic molecular graphics. Methods Enzymol. 277, 505-524.
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.