메뉴 건너뛰기




Volumn 44, Issue 33, 2005, Pages 10954-10965

Characterization and structural analysis of an active particulate methane monooxygenase trimer from Methylococcus capsulatus (Bath)

Author keywords

[No Author keywords available]

Indexed keywords

ELECTRON MICROSCOPY; ENZYMES; METHANOL; MONOMERS; OXIDATION; POLYPEPTIDES;

EID: 23944513777     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi050820u     Document Type: Article
Times cited : (46)

References (59)
  • 1
    • 1342287099 scopus 로고    scopus 로고
    • Methane oxidation and formation of EPS in compost: Effect of oxygen concentration
    • Wilshusen, J. H., Hettiaratchi, J. P. A., De Visscher, A., and Saint-Fort, R. (2004) Methane oxidation and formation of EPS in compost: Effect of oxygen concentration, Environ. Pollut. 129, 305-314.
    • (2004) Environ. Pollut. , vol.129 , pp. 305-314
    • Wilshusen, J.H.1    Hettiaratchi, J.P.A.2    De Visscher, A.3    Saint-Fort, R.4
  • 2
    • 0038610460 scopus 로고    scopus 로고
    • Cambridge University Press, Cambridge, U.K.
    • Intergovernmental Panel on Climate Change (2001) in Climate change 2001: The Scientific Basis, Cambridge University Press, Cambridge, U.K.
    • (2001) Climate Change 2001: The Scientific Basis
  • 3
    • 0017404563 scopus 로고
    • The soluble methane monooxygenase of Methylococcus capsulatus (Bath): Its ability to oxygenate n-akanes, n-alkenes, ethers, and acyclic, aromatic and heterocyclic compounds
    • Colby, J., Stirling, D. I., and Dalton, H. (1977) The soluble methane monooxygenase of Methylococcus capsulatus (Bath): Its ability to oxygenate n-akanes, n-alkenes, ethers, and acyclic, aromatic and heterocyclic compounds, Biochem. J. 165, 395-402.
    • (1977) Biochem. J. , vol.165 , pp. 395-402
    • Colby, J.1    Stirling, D.I.2    Dalton, H.3
  • 4
    • 0013693355 scopus 로고
    • A search for patterns in methylotrophic pathway
    • (Dalton, H., Ed.), Heyden, London
    • 1 Compounds (Dalton, H., Ed.) pp 42-54, Heyden, London.
    • (1981) 1 Compounds , pp. 42-54
    • Zatman, L.1
  • 5
    • 0000815740 scopus 로고
    • Trichloroethylene oxidation by the membrane associated methane monooxygenase in type I, II and X methanotrophs
    • DiSpirito, A. A., Gulledge, J., Shiemke, A. K., Murell, J. C., Lidstrom, M. E., and Krema, C. I. (1992) Trichloroethylene oxidation by the membrane associated methane monooxygenase in type I, II and X methanotrophs, Biodegradation 2, 151-164.
    • (1992) Biodegradation , vol.2 , pp. 151-164
    • DiSpirito, A.A.1    Gulledge, J.2    Shiemke, A.K.3    Murell, J.C.4    Lidstrom, M.E.5    Krema, C.I.6
  • 6
    • 0002548032 scopus 로고
    • The obligate methanotrophic bacteria Methylococcus, Methylosinus, Methylomonas and related bacteria
    • (Balows, A., Truper, H. G., Dworkin, M., Harder, W., and Schleifer, K. H., Eds.), Springer-Verlag, New York
    • Hanson, R. S., Netrusov, A. I., and Tsuji, K. (1991) The obligate methanotrophic bacteria Methylococcus, Methylosinus, Methylomonas and related bacteria, in The Prokaryotes (Balows, A., Truper, H. G., Dworkin, M., Harder, W., and Schleifer, K. H., Eds.) pp 2350-2365, Springer-Verlag, New York.
    • (1991) The Prokaryotes , pp. 2350-2365
    • Hanson, R.S.1    Netrusov, A.I.2    Tsuji, K.3
  • 7
    • 0025291817 scopus 로고
    • Haloalkene oxidation by the soluble methane monooxygenase from Methylosinus trichosporium OB3b: Mechanistic and environmental implications
    • Fox, B. G., Borneman, J. G., Wackett, L. P., and Lipscomb, J. D. (1990) Haloalkene oxidation by the soluble methane monooxygenase from Methylosinus trichosporium OB3b: Mechanistic and environmental implications, Biochemistry 29, 6419-6427.
    • (1990) Biochemistry , vol.29 , pp. 6419-6427
    • Fox, B.G.1    Borneman, J.G.2    Wackett, L.P.3    Lipscomb, J.D.4
  • 8
    • 0021911405 scopus 로고
    • The effect of copper ions on membrane content and methane monooxygenase activity in methanol-grown cells Methylococcus capsulatus (Bath)
    • Prior, S. D., and Dalton, H. (1985) The effect of copper ions on membrane content and methane monooxygenase activity in methanol-grown cells Methylococcus capsulatus (Bath), J. Gen. Microbiol. 131, 155-163.
    • (1985) J. Gen. Microbiol. , vol.131 , pp. 155-163
    • Prior, S.D.1    Dalton, H.2
  • 9
    • 0027913094 scopus 로고
    • Crystal-structure of a bacterial nonheme iron hydrohylase that catalyzes the biological oxidation of methane
    • Rosenzweig, A. C., Frederick, C. A., Lippard, S. J., and Nordlund, P. (1993) Crystal-structure of a bacterial nonheme iron hydrohylase that catalyzes the biological oxidation of methane, Nature 366, 537-543.
    • (1993) Nature , vol.366 , pp. 537-543
    • Rosenzweig, A.C.1    Frederick, C.A.2    Lippard, S.J.3    Nordlund, P.4
  • 10
    • 0030885887 scopus 로고    scopus 로고
    • Crystal structures of the methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath): Implications for substrate gating and component interactions
    • Rosenzweig, A. C., Brandstetter, H., Whittington, D. A., Nordlund, P., Lippard, S. J., and Frederick, C. A. (1997) Crystal structures of the methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath): Implications for substrate gating and component interactions, Proteins 29, 141-152.
    • (1997) Proteins , vol.29 , pp. 141-152
    • Rosenzweig, A.C.1    Brandstetter, H.2    Whittington, D.A.3    Nordlund, P.4    Lippard, S.J.5    Frederick, C.A.6
  • 11
    • 0034086965 scopus 로고    scopus 로고
    • Molecular biology and regulation of methane monooxygenase
    • Murrell, J. C., Gilbert, B., and McDonald, I. R. (2000) Molecular biology and regulation of methane monooxygenase, Arch. Microbiol. 173, 325-332.
    • (2000) Arch. Microbiol. , vol.173 , pp. 325-332
    • Murrell, J.C.1    Gilbert, B.2    McDonald, I.R.3
  • 12
    • 0027450659 scopus 로고
    • Soluble methane monooxygenase production and trichloroethylene degradation by type I methanotrophs Methylomonos methanica 68-1
    • Koh, S. C., Bowman, J. P., and Sayler, G. C. (1993) Soluble methane monooxygenase production and trichloroethylene degradation by type I methanotrophs Methylomonos methanica 68-1, Appl Environ. Microb. 59, 960-967.
    • (1993) Appl Environ. Microb. , vol.59 , pp. 960-967
    • Koh, S.C.1    Bowman, J.P.2    Sayler, G.C.3
  • 13
    • 0024707491 scopus 로고
    • Solubilization of methane monooxygenase from Methylococcus capsulatus (Bath)
    • Smith, D. D. S., and Dalton, H. (1989) Solubilization of methane monooxygenase from Methylococcus capsulatus (Bath), Eur. J. Biochem. 182, 667-671.
    • (1989) Eur. J. Biochem. , vol.182 , pp. 667-671
    • Smith, D.D.S.1    Dalton, H.2
  • 14
    • 0348087046 scopus 로고    scopus 로고
    • The membrane-associated form of methane mono-oxygenase from Methylococcus capsulatus (Bath) is a copper/iron protein
    • Basu, P., Katterle, B., Andersson, K. K., and Dalton, H. (2003) The membrane-associated form of methane mono-oxygenase from Methylococcus capsulatus (Bath) is a copper/iron protein, Biochem. J. 369, 417-427.
    • (2003) Biochem. J. , vol.369 , pp. 417-427
    • Basu, P.1    Katterle, B.2    Andersson, K.K.3    Dalton, H.4
  • 16
    • 0037386563 scopus 로고    scopus 로고
    • Purified paniculate methane monooxygenase from Methylococcus capsulatus (Bath) is a dimer with both mononuclear copper and a copper-containing cluster
    • Lieberman, R. L., Shrestha, D. B., Doan, P. E., Hoffman, B. M., Stemmler, T. L., and Rosenzweig, A. C. (2003) Purified paniculate methane monooxygenase from Methylococcus capsulatus (Bath) is a dimer with both mononuclear copper and a copper-containing cluster, Proc. Natl. Acad. Sci. U.S.A. 100, 3820-3825.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 3820-3825
    • Lieberman, R.L.1    Shrestha, D.B.2    Doan, P.E.3    Hoffman, B.M.4    Stemmler, T.L.5    Rosenzweig, A.C.6
  • 17
    • 0032478599 scopus 로고    scopus 로고
    • The paniculate methane monooxygenase from Methylococcus capsulatus (Bath) is a novel copper-containing three-subunit enzyme: Isolation and characterization
    • Nguyen, H. H. T., Elliott, S. J., Yip, J. H. K., and Chan, S. I. (1998) The paniculate methane monooxygenase from Methylococcus capsulatus (Bath) is a novel copper-containing three-subunit enzyme: Isolation and characterization, J. Biol. Chem. 273, 7957-7966.
    • (1998) J. Biol. Chem. , vol.273 , pp. 7957-7966
    • Nguyen, H.H.T.1    Elliott, S.J.2    Yip, J.H.K.3    Chan, S.I.4
  • 18
    • 0032526872 scopus 로고    scopus 로고
    • Purification and properties of particulate methane monooxygenase from Methylosinus trichosporium OB3b
    • Takeguchi, M., Miyakawa, K., and Okura, I. (1998) Purification and properties of particulate methane monooxygenase from Methylosinus trichosporium OB3b, J. Mol. Catal. A: Chem. 132, 145-153.
    • (1998) J. Mol. Catal. A: Chem. , vol.132 , pp. 145-153
    • Takeguchi, M.1    Miyakawa, K.2    Okura, I.3
  • 19
    • 0036856438 scopus 로고    scopus 로고
    • Improvement of the purification method for retaining the activity of the particulate methane monooxygenase from Methylosinus trichosporium OB3b
    • Miyaji, A., Kamachi, T., and Okura, I. (2002) Improvement of the purification method for retaining the activity of the particulate methane monooxygenase from Methylosinus trichosporium OB3b, Biotechnol. Lett. 24, 1883-1887.
    • (2002) Biotechnol. Lett. , vol.24 , pp. 1883-1887
    • Miyaji, A.1    Kamachi, T.2    Okura, I.3
  • 21
    • 0030580284 scopus 로고    scopus 로고
    • Evidence for an iron center in the ammonia monooxygenase from Nitrosomonas europaea
    • Zahn, J. A., Arciero, D. M., Hooper, A. B., and DiSpirito, A. A. (1996) Evidence for an iron center in the ammonia monooxygenase from Nitrosomonas europaea, FEBS Lett. 397, 35-38.
    • (1996) FEBS Lett. , vol.397 , pp. 35-38
    • Zahn, J.A.1    Arciero, D.M.2    Hooper, A.B.3    DiSpirito, A.A.4
  • 22
    • 0022365236 scopus 로고
    • Acetylene as suicide substrate and active site probe for methane monooxygenase from Methylococcus capsulatus (Bath)
    • Prior, S. D., and Dalton, H. (1985) Acetylene as suicide substrate and active site probe for methane monooxygenase from Methylococcus capsulatus (Bath), FEMS Microbiol. Lett. 29, 105-109.
    • (1985) FEMS Microbiol. Lett. , vol.29 , pp. 105-109
    • Prior, S.D.1    Dalton, H.2
  • 23
    • 0035542324 scopus 로고    scopus 로고
    • Structural and functional model of methane hydroxylase of membrane-bound monooxygenase from Methylococcus capsulatus (Bath)
    • Tukhvatullin, I. A., Gvozdev, R. I., and Andersson, K. K. (2001) Structural and functional model of methane hydroxylase of membrane-bound monooxygenase from Methylococcus capsulatus (Bath), Russ. Chem. Bull. 50, 1867-1876.
    • (2001) Russ. Chem. Bull. , vol.50 , pp. 1867-1876
    • Tukhvatullin, I.A.1    Gvozdev, R.I.2    Andersson, K.K.3
  • 24
    • 0141960385 scopus 로고    scopus 로고
    • Production of high-quality particulate methane monooxygenase in high yields from Methylococcus capsulatus (Bath) with a hollow-fiber membrane bioreactor
    • Yu, S. S. F., Chen, K. H. C., Tseng, M. Y. H., Wang, Y. S., Tseng, C. F., Chen, Y. J., Huang, D. S., and Chan, S. I. (2003) Production of high-quality particulate methane monooxygenase in high yields from Methylococcus capsulatus (Bath) with a hollow-fiber membrane bioreactor, J. Bacteriol. 185, 5915-5924.
    • (2003) J. Bacteriol. , vol.185 , pp. 5915-5924
    • Yu, S.S.F.1    Chen, K.H.C.2    Tseng, M.Y.H.3    Wang, Y.S.4    Tseng, C.F.5    Chen, Y.J.6    Huang, D.S.7    Chan, S.I.8
  • 25
    • 15044356424 scopus 로고    scopus 로고
    • Crystal structure of a membrane-bound metalloenzyme that catalyses the biological oxidation of methane
    • Lieberman, R. L., and Rosenzweig, A. C. (2005) Crystal structure of a membrane-bound metalloenzyme that catalyses the biological oxidation of methane, Nature 434, 177-182.
    • (2005) Nature , vol.434 , pp. 177-182
    • Lieberman, R.L.1    Rosenzweig, A.C.2
  • 26
    • 0035931906 scopus 로고    scopus 로고
    • The voltage-sensitive sodium channel is a bell-shaped molecule with several cavities
    • Sato, C., Ueno, Y., Asai, K., Takahashi, K., Sato, M., Engel, A., and Fujiyoshi, Y. (2001) The voltage-sensitive sodium channel is a bell-shaped molecule with several cavities, Nature 409, 1047-1051.
    • (2001) Nature , vol.409 , pp. 1047-1051
    • Sato, C.1    Ueno, Y.2    Asai, K.3    Takahashi, K.4    Sato, M.5    Engel, A.6    Fujiyoshi, Y.7
  • 27
    • 0035078574 scopus 로고    scopus 로고
    • Three-dimensional structure of a voltage-gated potassium channel at 2.5 nm resolution
    • Sokolova, O., Kolmakova-Partensky, L., and Grigorieff, N. (2001) Three-dimensional structure of a voltage-gated potassium channel at 2.5 nm resolution, Structure 9, 215-220.
    • (2001) Structure , vol.9 , pp. 215-220
    • Sokolova, O.1    Kolmakova-Partensky, L.2    Grigorieff, N.3
  • 28
    • 1342282941 scopus 로고    scopus 로고
    • The three-dimensional structure of the cardiac L-type voltage-gated calcium channel: Comparison with the skeletal muscle form reveals a common architectural motif
    • Wang, M. C., Collins, R. F., Ford, R. C., Berrow, N. S., Dolphin, A. C., and Kitmitto, A. (2004) The three-dimensional structure of the cardiac L-type voltage-gated calcium channel: Comparison with the skeletal muscle form reveals a common architectural motif, J. Biol. Chem. 279, 7159-7168.
    • (2004) J. Biol. Chem. , vol.279 , pp. 7159-7168
    • Wang, M.C.1    Collins, R.F.2    Ford, R.C.3    Berrow, N.S.4    Dolphin, A.C.5    Kitmitto, A.6
  • 29
    • 0030971840 scopus 로고    scopus 로고
    • Structure of the multidrug resistance P-glycoprotein to 2.5 nm resolution determined by electron microscopy and image analysis
    • Rosenberg, M. F., Callaghan, R., Ford, R. C., and Higgins, C. F. (1997) Structure of the multidrug resistance P-glycoprotein to 2.5 nm resolution determined by electron microscopy and image analysis, J. Biol. Chem. 272, 10685-10694.
    • (1997) J. Biol. Chem. , vol.272 , pp. 10685-10694
    • Rosenberg, M.F.1    Callaghan, R.2    Ford, R.C.3    Higgins, C.F.4
  • 31
    • 0034986184 scopus 로고    scopus 로고
    • Determining the structure of biological macromolecules by transmission electron microscopy, single particle analysis and 3D reconstruction
    • Ruprecht, J., and Nield, J. (2001) Determining the structure of biological macromolecules by transmission electron microscopy, single particle analysis and 3D reconstruction, Prog. Biophys. Mol. Biol. 75, 121-164.
    • (2001) Prog. Biophys. Mol. Biol. , vol.75 , pp. 121-164
    • Ruprecht, J.1    Nield, J.2
  • 32
    • 0014793109 scopus 로고
    • Enrichment, isolation and some properties of methane utilising bacteria
    • Whittenbury, R., Phillips, K. C., and Wilkinson, J. F. (1970) Enrichment, isolation and some properties of methane utilising bacteria, J. Gen. Microbiol. 61, 205-218.
    • (1970) J. Gen. Microbiol. , vol.61 , pp. 205-218
    • Whittenbury, R.1    Phillips, K.C.2    Wilkinson, J.F.3
  • 34
    • 4444347536 scopus 로고    scopus 로고
    • Blue native gel electrophoresis
    • (Hunte, C., Von Jagov, G., and Schagger, H., Eds.), Academic Press, London.
    • Schagger, H. (2003) Blue native gel electrophoresis, in Membrane protein purification and crystallisation (Hunte, C., Von Jagov, G., and Schagger, H., Eds.) pp 105 -130, Academic Press, London.
    • (2003) Membrane Protein Purification and Crystallisation , pp. 105-130
    • Schagger, H.1
  • 35
    • 0026409298 scopus 로고
    • Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form
    • Schagger, H., and Von Jagov, G. (1991) Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form, Anal. Biochem. 199, 223-231.
    • (1991) Anal. Biochem. , vol.199 , pp. 223-231
    • Schagger, H.1    Von Jagov, G.2
  • 36
    • 0014949207 scopus 로고
    • Cleavage of the structural proteins during the assembly of the head of the bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of the structural proteins during the assembly of the head of the bacteriophage T4, Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 37
    • 0026457773 scopus 로고
    • The light-harvesting complex II(B800/ 850) from Rhodospirillium molischianum is an octamer
    • Kleinekofort, W., Germeroth, L., van de Brock, J. A., Schubert, D., and Michel, H. (1992) The light-harvesting complex II(B800/ 850) from Rhodospirillium molischianum is an octamer, Eur. J. Biochem. 1140, 102-104.
    • (1992) Eur. J. Biochem. , vol.1140 , pp. 102-104
    • Kleinekofort, W.1    Germeroth, L.2    Van De Brock, J.A.3    Schubert, D.4    Michel, H.5
  • 38
    • 0003551994 scopus 로고    scopus 로고
    • Preparation techniques for transmission electron microscopy (TEM)
    • (Hoppert, M., and Holzenburg, A., Eds.), BIOS Scientific Publishers Ltd., Oxford, U.K.
    • Hoppert, M., and Holzenburg, A. (1998) Preparation techniques for transmission electron microscopy (TEM), in Electron Microscopy in Microbiology: RMS Handbook Series (Hoppert, M., and Holzenburg, A., Eds.) pp 11-18, BIOS Scientific Publishers Ltd., Oxford, U.K.
    • (1998) Electron Microscopy in Microbiology: RMS Handbook Series , pp. 11-18
    • Hoppert, M.1    Holzenburg, A.2
  • 39
    • 0027112252 scopus 로고
    • Crisp: Crystallographic image-processing on a personal-computer
    • Hovmoller, S. (1992) Crisp: Crystallographic Image-Processing on a Personal-Computer, Ultramicroscopy 41, 121-135.
    • (1992) Ultramicroscopy , vol.41 , pp. 121-135
    • Hovmoller, S.1
  • 41
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: Semiautomated software for high-resolution single-particle reconstructions
    • Ludtke, S. J., Baldwin, P. R., and Chiu, W. (1999) EMAN: Semiautomated software for high-resolution single-particle reconstructions, J. Struct. Biol. 128, 82-97.
    • (1999) J. Struct. Biol. , vol.128 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 42
    • 1842409555 scopus 로고    scopus 로고
    • Determination of the fold of the core protein of hepatitis B virus ky electron cryomicroscopy
    • Bottcher, B., Wynne, S. A., and Crowther, R. A. (1997) Determination of the fold of the core protein of hepatitis B virus ky electron cryomicroscopy, Nature 386, 88-91.
    • (1997) Nature , vol.386 , pp. 88-91
    • Bottcher, B.1    Wynne, S.A.2    Crowther, R.A.3
  • 43
    • 0000313739 scopus 로고
    • Exact filters for general geometry 3-dimensional reconstruction
    • Harauz, G., and Vanheel, M. (1986) Exact Filters for General Geometry 3-Dimensional Reconstruction, Optik 73, 146-156.
    • (1986) Optik , vol.73 , pp. 146-156
    • Harauz, G.1    Vanheel, M.2
  • 44
    • 0029975088 scopus 로고    scopus 로고
    • SPIDER and WEB: Processing and visualization of images in 3D electron microscopy and related fields
    • Frank, J., Radermacher, M., Penczek, P., Zhu, J., Li, Y. H., Ladjadj, M., and Leith, A. (1996) SPIDER and WEB: Processing and visualization of images in 3D electron microscopy and related fields, J. Struct. Biol. 116, 190-199.
    • (1996) J. Struct. Biol. , vol.116 , pp. 190-199
    • Frank, J.1    Radermacher, M.2    Penczek, P.3    Zhu, J.4    Li, Y.H.5    Ladjadj, M.6    Leith, A.7
  • 45
    • 0035161053 scopus 로고    scopus 로고
    • Membrane-associated quinoprotein formaldehyde dehydrogenase from Methylococcus capsulatus Bath
    • Zahn, J. A., Bergmann, D. J., Boyd, J. M., Kunz, R. C., and DiSpirito, A. A. (2001) Membrane-associated quinoprotein formaldehyde dehydrogenase from Methylococcus capsulatus Bath, J. Bacteriol. 183, 6832-6840.
    • (2001) J. Bacteriol. , vol.183 , pp. 6832-6840
    • Zahn, J.A.1    Bergmann, D.J.2    Boyd, J.M.3    Kunz, R.C.4    DiSpirito, A.A.5
  • 46
    • 0029097914 scopus 로고
    • Detergent solubilization of membrane-bound methane monooxygenase requires plastoquinol analogs as electron donors
    • Shiemke, A. K., Cook, S. A., Miley, T., and Singleton, P. (1995) Detergent solubilization of membrane-bound methane monooxygenase requires plastoquinol analogs as electron donors, Arch. Biochem. Biophys. 321, 421-428.
    • (1995) Arch. Biochem. Biophys. , vol.321 , pp. 421-428
    • Shiemke, A.K.1    Cook, S.A.2    Miley, T.3    Singleton, P.4
  • 47
    • 4444257275 scopus 로고    scopus 로고
    • Biological methane oxidation: Regulation, biochemistry, and active site structure of paniculate methane monooxygenase
    • Lieberman, R. L., and Rosenzweig, A. C. (2004) Biological methane oxidation: Regulation, biochemistry, and active site structure of paniculate methane monooxygenase, Crit. Rev. Biochem. Mol. Biol. 39, 147-164.
    • (2004) Crit. Rev. Biochem. Mol. Biol. , vol.39 , pp. 147-164
    • Lieberman, R.L.1    Rosenzweig, A.C.2
  • 48
    • 0034707086 scopus 로고    scopus 로고
    • Interaction of membrane proteins and lipids with solubilizing detergents
    • le Maire, M., Champeil, P., and Moller, J. V. (2000) Interaction of membrane proteins and lipids with solubilizing detergents, Biochim. Biophys. Acta 1508, 86-111.
    • (2000) Biochim. Biophys. Acta , vol.1508 , pp. 86-111
    • Maire, M.1    Champeil, P.2    Moller, J.V.3
  • 49
    • 0035443197 scopus 로고    scopus 로고
    • Biophysical approaches to membrane protein structure determination
    • Arora, A., and Tamm, L. K. (2001) Biophysical approaches to membrane protein structure determination, Curr. Opin. Struct. Biol. 11, 540-547.
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 540-547
    • Arora, A.1    Tamm, L.K.2
  • 50
    • 0036478793 scopus 로고    scopus 로고
    • Evidence that a type-2 NADH:quinone oxidoreductase mediates electron transfer to paniculate methane monooxygenase in Methylococcus capsulatus
    • Cook, S. A., and Shiemke, A. K. (2002) Evidence that a type-2 NADH:quinone oxidoreductase mediates electron transfer to paniculate methane monooxygenase in Methylococcus capsulatus, Arch. Biochem. Biophys. 398, 32-40.
    • (2002) Arch. Biochem. Biophys. , vol.398 , pp. 32-40
    • Cook, S.A.1    Shiemke, A.K.2
  • 51
    • 0003635936 scopus 로고
    • Biomembranes, molecular structure and function
    • (Cantor, C. R., Ed.), Springer-Verlag, New York
    • Gennis, R. B. (1989) Biomembranes, Molecular Structure and Function, in Biomembranes, Molecular Structure and Function (Cantor, C. R., Ed.) pp 91-105, Springer-Verlag, New York.
    • (1989) Biomembranes, Molecular Structure and Function , pp. 91-105
    • Gennis, R.B.1
  • 52
    • 0021714441 scopus 로고
    • The functional and physical form of mammalian cytochrome-C oxidase determined by gel-filtration, radiation inactivation, and sedimentation equilibrium-analysis
    • Suarez, M. D., Revzin, A., Narlock, R., Kempner, E. S., Thompson, D. A., and Fergusonmiller, S. (1984) The Functional and Physical Form of Mammalian Cytochrome-C Oxidase Determined by Gel-Filtration, Radiation Inactivation, and Sedimentation Equilibrium-Analysis, J. Biol. Chem. 259, 3791-3799.
    • (1984) J. Biol. Chem. , vol.259 , pp. 3791-3799
    • Suarez, M.D.1    Revzin, A.2    Narlock, R.3    Kempner, E.S.4    Thompson, D.A.5    Fergusonmiller, S.6
  • 53
    • 0036606751 scopus 로고    scopus 로고
    • Purification of the Escherichia coli ammonium transporter AmtB reveals a trimeric stoichiometry
    • Blakey, D., Leech, A., Thomas, G. H., Coutts, G., Findlay, K., and Merrick, M. (2002) Purification of the Escherichia coli ammonium transporter AmtB reveals a trimeric stoichiometry, Biochem. J. 364, 527-535.
    • (2002) Biochem. J. , vol.364 , pp. 527-535
    • Blakey, D.1    Leech, A.2    Thomas, G.H.3    Coutts, G.4    Findlay, K.5    Merrick, M.6
  • 55
    • 0038043211 scopus 로고    scopus 로고
    • Associations between light-harvesting complexes and Photosystem II from Marchantia polymorpha L. determined by two- and three-dimensional electron microscopy
    • Harrer, R. (2003) Associations between light-harvesting complexes and Photosystem II from Marchantia polymorpha L. determined by two- and three-dimensional electron microscopy, Photosynth. Res. 75, 249-258.
    • (2003) Photosynth. Res. , vol.75 , pp. 249-258
    • Harrer, R.1
  • 56
    • 0037057652 scopus 로고    scopus 로고
    • Crystal structure of bacterial multidrug efflux transporter AcrB
    • Murakami, S., Nakashima, R., Yamashita, E., and Yamaguchi, A. (2002) Crystal structure of bacterial multidrug efflux transporter AcrB, Nature 419, 587-593.
    • (2002) Nature , vol.419 , pp. 587-593
    • Murakami, S.1    Nakashima, R.2    Yamashita, E.3    Yamaguchi, A.4
  • 58
    • 0037423727 scopus 로고    scopus 로고
    • Detergent structure in crystals of the integral membrane light-harvesting complex LH2 from Rhodopseudomonas acidophila strain 10050
    • Prince, S. M., Howard, T. D., Myles, D. A. A., Wilkinson, C., Papiz, M. Z., Freer, A. A., Cogdell, R. J., and Isaacs, N. W. (2003) Detergent structure in crystals of the integral membrane light-harvesting complex LH2 from Rhodopseudomonas acidophila strain 10050, J. Mol. Biol. 326, 307-315.
    • (2003) J. Mol. Biol. , vol.326 , pp. 307-315
    • Prince, S.M.1    Howard, T.D.2    Myles, D.A.A.3    Wilkinson, C.4    Papiz, M.Z.5    Freer, A.A.6    Cogdell, R.J.7    Isaacs, N.W.8
  • 59
    • 36849148472 scopus 로고
    • Detergent structure in crystals of a bacterial photosynthetic reaction center
    • Roth, M., Lewitbentley, A., Michel, H., Deisenhofer, J., Huber, R., and Oesterhelt, D. (1989) Detergent Structure in Crystals of a Bacterial Photosynthetic Reaction Center, Nature 340, 659-662.
    • (1989) Nature , vol.340 , pp. 659-662
    • Roth, M.1    Lewitbentley, A.2    Michel, H.3    Deisenhofer, J.4    Huber, R.5    Oesterhelt, D.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.