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Volumn 151, Issue 10, 2005, Pages 3417-3426

Effect of methanobactin on the activity and electron paramagnetic resonance spectra of the membrane-associated methane monooxygenase in Methylococcus capsulatus Bath

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; COPPER ION; DUROQUINOL; FREE RADICAL; METHANE MONOOXYGENASE; METHANOBACTIN; NITROGEN; PROPYLENE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; SULFUR; UNCLASSIFIED DRUG;

EID: 27144506654     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/mic.0.28169-0     Document Type: Article
Times cited : (62)

References (36)
  • 1
    • 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. & 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
  • 2
    • 0346568963 scopus 로고
    • Electron paramagnetic resonance of copper proteins
    • Edited by R. Lontie. Boca Raton, FL: CRC Press
    • Boas, J. F. (1984). Electron paramagnetic resonance of copper proteins. In Copper Proteins and Copper Enzymes, pp. 2-26. Edited by R. Lontie. Boca Raton, FL: CRC Press.
    • (1984) Copper Proteins and Copper Enzymes , pp. 2-26
    • Boas, J.F.1
  • 3
    • 0028277764 scopus 로고
    • The protonmotive Q cycle in mitochondria and bacteria
    • Brand, U. & Trumpower, B. (1994). The protonmotive Q cycle in mitochondria and bacteria. Crit Rev Biochem Mol Biol 29, 165-197.
    • (1994) Crit. Rev. Biochem. Mol. Biol. , vol.29 , pp. 165-197
    • Brand, U.1    Trumpower, B.2
  • 4
    • 0025528777 scopus 로고
    • Optimization of trichloroethylene oxidation by methanotrophs and the use of a colorimetric assay to detect soluble methane monooxygenase activity
    • Brusseau, G. A., Tsien, H.-C., Hanson, R. S. & Wackett, L. P. (1990). Optimization of trichloroethylene oxidation by methanotrophs and the use of a colorimetric assay to detect soluble methane monooxygenase activity. Biodegradation 1, 19-29.
    • (1990) Biodegradation , vol.1 , pp. 19-29
    • Brusseau, G.A.1    Tsien, H.-C.2    Hanson, R.S.3    Wackett, L.P.4
  • 5
    • 4644230771 scopus 로고    scopus 로고
    • Toward delineating the structure and function of the particulate methane monooxygenase from methanotrophic bacteria
    • Chan, S. I., Chen, K. H.-C., Yu, S. S.-F., Chen, C.-L. & Kuo, S. S.-J. (2004). Toward delineating the structure and function of the particulate methane monooxygenase from methanotrophic bacteria. Biochemistry 43, 4421-4430.
    • (2004) Biochemistry , vol.43 , pp. 4421-4430
    • Chan, S.I.1    Chen, K.H.-C.2    Yu, S.S.-F.3    Chen, C.-L.4    Kuo, S.S.-J.5
  • 6
    • 0141838951 scopus 로고    scopus 로고
    • The membrane-associated methane monooxygenase (pMMO) and pMMO-NADH: Quinone oxidoreductase complex from Methylococcus capsulatus Bath
    • 7 other authors
    • Choi, D.-W., Kunz, R. C., Boyd, E. S. & 7 other authors (2003). The membrane-associated methane monooxygenase (pMMO) and pMMO-NADH: quinone oxidoreductase complex from Methylococcus capsulatus Bath. J Bacteriol 185, 5755-5764.
    • (2003) J Bacteriol , vol.185 , pp. 5755-5764
    • Choi, D.-W.1    Kunz, R.C.2    Boyd, E.S.3
  • 8
    • 0002443852 scopus 로고
    • Regulation and control of methane monooxygenase
    • Edited by R. L. Crawford & R. S. Hanson. Washington, DC: American Society for Microbiology
    • 1 Compounds, pp. 75-82. Edited by R. L. Crawford & R. S. Hanson. Washington, DC: American Society for Microbiology.
    • (1984) 1 Compounds , pp. 75-82
    • Dalton, H.1    Prior, S.D.2    Leak, D.J.3    Stanley, S.H.4
  • 10
    • 27144455152 scopus 로고    scopus 로고
    • Electron flow during methane oxidation in methanotrophs
    • Edited by D. Zannoni. The Netherlands: Kluwer Scientific
    • DiSpirito, A. A., Kunz, R. C., Choi, D. W. & Zahn, J. A. (2004). Electron flow during methane oxidation in methanotrophs. In Respiration in Archaea and Bacteria, pp. 141-169. Edited by D. Zannoni. The Netherlands: Kluwer Scientific.
    • (2004) Respiration in Archaea and Bacteria , pp. 141-169
    • DiSpirito, A.A.1    Kunz, R.C.2    Choi, D.W.3    Zahn, J.A.4
  • 12
    • 0026633609 scopus 로고
    • Singular value decomposition: Application to analysis of experimental data
    • Henry, E. R. & Hofrichter, J. (1992). Singular value decomposition: application to analysis of experimental data. Methods Enzymol 210, 129-192.
    • (1992) Methods Enzymol. , vol.210 , pp. 129-192
    • Henry, E.R.1    Hofrichter, J.2
  • 14
    • 16344378611 scopus 로고    scopus 로고
    • Purification and physical-chemical properties of methanobactin: A chalkophore from Methylosinus trichosporium OB3b
    • Kim, H. J., Galeva, N., Larive, C. K., Alterman, M. & Graham, D. W. (2005). Purification and physical-chemical properties of methanobactin: a chalkophore from Methylosinus trichosporium OB3b. Biochemistry 44, 5140-5148.
    • (2005) Biochemistry , vol.44 , pp. 5140-5148
    • Kim, H.J.1    Galeva, N.2    Larive, C.K.3    Alterman, M.4    Graham, D.W.5
  • 15
    • 4444257275 scopus 로고    scopus 로고
    • Biological methane oxidation: Regulation, biochemistry, and active site structure of particulate methane monooxygenase
    • Lieberman, R. L. & Rosenzweig, A. C. (2004). Biological methane oxidation: regulation, biochemistry, and active site structure of particulate 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
  • 16
    • 15044356424 scopus 로고    scopus 로고
    • Crystal structure of a membrane-bound metalloenzyme that catalyses the biological oxidation of methane
    • Lieberman, R. L. & 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
  • 17
    • 0037386563 scopus 로고    scopus 로고
    • Purified particulate 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. & Rosenzweig, A. C. (2003). Purified particulate 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
  • 18
    • 0033515466 scopus 로고    scopus 로고
    • Ubiquinol: Cytochrome c oxidoreductase: Effects of inhibitors on reverse electron transfer from the iron-sulfur protein to cytochrome b
    • Matsumo-Yagi, A. & Hatefi, Y. (1999). Ubiquinol: cytochrome c oxidoreductase: effects of inhibitors on reverse electron transfer from the iron-sulfur protein to cytochrome b. J Biol Chem 274, 9283-9288.
    • (1999) J. Biol. Chem. , vol.274 , pp. 9283-9288
    • Matsumo-Yagi, A.1    Hatefi, Y.2
  • 19
    • 0028304991 scopus 로고
    • The nature of the copper ions in the membranes containing the particulate methane monooxygenase from Methylococcus capsulatus (Bath)
    • Nguyen, H.-H. T., Shiemke, A. K., Jacobs, S. J., Hales, B. J., Lidstrom, M. E. & Chan, S. I. (1994). The nature of the copper ions in the membranes containing the particulate methane monooxygenase from Methylococcus capsulatus (Bath). J Biol Chem 269, 14995-15005.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14995-15005
    • Nguyen, H.-H.T.1    Shiemke, A.K.2    Jacobs, S.J.3    Hales, B.J.4    Lidstrom, M.E.5    Chan, S.I.6
  • 20
    • 12644275421 scopus 로고    scopus 로고
    • X-ray absorption and EPR studies on the copper ions associated with the particulate methane monooxygenase from Methylococcus capsulatus (Bath). Cu(I) ions and their implications
    • Nguyen, H.-H. T., Nakagawa, K. H., Hedman, B., Elliott, S. J., Lidstrom, M. E., Hodgson, K. O. & Chan, S. I. (1996). X-ray absorption and EPR studies on the copper ions associated with the particulate methane monooxygenase from Methylococcus capsulatus (Bath). Cu(I) ions and their implications. J Am Chem Soc 118, 12766-12776.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 12766-12776
    • Nguyen, H.-H.T.1    Nakagawa, K.H.2    Hedman, B.3    Elliott, S.J.4    Lidstrom, M.E.5    Hodgson, K.O.6    Chan, S.I.7
  • 21
    • 0032478599 scopus 로고    scopus 로고
    • The particulate methane monooxygenase from Methylococcus capsulatus (Bath) is a novel copper-containing three-subunit enzyme
    • Nguyen, H.-H. T., Elliott, S. J., Yip, J. H.-K. & Chan, S. I. (1998). The particulate methane monooxygenase from Methylococcus capsulatus (Bath) is a novel copper-containing three-subunit enzyme. 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
  • 22
    • 0029097914 scopus 로고
    • Detergent solubilization of membrane-bound methane monooxygenase requires plastoquinol analogs as electron donors
    • Shiemke, A. K., Cook, S. A., Miley, T. & 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
  • 23
    • 1142286475 scopus 로고    scopus 로고
    • Inhibition of membrane-bound methane monooxygenase and ammonia monooxygenase by diphenyliodonium: Implications for electron transfer
    • Shiemke, A. K., Arp, D. J. & Sayavedra-Soto, L. A. (2004). Inhibition of membrane-bound methane monooxygenase and ammonia monooxygenase by diphenyliodonium: implications for electron transfer. J Bacteriol 186, 928-937.
    • (2004) J. Bacteriol. , vol.186 , pp. 928-937
    • Shiemke, A.K.1    Arp, D.J.2    Sayavedra-Soto, L.A.3
  • 24
    • 13844294471 scopus 로고    scopus 로고
    • X-ray crystallography and biological metal centers: Is seeing believing?
    • Sommerhalter, M., Lieberman, R. L. & Rosenzweig, A. C. (2005). X-ray crystallography and biological metal centers: is seeing believing? Inorg Chem 44, 770-778.
    • (2005) Inorg. Chem. , vol.44 , pp. 770-778
    • Sommerhalter, M.1    Lieberman, R.L.2    Rosenzweig, A.C.3
  • 25
    • 0034311053 scopus 로고    scopus 로고
    • Role of iron and copper in particulate methane monooxygenase of Methylosinus trichosporium OB3b
    • Takeguchi, M. & Okura, I. (2000). Role of iron and copper in particulate methane monooxygenase of Methylosinus trichosporium OB3b. Catal Surv Jpn 4, 51-63.
    • (2000) Catal. Surv. Jpn. , vol.4 , pp. 51-63
    • Takeguchi, M.1    Okura, I.2
  • 26
    • 0033534320 scopus 로고    scopus 로고
    • The role of copper in particulate methane monooxygenase from Methylosinus trichosporium OB3b
    • Takeguchi, M., Miyakawa, K. & Okura, I. (1999). The role of copper in particulate methane monooxygenase from Methylosinus trichosporium OB3b. J Mol Catal 137, 161-168.
    • (1999) J. Mol. Catal. , vol.137 , pp. 161-168
    • Takeguchi, M.1    Miyakawa, K.2    Okura, I.3
  • 27
    • 0344505236 scopus 로고    scopus 로고
    • Isolation of copper biochelates from Methylosinus trichosporium OB3b and soluble methane monooxygenase mutants
    • Téllez, C. M., Gaus, K. P., Graham, D. W., Arnold, R. G. & Guzman, R. Z. (1998). Isolation of copper biochelates from Methylosinus trichosporium OB3b and soluble methane monooxygenase mutants. Appl Environ Microbiol 64, 1115-1122.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 1115-1122
    • Téllez, C.M.1    Gaus, K.P.2    Graham, D.W.3    Arnold, R.G.4    Guzman, R.Z.5
  • 28
    • 0000239991 scopus 로고    scopus 로고
    • Dioxygen activation by enzymes containing binuclear non-heme iron clusters
    • Wallar, B. J. & Lipscomb, J. D. (1996). Dioxygen activation by enzymes containing binuclear non-heme iron clusters. Chem Rev 96, 2625-2658.
    • (1996) Chem. Rev. , vol.96 , pp. 2625-2658
    • Wallar, B.J.1    Lipscomb, J.D.2
  • 29
    • 0035916223 scopus 로고    scopus 로고
    • Methane monooxygenase component B mutants alter the kinetics of steps throughout the catalytic cycle
    • Wallar, B. J. & Lipscomb, J. D. (2001). Methane monooxygenase component B mutants alter the kinetics of steps throughout the catalytic cycle. Biochemistry 40, 2220-2233.
    • (2001) Biochemistry , vol.40 , pp. 2220-2233
    • Wallar, B.J.1    Lipscomb, J.D.2
  • 30
    • 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. & 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
  • 31
    • 0030987924 scopus 로고    scopus 로고
    • Low-frequency EPR of the copper in particulate methane monooxygenase from Methylomicrobium albus BG8
    • Yuan, H., Collins, M. L. P. & Antholine, W. E. (1997). Low-frequency EPR of the copper in particulate methane monooxygenase from Methylomicrobium albus BG8. J Am Chem Soc 119, 5073-5074.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 5073-5074
    • Yuan, H.1    Collins, M.L.P.2    Antholine, W.E.3
  • 33
    • 0345355219 scopus 로고    scopus 로고
    • Concentration of Cu, EPR-detectable Cu, and formation of cupric-ferrocyanide in membranes with pMMO
    • Yuan, H., Collins, M. L. P. & Antholine, W. E. (1998b). Concentration of Cu, EPR-detectable Cu, and formation of cupric-ferrocyanide in membranes with pMMO. J Inorg Biochem 72, 179-185.
    • (1998) J. Inorg. Biochem. , vol.72 , pp. 179-185
    • Yuan, H.1    Collins, M.L.P.2    Antholine, W.E.3
  • 35
    • 0030067648 scopus 로고    scopus 로고
    • Membrane-associated methane monooxygenase from Methylococcus capsulatus (Bath)
    • Zahn, J. A. & DiSpirito, A. A. (1996). Membrane-associated methane monooxygenase from Methylococcus capsulatus (Bath). J Bacteriol 178, 1018-1029.
    • (1996) J. Bacteriol. , vol.178 , pp. 1018-1029
    • Zahn, J.A.1    DiSpirito, A.A.2


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