메뉴 건너뛰기




Volumn 241, Issue 2, 1996, Pages 552-556

Direct electrochemistry of the hydroxylase of soluble methane monooxygenase from Methylococcus capsulatus (Bath)

Author keywords

Differential pulse voltammetry; Direct electrochemistry; Hydroxylase component; Methane monooxygenase; Promoter

Indexed keywords

METHANE MONOOXYGENASE; OXYGENASE; UNSPECIFIC MONOOXYGENASE;

EID: 0029858185     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1996.00552.x     Document Type: Article
Times cited : (38)

References (28)
  • 1
    • 0001618049 scopus 로고
    • Studies of the soluble methane monooxygenase protein system: Structure, component interactions and hydroxylation mechanism
    • Liu, K. E. & Lippard, S. J. (1995) Studies of the soluble methane monooxygenase protein system: structure, component interactions and hydroxylation mechanism. Adv. Inorg. Chem. 42, 263-289.
    • (1995) Adv. Inorg. Chem. , vol.42 , pp. 263-289
    • Liu, K.E.1    Lippard, S.J.2
  • 2
    • 0027913094 scopus 로고
    • Crystal structure of a bacterial non-heme iron hydroxylase that catalyses the biological oxidation of methane
    • Rosenzweig, A. C., Frederick, C. A., Lippard. S. J. & Nordlund, P. (1993) Crystal structure of a bacterial non-heme iron hydroxylase that catalyses 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
  • 3
    • 0000950578 scopus 로고
    • Determining the structure of a hydroxylase enzyme that catalyses the conversion of methane to methanol in methanotrophic bacteria
    • Rosenzweig, A. C. & Lippard S. J. (1994) Determining the structure of a hydroxylase enzyme that catalyses the conversion of methane to methanol in methanotrophic bacteria, Acc. Chem. Res. 27, 229-236.
    • (1994) Acc. Chem. Res. , vol.27 , pp. 229-236
    • Rosenzweig, A.C.1    Lippard, S.J.2
  • 4
    • 58149367966 scopus 로고
    • Geometry of the soluble methane monooxygenase catalytic diiron center in two oxidation states
    • Rosenzweig, A. C., Nordlund, P., Takahara, P. M. Frederick. C. A. & Lippard, S. J. (1995) Geometry of the soluble methane monooxygenase catalytic diiron center in two oxidation states. Chem. & Biol. 2, 409-418.
    • (1995) Chem. & Biol. , vol.2 , pp. 409-418
    • Rosenzweig, A.C.1    Nordlund, P.2    Takahara, P.M.3    Frederick, C.A.4    Lippard, S.J.5
  • 5
    • 0028090067 scopus 로고
    • Biochemistry of the soluble methane monooxygenase
    • Lipscomb, J. D. (1994) Biochemistry of the soluble methane monooxygenase. Annu. Rev. Microbiol. 48, 371-399.
    • (1994) Annu. Rev. Microbiol. , vol.48 , pp. 371-399
    • Lipscomb, J.D.1
  • 6
    • 0002160295 scopus 로고
    • ESR studies of the soluble methane monooxygenase from Methylococcus capsulatus (Bath)
    • Woodland, M. P., Patil, D. S., Cammack, R. & Dalton, H. (1986) ESR studies of the soluble methane monooxygenase from Methylococcus capsulatus (Bath), Biochim. Biophys. Acta 873, 237-242.
    • (1986) Biochim. Biophys. Acta , vol.873 , pp. 237-242
    • Woodland, M.P.1    Patil, D.S.2    Cammack, R.3    Dalton, H.4
  • 7
    • 0025766709 scopus 로고
    • Redox properties of the hydroxylase component of methane monooxygenase from Methylococcus capsulatus (Bath)
    • Liu, K. E. & Lippard, S. J. (1991) Redox properties of the hydroxylase component of methane monooxygenase from Methylococcus capsulatus (Bath), J. Biol. Chem. 266, 12836-12839.
    • (1991) J. Biol. Chem. , vol.266 , pp. 12836-12839
    • Liu, K.E.1    Lippard, S.J.2
  • 8
    • 0028008778 scopus 로고
    • Oxidation - Reduction potentials of the methane monooxygenase hydroxylase component from Methylosinus trichosporium OB3b
    • Paulsen, K. E., Liu, Y., Fox, B. G., Lipscomb, J. D., Münck, E. & Stankovich, M. T. (1994) Oxidation - reduction potentials of the methane monooxygenase hydroxylase component from Methylosinus trichosporium OB3b, Biochemistry 33, 713-722.
    • (1994) Biochemistry , vol.33 , pp. 713-722
    • Paulsen, K.E.1    Liu, Y.2    Fox, B.G.3    Lipscomb, J.D.4    Münck, E.5    Stankovich, M.T.6
  • 9
    • 0025109631 scopus 로고
    • Soluble methane monooxygenase from Methylococcus capsulants (Bath)
    • Pilkington, S. J. & Dalton, H. (1990) Soluble methane monooxygenase from Methylococcus capsulants (Bath), Methods Enzvmol. 188, 181-190.
    • (1990) Methods Enzvmol. , vol.188 , pp. 181-190
    • Pilkington, S.J.1    Dalton, H.2
  • 10
    • 0021506235 scopus 로고
    • Surface modifiers for the promotion of direct electrochemistry of cytochrome c
    • Allen, P. M., Hill, H. A. O. & Walton N. J. (1984) surface modifiers for the promotion of direct electrochemistry of cytochrome c, J. Electroanal. Chem. 178, 69-86.
    • (1984) J. Electroanal. Chem. , vol.178 , pp. 69-86
    • Allen, P.M.1    Hill, H.A.O.2    Walton, N.J.3
  • 11
    • 0000015668 scopus 로고
    • Direct electrochemistry of horse-heart cytochrome c at amino acid-modified gold electrodes
    • Di Gleria, K., Hill, H. A. O., Lowe, V. J. & Page, D. J. (1986) Direct electrochemistry of horse-heart cytochrome c at amino acid-modified gold electrodes, J. Electroanal. Chem. 213, 333-338.
    • (1986) J. Electroanal. Chem. , vol.213 , pp. 333-338
    • Di Gleria, K.1    Hill, H.A.O.2    Lowe, V.J.3    Page, D.J.4
  • 12
    • 0025300361 scopus 로고
    • Electron-transfer reactions of metalloproteins at peptide-modified gold electrodes
    • Barker, P. D., Di Gleria, K., Hill, H. A. O. & Lowe, V. J. (1990) Electron-transfer reactions of metalloproteins at peptide-modified gold electrodes, Eur. J. Biochem. 190, 171-175.
    • (1990) Eur. J. Biochem. , vol.190 , pp. 171-175
    • Barker, P.D.1    Di Gleria, K.2    Hill, H.A.O.3    Lowe, V.J.4
  • 13
    • 0026088028 scopus 로고
    • Complex formation between the protein components of methane monooxygenase from Methylosinus trichosporium OB3b
    • Fox, B., Liu, Y., Dege, J. E. & Lipscomb, J. D. (1991) Complex formation between the protein components of methane monooxygenase from Methylosinus trichosporium OB3b, J. Biol. Chem. 266, 540-550.
    • (1991) J. Biol. Chem. , vol.266 , pp. 540-550
    • Fox, B.1    Liu, Y.2    Dege, J.E.3    Lipscomb, J.D.4
  • 14
    • 0015209388 scopus 로고
    • Properties of graphical representations of multiple classes of binding sites
    • Klotz, I. M. & Hunston, D. L. (1970) Properties of graphical representations of multiple classes of binding sites, Biochem. 10, 3065-3069.
    • (1970) Biochem. , vol.10 , pp. 3065-3069
    • Klotz, I.M.1    Hunston, D.L.2
  • 15
  • 16
    • 0025976406 scopus 로고
    • Molecular analysis of the methane monooxygenase MMO gene cluster of Methylosinus trichosporium OB3b
    • Cardy, D. L. N., Laidler, V., Salmond, G. P. C. & Murrell, J. C. (1991) Molecular analysis of the methane monooxygenase MMO gene cluster of Methylosinus trichosporium OB3b, Mol. Microbiol. 5, 335-342.
    • (1991) Mol. Microbiol. , vol.5 , pp. 335-342
    • Cardy, D.L.N.1    Laidler, V.2    Salmond, G.P.C.3    Murrell, J.C.4
  • 17
    • 0017404563 scopus 로고
    • The soluble methane monooxygenase of Methylococcus capsulatus (Bath): Its ability to oxygenate n-alkanes, n-alkenes, ether and alicyclic, aromatic and heterocyclic compounds
    • Colby, J., Stirling, D. I. & Dalton, H. (1977) The soluble methane monooxygenase of Methylococcus capsulatus (Bath): its ability to oxygenate n-alkanes, n-alkenes, ether and alicyclic, 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
  • 18
    • 0018947980 scopus 로고
    • New findings in methane utilizing bacteria highlight their importance in the biosphere and their commercial potential
    • Higgins, I. J., Best, D. J. & Hammond, R. C. (1980) New findings in methane utilizing bacteria highlight their importance in the biosphere and their commercial potential, Nature 286, 561-564.
    • (1980) Nature , vol.286 , pp. 561-564
    • Higgins, I.J.1    Best, D.J.2    Hammond, R.C.3
  • 19
    • 0024978652 scopus 로고
    • Substrate specificity of soluble methane monooxygenase
    • Green, J. & Dalton, H. (1989) Substrate specificity of soluble methane monooxygenase, J. Biol. Chem. 264, 17698-17703.
    • (1989) J. Biol. Chem. , vol.264 , pp. 17698-17703
    • Green, J.1    Dalton, H.2
  • 21
    • 0009369792 scopus 로고
    • Direct electrochemistry of parsley plastocyanin on pyrolytic graphite electrodes
    • Conrad, L. S., Hill, H. A. O., Hunt, N. I. & Ulstrup, J. (1994) Direct electrochemistry of parsley plastocyanin on pyrolytic graphite electrodes, J. Electroanal. Chem. 364, 17-22.
    • (1994) J. Electroanal. Chem. , vol.364 , pp. 17-22
    • Conrad, L.S.1    Hill, H.A.O.2    Hunt, N.I.3    Ulstrup, J.4
  • 22
    • 0026630133 scopus 로고
    • Methane monooxygenase component B and reductase alter the regioselectivity of the hydroxylase component catalysed reactions
    • Froland, W. A., Andersson, K. K., Lee, S.-K., Liu, Y. & Lipscomb, J. D. (1992) Methane monooxygenase component B and reductase alter the regioselectivity of the hydroxylase component catalysed reactions. J. Biol. Chem. 267, 17588-17597.
    • (1992) J. Biol. Chem. , vol.267 , pp. 17588-17597
    • Froland, W.A.1    Andersson, K.K.2    Lee, S.-K.3    Liu, Y.4    Lipscomb, J.D.5
  • 23
    • 0027447439 scopus 로고
    • Activation of the hydroxylase of sMMO from Methylococcus capsulants (Bath) by hydrogen peroxide
    • Jiang, Y., Wilkins, P. C. & Dalton, H. (1993) Activation of the hydroxylase of sMMO from Methylococcus capsulants (Bath) by hydrogen peroxide, Biochim. Biophys. Acta 1163, 105-112.
    • (1993) Biochim. Biophys. Acta , vol.1163 , pp. 105-112
    • Jiang, Y.1    Wilkins, P.C.2    Dalton, H.3
  • 24
    • 0000525120 scopus 로고
    • X-ray absorption spectroscopic studies of the diiron center in methane monooxygenase in the presence of substrate and the coupling protein of the enzyme system
    • DeWitt, J. G., Rosenzweig, A. C., Salifoglou, A., Hedman, B., Lippard, S. J. & Hodgson, K. O. (1995) X-ray absorption spectroscopic studies of the diiron center in methane monooxygenase in the presence of substrate and the coupling protein of the enzyme system, Inorg. Chem. 34, 2505-2515.
    • (1995) Inorg. Chem. , vol.34 , pp. 2505-2515
    • DeWitt, J.G.1    Rosenzweig, A.C.2    Salifoglou, A.3    Hedman, B.4    Lippard, S.J.5    Hodgson, K.O.6
  • 25
    • 0029379564 scopus 로고
    • Kinetic and spectroscopic characterization of intermediates and component interactions in reactions of methane monooxygenase from Methyococcus capsulatus (Bath)
    • Liu, K. E., Valentine, A. M., Wang, D., Huynh, B. H., Edmonson, D. E., Salifoglou, A. & Lippard, S. J. (1995) Kinetic and spectroscopic characterization of intermediates and component interactions in reactions of methane monooxygenase from Methyococcus capsulatus (Bath), J. Am Chem. Soc. 117, 10174-10185.
    • (1995) J. Am Chem. Soc. , vol.117 , pp. 10174-10185
    • Liu, K.E.1    Valentine, A.M.2    Wang, D.3    Huynh, B.H.4    Edmonson, D.E.5    Salifoglou, A.6    Lippard, S.J.7
  • 26
    • 0028882691 scopus 로고
    • Gating effects of component B on oxygen activation by the methane monooxygenase hydroxylase component
    • Liu, Y., Nesheim, J. C., Lee, S.-K. & Lipscomb, J. D. (1995) Gating effects of component B on oxygen activation by the methane monooxygenase hydroxylase component, J. Biol. Chem. 270, 24662-24665.
    • (1995) J. Biol. Chem. , vol.270 , pp. 24662-24665
    • Liu, Y.1    Nesheim, J.C.2    Lee, S.-K.3    Lipscomb, J.D.4
  • 27
    • 0025011069 scopus 로고
    • Identification of the gene encoding the regulatory protein B of soluble methane monooxygenase
    • Pilkington. S. J., Salmond, G. P. C., Murrell, J. C. & Dalton, H. (1990) Identification of the gene encoding the regulatory protein B of soluble methane monooxygenase, FEMS Microbiol. Lett. 72, 345-348.
    • (1990) FEMS Microbiol. Lett. , vol.72 , pp. 345-348
    • Pilkington, S.J.1    Salmond, G.P.C.2    Murrell, J.C.3    Dalton, H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.