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Volumn 46, Issue 2, 2006, Pages 316-320

A rapid method for the purification of methanol dehydrogenase from Methylobacterium extorquens

Author keywords

Cation exchange chromatography; Methanol dehydrogenase; Methylobacterium extorquens AM1; Purification

Indexed keywords

ALCOHOL DEHYDROGENASE; ALCOHOL DEHYDROGENASE (ACCEPTOR); BACTERIAL PROTEIN;

EID: 33645404349     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2005.07.014     Document Type: Article
Times cited : (17)

References (24)
  • 1
    • 1242273667 scopus 로고    scopus 로고
    • The structure and mechanism of methanol dehydrogenase
    • C. Anthony, and P. Williams The structure and mechanism of methanol dehydrogenase Biochim. Biophys. Acta 1647 2003 18 23
    • (2003) Biochim. Biophys. Acta , vol.1647 , pp. 18-23
    • Anthony, C.1    Williams, P.2
  • 2
    • 0022541528 scopus 로고
    • Bacterial oxidation of methane and methanol
    • C. Anthony Bacterial oxidation of methane and methanol Adv. Microb. Physiol. 27 1986 113 210
    • (1986) Adv. Microb. Physiol. , vol.27 , pp. 113-210
    • Anthony, C.1
  • 3
    • 0025115682 scopus 로고
    • Methanol dehydrogenase from Methylobacterium extorquens AM1
    • D.J. Day, and C. Anthony Methanol dehydrogenase from Methylobacterium extorquens AM1 Methods Enzymol. 188 1990 210 216
    • (1990) Methods Enzymol. , vol.188 , pp. 210-216
    • Day, D.J.1    Anthony, C.2
  • 4
    • 0023140123 scopus 로고
    • Purification, crystallization and preliminary X-ray diffraction characterization of methanol dehydrogenase from Methylosinus trichosporium OB3b
    • M.W. Parker, A. Cornish, V. Gossain, and D.J. Best Purification, crystallization and preliminary X-ray diffraction characterization of methanol dehydrogenase from Methylosinus trichosporium OB3b Eur. J. Biochem. 164 1987 223 227
    • (1987) Eur. J. Biochem. , vol.164 , pp. 223-227
    • Parker, M.W.1    Cornish, A.2    Gossain, V.3    Best, D.J.4
  • 5
    • 0017844388 scopus 로고
    • Purification and properties of methanol dehydrogenase from HYPHOMICROBIUM X
    • J.A. Duine, J. Frank, and J. Westerling Purification and properties of methanol dehydrogenase from HYPHOMICROBIUM X Biochim. Biophys. Acta 524 1978 277 287
    • (1978) Biochim. Biophys. Acta , vol.524 , pp. 277-287
    • Duine, J.A.1    Frank, J.2    Westerling, J.3
  • 6
    • 0031928441 scopus 로고    scopus 로고
    • Purification and properties of methanol dehydrogenase from Methylosinus sp. WI 14
    • S. Grosse, C. Voigt, K.-D. Wendlandt, and H.-P. Kleber Purification and properties of methanol dehydrogenase from Methylosinus sp. WI 14 J. Basic Microbiol. 38 1998 189 196
    • (1998) J. Basic Microbiol. , vol.38 , pp. 189-196
    • Grosse, S.1    Voigt, C.2    Wendlandt, K.-D.3    Kleber, H.-P.4
  • 8
    • 0029643953 scopus 로고
    • The refined structure of the quinoprotein methanol dehydrogenase from methylobacterium extorquens at 1.94 Å
    • M. Ghosh, C. Anthony, K. Harlos, M.G. Goodwin, and C. Blake The refined structure of the quinoprotein methanol dehydrogenase from methylobacterium extorquens at 1.94 Å Structure 3 1995 177 187
    • (1995) Structure , vol.3 , pp. 177-187
    • Ghosh, M.1    Anthony, C.2    Harlos, K.3    Goodwin, M.G.4    Blake, C.5
  • 9
    • 0030000290 scopus 로고    scopus 로고
    • Determination of the gene sequence and the three-dimensional structure at 2.4 Å resolution of methanol dehydrogenase from methylophilus W3A1
    • Z.-X. Xia, W.-W. Dai, Y.-F. Zhang, S.A. White, G.D. Boyd, and F.S. Mathews Determination of the gene sequence and the three-dimensional structure at 2.4 Å resolution of methanol dehydrogenase from methylophilus W3A1 J. Mol. Biol. 259 1996 480 501
    • (1996) J. Mol. Biol. , vol.259 , pp. 480-501
    • Xia, Z.-X.1    Dai, W.-W.2    Zhang, Y.-F.3    White, S.A.4    Boyd, G.D.5    Mathews, F.S.6
  • 10
    • 0344419995 scopus 로고    scopus 로고
    • X-ray structure of methanol dehydrogenase from Paracoccus denitrificans and molecular modeling of its interactions with cytochrome c-551I
    • Z.-X. Xia, W.-W. Dai, Y.-N. He, S.A. White, F.S. Mathews, and V.L. Davidson X-ray structure of methanol dehydrogenase from Paracoccus denitrificans and molecular modeling of its interactions with cytochrome c-551I J. Biol. Inorg. Chem. 8 2003 843 854
    • (2003) J. Biol. Inorg. Chem. , vol.8 , pp. 843-854
    • Xia, Z.-X.1    Dai, W.-W.2    He, Y.-N.3    White, S.A.4    Mathews, F.S.5    Davidson, V.L.6
  • 11
    • 0000929980 scopus 로고
    • Voltammetric determination of acid dissociation constants of pyrroloquinoline quinone and its reduced form under acidic conditions
    • K. Kano, K. Mori, B. Uno, T. Kubota, T. Ikeda, and M. Senda Voltammetric determination of acid dissociation constants of pyrroloquinoline quinone and its reduced form under acidic conditions Bioelectrochem. Bioenerg. 24 1990 193 201
    • (1990) Bioelectrochem. Bioenerg. , vol.24 , pp. 193-201
    • Kano, K.1    Mori, K.2    Uno, B.3    Kubota, T.4    Ikeda, T.5    Senda, M.6
  • 12
    • 0001407788 scopus 로고
    • Voltammetric and spectroscopic studies of pyrroloquinoline quinone coenzyme under neutral and basic conditions
    • K. Kano, K. Mori, B. Uno, T. Kubota, T. Ikeda, and M. Senda Voltammetric and spectroscopic studies of pyrroloquinoline quinone coenzyme under neutral and basic conditions Bioelectrochem. Bioenerg. 23 1990 227 238
    • (1990) Bioelectrochem. Bioenerg. , vol.23 , pp. 227-238
    • Kano, K.1    Mori, K.2    Uno, B.3    Kubota, T.4    Ikeda, T.5    Senda, M.6
  • 13
    • 0029092019 scopus 로고
    • High performance liquid chromatographic separation and pH-dependent electrochemical properties of pyrroloquinoline quinone and three closely related isomers
    • Z. Zhang, L.M.V. Tillekeratne, J.R. Kirchhoff, and R.A. Hudson High performance liquid chromatographic separation and pH-dependent electrochemical properties of pyrroloquinoline quinone and three closely related isomers Biochem. Biophys. Res. Commun. 212 1995 41 47
    • (1995) Biochem. Biophys. Res. Commun. , vol.212 , pp. 41-47
    • Zhang, Z.1    Tillekeratne, L.M.V.2    Kirchhoff, J.R.3    Hudson, R.A.4
  • 14
    • 85007870321 scopus 로고
    • Kinetics and mechanism of the oxidative deamination of amines by coenzyme PQQ
    • S. Itoh, Y. Kitamura, Y. Ohshiro, and T. Agawa Kinetics and mechanism of the oxidative deamination of amines by coenzyme PQQ Bull. Chem. Soc. Jpn. 59 1986 1907 1910
    • (1986) Bull. Chem. Soc. Jpn. , vol.59 , pp. 1907-1910
    • Itoh, S.1    Kitamura, Y.2    Ohshiro, Y.3    Agawa, T.4
  • 15
    • 0001349751 scopus 로고
    • Kinetic studies on the oxidation of thiols by coenzyme PQQ
    • S. Itoh, N. Kato, M. Mure, and Y. Ohshiro Kinetic studies on the oxidation of thiols by coenzyme PQQ Bull. Chem. Soc. Jpn. 60 1987 420 422
    • (1987) Bull. Chem. Soc. Jpn. , vol.60 , pp. 420-422
    • Itoh, S.1    Kato, N.2    Mure, M.3    Ohshiro, Y.4
  • 16
    • 0026535329 scopus 로고
    • Pyrroloquinoline quinone (coenzyme PQQ) and the oxidation of SH residues in proteins
    • J. Park, and J.E. Churchich Pyrroloquinoline quinone (coenzyme PQQ) and the oxidation of SH residues in proteins Biofactors 3 1992 257 260
    • (1992) Biofactors , vol.3 , pp. 257-260
    • Park, J.1    Churchich, J.E.2
  • 18
    • 0034529358 scopus 로고    scopus 로고
    • Electrochemical detection of thiols with a coenzyme pyrroloquinoline quinone modified electrode
    • T. Inoue, and J.R. Kirchhoff Electrochemical detection of thiols with a coenzyme pyrroloquinoline quinone modified electrode Anal. Chem. 72 2000 5755 5760
    • (2000) Anal. Chem. , vol.72 , pp. 5755-5760
    • Inoue, T.1    Kirchhoff, J.R.2
  • 19
    • 0037086254 scopus 로고    scopus 로고
    • Determination of thiols by capillary electrophoresis with amperometric detection at a coenzyme pyrroloquinoline quinone modified electrode
    • T. Inoue, and J.R. Kirchhoff Determination of thiols by capillary electrophoresis with amperometric detection at a coenzyme pyrroloquinoline quinone modified electrode Anal. Chem. 74 2002 1349 1354
    • (2002) Anal. Chem. , vol.74 , pp. 1349-1354
    • Inoue, T.1    Kirchhoff, J.R.2
  • 21
    • 1242318571 scopus 로고    scopus 로고
    • Bioelectrocatalysis-based application of quinoproteins and quinoprotein-containing bacterial cells in biosensors and biofuel cells
    • T. Ikeda, and K. Kano Bioelectrocatalysis-based application of quinoproteins and quinoprotein-containing bacterial cells in biosensors and biofuel cells Biochim. Biophys. Acta 1647 2003 121 126
    • (2003) Biochim. Biophys. Acta , vol.1647 , pp. 121-126
    • Ikeda, T.1    Kano, K.2
  • 22
    • 0032791749 scopus 로고    scopus 로고
    • A biofuel cell based on two immiscible solvents and glucose oxidase and microperoxidase-11 monolayer-functionalized electrodes
    • E. Katz, B. Filanovsky, and I. Willner A biofuel cell based on two immiscible solvents and glucose oxidase and microperoxidase-11 monolayer-functionalized electrodes New J. Chem. 1999 481 487
    • (1999) New J. Chem. , pp. 481-487
    • Katz, E.1    Filanovsky, B.2    Willner, I.3
  • 23
    • 0037980436 scopus 로고    scopus 로고
    • A biofuel cell with electrochemically switchable and tunable power output
    • E. Katz, and I. Willner A biofuel cell with electrochemically switchable and tunable power output J. Am. Chem. Soc. 125 2003 6803 6813
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 6803-6813
    • Katz, E.1    Willner, I.2
  • 24
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72 1976 248 254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1


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