1887

Abstract

The intracellular location of methane mono-oxygenase (MMO) (soluble or particulate) in OB3b is dependent on the availability of copper in the growth medium. Raising the Cu concentration from 1 μ to 5 μ effected a transition from soluble to particulate MMO activity, and changes in major cell polypeptides were observed on SDS-polyacrylamide gels. Organisms containing soluble MMO oxidized a wide range of substrates including -alkanes, -alkenes, aromatic and alicyclic compounds. By contrast, organisms containing particulate MMO did not oxidize aromatic or alicyclic compounds. These observations provide further evidence that the two types of MMO are fundamentally different.

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1984-12-01
2024-12-03
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References

  1. Colby J., Dalton H. 1976; Some properties of a soluble methane mono-oxygenase from Methylococcus capsulatus strain Bath. Biochemical Journal 157:495–497
    [Google Scholar]
  2. Colby J., Dalton H., Whittenbury R. 1975; An improved assay for bacterial methane mono-oxygenase: some properties of the enzyme from Methylomonas methanica. Biochemical Journal 151:459–462
    [Google Scholar]
  3. Colby J., Stirling D.I., Dalton H. 1977; The soluble methane mono-oxygenase of Methylococcus capsulatus (Bath). Its ability to oxygenate H-alkanes, n-alkenes, ethers and alicyclic, aromatic and heterocyclic compounds. Biochemical Journal 165:395–402
    [Google Scholar]
  4. Cornish A., Nicholls K.M., Scott D., Hunter B.K., Aston W.J., Higgins I.J., Sanders J.K.M. 1984; In vivo l3C-NMR investigations of methanol oxidation by the obligate methanotroph, Methylo- sinus trichosporium OB3b. Journal of General Microbiology 130:2565–2575
    [Google Scholar]
  5. Higgins I.J., Best D.J., Hammond R.C., Scott D. 1981; Methane-oxidizing microorganisms. Microbiological Reviews 45:556–590
    [Google Scholar]
  6. Higgins I.J., Quayle J.R. 1970; Oxygenation of methane by methane-grown Pseudomonas methanica and Methanomonas methanooxidans. Biochemical Journal 118:201–208
    [Google Scholar]
  7. Higgins I.J., Hammond R.C., Sariaslani F.S., Best D.J., Davies M.M., Tryhorn S.E., Taylor F. 1979; Biotransformation of hydrocarbons and related compounds by whole organism suspensions of methane-grown Methylosinus tricho- sporium OB3b. Biochemical and Biophysical Research Communications 89(2):671–677
    [Google Scholar]
  8. Hou C.T. 1984; Propylene oxide production from propylene by immobilised whole cells of Methylo- , sinus sp. CRL 31 in a gas-solid bioreactor. Applied Microbiology and Biotechnology 19:1–4
    [Google Scholar]
  9. Laemmli U.K. 1970; Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, London 277:680–685
    [Google Scholar]
  10. Leak D.J., Dalton H. 1983; In vivo studies of primary alcohols, aldehydes and carboxylic acids as electron donors for the methane mono-oxygenase in a variety of methanotrophs. Journal of General Microbiology 129:3487–3497
    [Google Scholar]
  11. Patel R.N., Bose H.R., Mandy W.J., Hoare D.S. 1972; Physiological studies of methane- and methanol-oxidizing bacteria: comparison of a primary alcohol dehydrogenase from Meihylococcus capsulatus (Texas strain) and Pseudomonas species M27. Journal of Bacteriology 110(2):570–577
    [Google Scholar]
  12. Patel R.N., Hou C.T., Derelenko P., Felix A. 1980; Purification and properties of a heme- containing aldehyde dehydrogenase from Methylosinus trichosporium. Archives of Biochemistry and Biophysics 203(2):654–662
    [Google Scholar]
  13. Peterson G.L. 1977; A simplification of the protein assay of Lowry et al. which is more generally applicable. Analytical Biochemistry 83:346–356
    [Google Scholar]
  14. Scott D., Brannan J., Higgins I.J. 1981a; The effect of growth conditions on intracytoplasmic membranes and methane mono-oxygenase activities in Methylosinus trichosporium OB3b. Journal of General Microbiology 125:63–72
    [Google Scholar]
  15. Scott D., Best D.J., Higgins I.J. 1981b; Intracytoplasmic membranes in oxygen-limited chemostat cultures of Methylosinus trichosporium OB3b: biocatalytic implications of physiologically balanced growth. Biotechnology Letters 3:641–644
    [Google Scholar]
  16. Stanley S.H., Prior S.D., Leak D.J., Dalton H. 1983; Copper stress underlies the fundamental change in intracellular location of methane monooxygenase in methane-oxidising microorganisms: Studies in batch and continuous culture. Biotechnology Letters 5:487–492
    [Google Scholar]
  17. Stirling D.I., Colby J., Dalton H. 1979; A comparison of the substrate and electron-donor specificities of the methane mono-oxygenases from three strains of methane-oxidising bacteria. Biochemical Journal 177:361–364
    [Google Scholar]
  18. Stirling D.I., Dalton H. 1979; Properties of the methane mono-oxygenase from extracts of Methylosinus trichosporium OB3b and evidence for its similarity to the enzyme from Methylococcus capsulatus (Bath). European Journal of Biochemistry 96:205–212
    [Google Scholar]
  19. Tonge G.M., Harrison D.E.F., Knowles C.J., Higgins I.J. 1975; Properties and partial purification of the methane oxidising enzyme system from Methylosinus trichosporium. FEBS Letters 58(1):293–299
    [Google Scholar]
  20. Whittenbury R., Dalton H. 1982; The obligate methane-oxidizing bacteria and their biotechnological potential. Basic Life Sciences 25:439–460
    [Google Scholar]
  21. Woodland M.P., Dalton H. 1984; Purification and characterization of component A of the methane monooxygenase from Methylococcus capsulatus (Bath). The Journal of Biological Chemistry 259(1):53–59
    [Google Scholar]
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