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Role of iron and copper in particulate methane monooxygenase of Methylosinus trichosporium OB3b

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Abstract

The role of iron and copper in particulate methane monooxygenase (pMMO) of Methylosinus trichosporium OB3b is described, and an overview of the enzyme's properties is presented. The pMMO from M. trichosporium OB3b was solubilized in the detergent n-dodecyl-β-D-maltoside and purified by chromatographic techniques. The enzyme consists of 0.9 iron atoms and 12.8 copper atoms per molecule. The iron site in pMMO may be mononuclear non-heme iron. Copper exists as either copper ion coupled to four nitrogen atoms and/or trinuclear copper cluster wherein copper ions are ferromagnetically coupled.

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References

  1. [1]

    R.I. Hanson and T.E. Hanson, Microbiol. Rev. 60 (1996) 439.

  2. [2]

    D. Scott, J. Brannan and I.J. Higgins, J. Gen. Microbiol. 125 (1981) 63.

  3. [3]

    H. Dalton, in: Methane and Methanol Utilizer, eds. J.C. Murrell and H. Dalton (Plenum, New York, 1992) p. 85.

  4. [4]

    S.J. Lippard, in: Bioinorganic Chemistry, ed. D.P. Kessissoglou (Kluwer Academic, Dordrecht, 1995) p. 1.

  5. [5]

    J.C. Murrel, FEMS Microbiol. Rev. 88 (1992) 233.

  6. [6]

    J.D. Lipscomb, Annu. Rev. Microbiol. 48 (1994) 371.

  7. [7]

    Y. Liu, J.C. Nesheim, S.-K. Lee and J.D. Lipscomb, J. Biol. Chem. 270 (1995) 24662.

  8. [8]

    S.C. Pulver, W.A. Froland, J.D. Lipscomb and E.D. Solomon, J. Am. Chem. Soc. 119 (1997) 387.

  9. [9]

    Y. Shinohara, H. Uchiyama, O. Yagi and I. Kusahara, J. Ferment. Bioeng. 85 (1998) 37.

  10. [10]

    J.A. Zahn and A.A. DiSpirito, J. Bacteriol. 178 (1996) 1018.

  11. [11]

    M. Takeguchi, K. Miyakawa and I. Okura, J. Mol. Catal. 132 (1998) 145.

  12. [12]

    H.-H.T. Nguyen, A.K. Sheimke, S.J. Jacobs, B.J. Hales, M.E. Lidstrom and S.I. Chan, J. Biol. Chem. 269 (1994) 14995.

  13. [13]

    J.D. Semrau, D. Zolandz, M.E. Lidstrom and S.I. Chan, J. Inorg. Biochem. 58 (1995) 235.

  14. [14]

    H.-H.T. Nguyen, K.H. Nakagawa, B. Hedman, S.J. Elliott, M.E. Lidstrom, K.O. Hodgson and S.I. Chan, J. Am. Chem. Soc. 118 (1996) 12766.

  15. [15]

    G.A. Brussseau, H.-C. Tsien, R.S. Richard and L.P. Wackett, Biodegradation 1 (1990) 19.

  16. [16]

    A.K. Shiemke, S.A. Cook, T. Miley and P. Singleton, Arch. Biochem. Biophys. 321 (1995) 421.

  17. [17]

    M. Takeguchi, K. Miyakawa and I. Okura, BioMetals 11 (1998) 229.

  18. [18]

    C. Bedard and R. Knowles, Microbiol. Rev. 53 (1989) 68.

  19. [19]

    A.J. Holmes, A. Costello, J.C. Murrell and M.E. Lidstrom, FEMS Microbiol. Lett. 132 (1995) 203.

  20. [20]

    J.D. Senrau, A. Christoserdov, J. Lebron, A. Costello, J. Davagnino, E. Kenna, A.J. Holmes, R. Finch, J.C. Murrell and M.E. Lidstrom, J. Bacteriol. 177 (1995) 3071.

  21. [21]

    L.Y. Juliette, M.R. Hyman and D.J. Arp, J. Bacteriol. 177 (1995) 4908.

  22. [22]

    M. Takeguchi and I. Okura, J. Mol. Catal. 145 (1999) 45.

  23. [23]

    A.A. DiSpirito, J. Gulledge, A.K. Shiemke, J.C. Murrell, M.E. Lidstrom and C.L. Krema, Biodegradation 2 (1992) 105.

  24. [24]

    M. Takeguchi, K. Miyakawa and I. Okura, J. Mol. Catal. 137 (1999) 161.

  25. [25]

    I. Suzuki and S.-C. Kwok, Biochem. Biophys. Res. Commun. 39 (1970) 950.

  26. [26]

    I.A. Tukhvatullin, L.A. Korshunova, R.I. Grpzdev and H. Dalton, Biochemistry (Moscow) 61 (1996) 886.

  27. [27]

    M. Takeguchi, T. Yamada, T. Kamachi and I. Okura, BioMetals 12 (1999) 27.

  28. [28]

    S.D. Prior and H. Dalton, FEMS Microbiol. Lett. 29 (1985) 105.

  29. [29]

    J.A. Zahn, D.M. Arciero, A.B. Hopper and A.A. DiSprito, FEMS Lett. 397 (1996) 35.

  30. [30]

    D.M. Arciero, J.D. Lipscomb, B.H. Huynh, T.A. Kent and E. Munck, J. Biol. Chem. 258 (1983) 14981.

  31. [31]

    J. Peisach and W.E. Blumberg, Arch. Biochem. Biophys. 165 (1974) 691.

  32. [32]

    D.H. Yokoi and A.W. Addison, Inorg. Chem. 16 (1977) 1341.

  33. [33]

    D. Kvelson and R. Neiman, Chem. Phys. 35 (1961) 149.

  34. [34]

    T. Sawada, K. Fukumaru and H. Sakurai, Chem. Pharm. Bull. 44 (1996) 1009.

  35. [35]

    W.B. Mims and J. Peisach, J. Chem. Phys. 69 (1978) 4921.

  36. [36]

    S.J. Elliott, D.W. Randall, R.D. Britt and S.I. Chan, J. Am. Chem. Soc. 120 (1998) 3247.

  37. [37]

    K. Fukui, H. Ohya-Nishiguchi and H. Kamada, Inorg. Chem. 36 (1997) 5518.

  38. [38]

    K. Fukui, H. Ohya-Nishiguchi M. Iwaizumi and Y. Xu, Bull. Chem. Soc. Jpn. 71 (1998) 2787.

  39. [39]

    H. Barkhuijsen, R. De Beer, W.M.M.J. Bovee and D. Van Ormondt, J. Magn. Reson. 61 (1985) 465.

  40. [40]

    D.S. Stephenson, Prog. NMR Spectrosc. 20 (1988) 515.

  41. [41]

    J. Li, C.J. Bender, J. McCracken, J. Peisach, J.C. Severns and D.R. McMillin, Biochemistry 31 (1992) 6265.

  42. [42]

    H. Yuan, M.L.P. Collins and W.E. Antholine, J. Inorg. Biochem. 72 (1998) 179.

  43. [43]

    H. Yuan, M.L.P. Collins and W.E. Antholine, Biophys. J. 76 (1999) 2223.

  44. [44]

    W.B. Mims and J. Peisach, in: Advanced EPR; Application in Biology and Biochemistry, ed. A.J. Hoff (Elsevier, Amsterdam, 1989) p. 1.

  45. [45]

    M. Takeguchi, M. Ohashi and I. Okura, BioMetals 12 (1999) 123.

  46. [46]

    J.A. Zahn, D. Arciero, A.B. Hooper and A.A. DiSpirito, FEBS Lett. 397 (1996) 35.

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Takeguchi, M., Okura, I. Role of iron and copper in particulate methane monooxygenase of Methylosinus trichosporium OB3b. Catalysis Surveys from Asia 4, 51–63 (2000). https://doi.org/10.1023/A:1019036105038

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  • particulate methane monooxygenase
  • methanotrophs
  • Methylosinus trichosporium OB3b
  • methane