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Biochemistry

Getting the metal right

Nature volume 465, pages 40–41 (2010)Cite this article

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Controversy has raged over the identity of the metal cofactor of membrane-bound methane monooxygenase, a methane-oxidizing enzyme. A study suggests that the answer is a cluster of two copper ions.

Enzymes that catalyse redox reactions often use metal ions to bind and activate substrates, and to carry and distribute electrons. But during the isolation of such an enzyme from its natural source, the metal-containing cofactor can degrade, causing the enzyme to lose activity. Extensively purified enzyme preparations can thus be severely heterogeneous in their cofactor composition. In the worst-case scenario, a minor, undetected form of a purified enzyme can contribute all the catalytic activity. This complicates the seemingly simple task of identifying the functional metal cofactors of enzymes, as recent high-profile controversies involving several metalloenzymes document. On page 115 of this issue, Balasubramanian et al.1 resolve one of the most intriguing of these controversies, establishing the nature of the metal-ion cofactor in the membrane-bound (particulate) variety of the important enzyme methane monooxygenase (pMMO).

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Figure 1: Structure of membrane-bound methane monooxygenase (pMMO).

References

  1. Balasubramanian, R. et al. Nature 465, 115–119 (2010).

    Article  ADS  CAS  Google Scholar 

  2. Hakemian, A. S. & Rosenzweig, A. C. Annu. Rev. Biochem. 76, 223–241 (2007).

    Article  CAS  Google Scholar 

  3. Kovaleva, E. G., Neibergall, M. B., Chakrabarty, S. & Lipscomb, J. D. Acc. Chem. Res. 40, 475–483 (2007).

    Article  CAS  Google Scholar 

  4. Merkx, M. et al. Angew. Chem. Int. Edn 40, 2782–2807 (2001).

    Article  CAS  Google Scholar 

  5. Rosenzweig, A. C. Biochem. Soc. Trans. 36, 1134–1137 (2008).

    Article  CAS  Google Scholar 

  6. Wilkinson, B. et al. J. Am. Chem. Soc. 118, 921–922 (1996).

    Article  CAS  Google Scholar 

  7. Chan, S. I. et al. Angew. Chem. Int. Edn 46, 1992–1994 (2007).

    Article  CAS  Google Scholar 

  8. Chen, K. H.-C. J. Chin. Chem. Soc. 51, 1081–1098 (2004).

    Article  CAS  Google Scholar 

  9. Ngyuen, H.-H. T. et al. J. Am. Chem. Soc. 118, 12766–12776 (1996).

    Article  Google Scholar 

  10. Yu, S. S. et al. Biochemistry 46, 13762–13774 (2007).

    Article  CAS  Google Scholar 

  11. Hakemian, A. S. et al. Biochemistry 47, 6793–6801 (2008).

    Article  CAS  Google Scholar 

  12. Lieberman, R. L. & Rosenzweig, A. C. Nature 434, 177–182 (2005).

    Article  ADS  CAS  Google Scholar 

  13. Martinho, M. et al. J. Am. Chem. Soc. 129, 15783–15785 (2007).

    Article  CAS  Google Scholar 

  14. Woertink, J. S. et al. Proc. Natl Acad. Sci. USA 106, 18908–18913 (2009).

    Article  ADS  CAS  Google Scholar 

Download references

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  1. J. Martin Bollinger Jr is in the Departments of Chemistry, and Biochemistry and Molecular Biology, Penn State University, University Park, Pennsylvania 16802, USA. jmb21@psu.edu,

    J. Martin Bollinger Jr

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  1. J. Martin Bollinger Jr
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Bollinger Jr, J. Getting the metal right. Nature 465, 40–41 (2010). https://doi.org/10.1038/465040a

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