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Oxidation of methane by a biological dicopper centre

Author

Listed:
  • Ramakrishnan Balasubramanian

    (Molecular Biology and Cell Biology
    Northwestern University, Evanston, Illinois 60208, USA)

  • Stephen M. Smith

    (Molecular Biology and Cell Biology
    Northwestern University, Evanston, Illinois 60208, USA)

  • Swati Rawat

    (Wayne State University, School of Medicine, Detroit, Michigan 48201, USA)

  • Liliya A. Yatsunyk

    (Molecular Biology and Cell Biology
    Northwestern University, Evanston, Illinois 60208, USA)

  • Timothy L. Stemmler

    (Wayne State University, School of Medicine, Detroit, Michigan 48201, USA)

  • Amy C. Rosenzweig

    (Molecular Biology and Cell Biology
    Northwestern University, Evanston, Illinois 60208, USA)

Abstract

Copper-dependent methane monooxygenase Particulate methane monooxygenase (pMMO) is an integral membrane protein that can selectively oxidize methane to methanol. This metalloenzyme contains three subunits, and the metal composition and exact location of the active site of this enzyme has been the subject of much speculation and controversy. In this paper, the authors determined that the pMMO activity is dependent on copper and not — as has been suggested elsewhere — iron. They also determine that the copper active site is located in the soluble domains of the pmoB subunit, not within the membrane portion of the protein.

Suggested Citation

  • Ramakrishnan Balasubramanian & Stephen M. Smith & Swati Rawat & Liliya A. Yatsunyk & Timothy L. Stemmler & Amy C. Rosenzweig, 2010. "Oxidation of methane by a biological dicopper centre," Nature, Nature, vol. 465(7294), pages 115-119, May.
    • Handle: RePEc:nat:nature:v:465:y:2010:i:7294:d:10.1038_nature08992
    DOI: 10.1038/nature08992
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    Cited by:

    1. Yang, Le & Lin, Hongju & Fang, Zhihao & Yang, Yanhui & Liu, Xiaohao & Ouyang, Gangfeng, 2023. "Recent advances on methane partial oxidation toward oxygenates under mild conditions," Renewable and Sustainable Energy Reviews, Elsevier, vol. 184(C).

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