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Crystal structure of a membrane-bound metalloenzyme that catalyses the biological oxidation of methane

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  • Raquel L. Lieberman

    (Northwestern University)

  • Amy C. Rosenzweig

    (Northwestern University)

Abstract

Particulate methane monooxygenase (pMMO) is an integral membrane metalloenzyme that catalyses the conversion of methane to methanol. Knowledge of how pMMO performs this extremely challenging chemistry may have an impact on the use of methane as an alternative energy source by facilitating the development of new synthetic catalysts. We have determined the structure of pMMO from the methanotroph Methylococcus capsulatus (Bath) to a resolution of 2.8 Å. The enzyme is a trimer with an α3β3γ3 polypeptide arrangement. Two metal centres, modelled as mononuclear copper and dinuclear copper, are located in soluble regions of each pmoB subunit, which resembles cytochrome c oxidase subunit II. A third metal centre, occupied by zinc in the crystal, is located within the membrane. The structure provides new insight into the molecular details of biological methane oxidation.

Suggested Citation

  • Raquel L. Lieberman & Amy C. Rosenzweig, 2005. "Crystal structure of a membrane-bound metalloenzyme that catalyses the biological oxidation of methane," Nature, Nature, vol. 434(7030), pages 177-182, March.
  • Handle: RePEc:nat:nature:v:434:y:2005:i:7030:d:10.1038_nature03311
    DOI: 10.1038/nature03311
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    Cited by:

    1. Hailong Zhang & Peijie Han & Danfeng Wu & Congcong Du & Jiafei Zhao & Kelvin H. L. Zhang & Jingdong Lin & Shaolong Wan & Jianyu Huang & Shuai Wang & Haifeng Xiong & Yong Wang, 2023. "Confined Cu-OH single sites in SSZ-13 zeolite for the direct oxidation of methane to methanol," Nature Communications, Nature, vol. 14(1), pages 1-10, December.
    2. Yanan Zhu & Christopher W. Koo & C. Keith Cassidy & Matthew C. Spink & Tao Ni & Laura C. Zanetti-Domingues & Benji Bateman & Marisa L. Martin-Fernandez & Juan Shen & Yuewen Sheng & Yun Song & Zhengyi , 2022. "Structure and activity of particulate methane monooxygenase arrays in methanotrophs," Nature Communications, Nature, vol. 13(1), pages 1-10, December.

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