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

Raquel L. Lieberman; Amy C. Rosenzweig

doi:10.1038/nature03311

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

Raquel L. Lieberman, Amy C. Rosenzweig^*

^*Corresponding author for this work

CLP - Chemistry of Life Processes Institute

Research output: Contribution to journal › Article › peer-review

571 Scopus citations

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 α₃β ₃γ₃ 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.

Original language	English (US)
Pages (from-to)	177-182
Number of pages	6
Journal	Nature
Volume	434
Issue number	7030
DOIs	https://doi.org/10.1038/nature03311
State	Published - Mar 10 2005

Funding

Acknowledgements This work was supported by a grant from the American Chemical Society Petroleum Research Fund (A.C.R.), funds from the David and Lucile Packard Foundation (A.C.R.), and the NIH (A.C.R.). R.L.L. was supported in part by a NIH training grant. We thank D. Shrestha for assistance cultivating M. capsulatus (Bath), M. Sommerhalter for assistance with data collection, J. Brunzelle for suggestions, Z. Wawrzak for assistance with data collection, and B. Hoffman, T. Stemmler, and K. Karlin for discussions.

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10.1038/nature03311

Cite this

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title = "Crystal structure of a membrane-bound metalloenzyme that catalyses the biological oxidation of methane",

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 {\AA}. The enzyme is a trimer with an α3β 3γ3 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.",

author = "Lieberman, {Raquel L.} and Rosenzweig, {Amy C.}",

note = "Funding Information: Acknowledgements This work was supported by a grant from the American Chemical Society Petroleum Research Fund (A.C.R.), funds from the David and Lucile Packard Foundation (A.C.R.), and the NIH (A.C.R.). R.L.L. was supported in part by a NIH training grant. We thank D. Shrestha for assistance cultivating M. capsulatus (Bath), M. Sommerhalter for assistance with data collection, J. Brunzelle for suggestions, Z. Wawrzak for assistance with data collection, and B. Hoffman, T. Stemmler, and K. Karlin for discussions.",

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AU - Rosenzweig, Amy C.

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N2 - 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 α3β 3γ3 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.

AB - 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 α3β 3γ3 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.

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

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Crystal structure of particulate methane monooxygenase

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

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Crystal structure of particulate methane monooxygenase

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