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

Nature volume 434, pages 177–182 (2005)Cite this article

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.

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Figure 1: The pMMO trimer viewed parallel to the membrane normal (a) and perpendicular to the membrane normal (b).
Figure 2: The pMMO subunits.
Figure 3: Comparison of pmoB (magenta) with Paracoccus denitrificans cytochrome c oxidase subunit II (green, PDB accession code 1AR1).
Figure 4: The pMMO metal centres viewed approximately 90° from the orientation shown in Fig. 2a.

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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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Authors and Affiliations

  1. Departments of Biochemistry, Molecular Biology, and Cell Biology and of Chemistry, Northwestern University, Evanston, Illinois, 60208, USA

    Raquel L. Lieberman & Amy C. Rosenzweig

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  1. Raquel L. Lieberman
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Correspondence to Amy C. Rosenzweig.

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Supplementary information

Supplementary Table S1

Data collection and refinement statistics for pMMO crystal structure determination. (DOC 30 kb)

Supplementary Figure S1

Patch of unmodelled electron density in the pmoB subunit with duroquinone superimposed. (DOC 1366 kb)

Supplementary Figure S2

Electrostatic surface representation of the pMMO protomer. (DOC 1149 kb)

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Lieberman, R., Rosenzweig, A. Crystal structure of a membrane-bound metalloenzyme that catalyses the biological oxidation of methane. Nature 434, 177–182 (2005). https://doi.org/10.1038/nature03311

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