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) |
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Pages (from-to) | 177-182 |
Number of pages | 6 |
Journal | Nature |
Volume | 434 |
Issue number | 7030 |
DOIs | |
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.
ASJC Scopus subject areas
- General
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Crystal structure of particulate methane monooxygenase
Lieberman, R. L. (Contributor) & Rosenzweig, A. C. (Contributor), Protein Data Bank (PDB), Feb 8 2005
DOI: 10.2210/pdb1YEW/pdb, https://www.wwpdb.org/pdb?id=pdb_00001yew
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