Oxidation of methane by a biological dicopper centre

Ramakrishnan Balasubramanian, Stephen M. Smith, Swati Rawat, Liliya A. Yatsunyk, Timothy L. Stemmler () and Amy C. Rosenzweig ()
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Ramakrishnan Balasubramanian: Molecular Biology and Cell Biology
Stephen M. Smith: Molecular Biology and Cell Biology
Swati Rawat: Wayne State University, School of Medicine, Detroit, Michigan 48201, USA
Liliya A. Yatsunyk: Molecular Biology and Cell Biology
Timothy L. Stemmler: Wayne State University, School of Medicine, Detroit, Michigan 48201, USA
Amy C. Rosenzweig: Molecular Biology and Cell Biology

Nature, 2010, vol. 465, issue 7294, 115-119

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.

Date: 2010
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DOI: 10.1038/nature08992

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