PubReading [39] - Crystal structure of a membrane-bound metalloenzyme that catalyses the biological oxidation of methane - R. L. Lieberman and A. C. Rosenzweig

<p>Particulate <strong>methane monooxygenase</strong> (pMMO) is an integral membrane metalloenzyme that <strong>catalyses</strong> 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 <strong>pMMO</strong> from the methanotroph Methylococcus capsulatus (Bath) to a resolution of 2.8A ̊. The enzyme is a trimer with an a3b3g3 polypeptide arrangement. Two metal centres, modelled as mononuclear <strong>copper</strong> and dinuclear copper, are located in soluble regions of each pmoB subunit, which resembles <strong>cytochrome c oxidase</strong> 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. - <a href="https://doi.org/10.1038/nature03311" rel="noopener noreferrer nofollow">doi.org/10.1038/nature03311</a> - 2005</p>