Bacteria that oxidize methane into methanol are fundamental to mitigating emissions of methane. The character of the copper active site from the principal metabolic receptor of the bacteria, particulate methane monooxygenase (pMMO), has been controversial owing to seemingly contradictory biochemical, spectroscopic, and crystallographic results. We provide biochemical and electron paramagnetic resonance spectroscopic characterization most consistent with two monocopper websites within pMMO: 1 at the soluble PmoB subunit at the previously assigned active site (CuB) and one ~2 nanometers away from the membrane-bound PmoC subunit (CuC). On the basis of the results, we propose a monocopper website can catalyze methane oxidation in pMMO.