Methane gas is a major contributor to climate change, which presents a significant threat to human health. Methane oxidation by methanotrophic bacteria is a promising route for bioremediation of this potent greenhouse gas. The methane monooxygenase enzymes (MMOs) that perform this chemically challenging reaction are metalloenzymes that can either be soluble (sMMO) or membrane-bound (particulate MMO, pMMO). The pMMO is a copper-dependent enzyme that is found in methanotroph intracytoplasmic membranes (ICMs), organized into hexagonal arrays. pMMO is only active in a lipid environment, indicating the essential role of the membrane in the methane oxidation activity. Previous studies of pMMO in detergent micelles, native lipid nanodiscs, synthetic lipid nanodiscs, and native membranes enabled comparisons of activity in different lipid environments. However, the nanodiscs only encapsulate a single pMMO trimer and do not allow for the study of these hexagonal arrays. In this study, we developed a proteoliposome system that allows for reconstitution of the hexagonal array organization of pMMO found in the native ICMs. Our results show that liposome-incorporated pMMO exhibits markedly enhanced methane oxidation compared to enzyme preparations in nanodiscs. Additionally, the effects of specific lipids could be dissected in synthetic lipid liposomes. By encapsulating dyes within the liposomes, we were able to monitor the transport of ions and small molecules across the bilayer, linking membrane dynamics with pMMO function. These findings underscore the critical role of native lipids in optimizing pMMO activity.