Aerobic methanotrophy is strongly controlled by copper, and methanotrophs are known to use different mechanisms for copper uptake. Some methanotrophs secrete a modified polypeptide—methanobactin—while others utilize a surface-bound protein (MopE) and a secreted form of it (MopE*) for copper collection. As different methanotrophs have different means of sequestering copper, competition for copper significantly impacts methanotrophic activity. Herein, we show that Methylomicrobium albumBG8, Methylocystissp. strain Rockwell, and Methylococcus capsulatusBath, all lacking genes for methanobactin biosynthesis, are not limited for copper by multiple forms of methanobactin. Interestingly, Mm. albumBG8 and Methylocystissp. strain Rockwell were found to have genes similar to mbnTthat encodes for a TonB-dependent transporter required for methanobactin uptake. Data indicate that these methanotrophs “steal” methanobactin and such “theft” enhances the ability of these strains to degrade methylmercury, a potent neurotoxin. Further, when mbnTwas deleted in Mm. albumBG8, methylmercury degradation in the presence of methanobactin was indistinguishable from when MB was not added. Mc. capsulatusBath lacks anything similar to mbnTand was unable to degrade methylmercury either in the presence or absence of methanobactin. Rather, Mc. capsulatusBath appears to rely on MopE/MopE* for copper collection. Finally, not only does Mm. albumBG8 steal methanobactin, it synthesizes a novel chalkophore, suggesting that some methanotrophs utilize both competition and cheating strategies for copper collection. Through a better understanding of these strategies, methanotrophic communities may be more effectively manipulated to reduce methane emissions and also enhance mercury detoxification in situ.