The effect of the lipid oxidation product, 4-hydroxy-2-nonenal (HNE), on oxidation of oxymyoglobin (OxyMb) from seven different meat-producing species was investigated. Relative to controls, HNE increased OxyMb oxidation within all species (p < 0.05) at both 25 and 4 °C, pH 5.6. The relative effect of HNE was greater for myoglobins (Mbs) that contained 12 ± 1 histidine (His) residues than for those that contained 9 His residues (p < 0.05); HNE efficacy in all species except chicken and turkey decreased with time. Mono-HNE adducts were detected in all species except chicken and turkey. In general, HNE alkylation increased the Mbs' ability to accelerate lipid oxidation in a microsome model. However, neither an HNE nor a Mb species dependent effect was observed. Results suggested that microsome model system associated lipid oxidation overshadowed HNE and species effects on OxyMb oxidation observed in lipid-free systems.