Impact of subunit and oligomeric structure on the thermal and conformational stability of chlorite dismutases

► Comparison of two chlorite dismutases of different subunit and oligomeric structure but similar enzymatic activity. ► Significant differences in conformational and thermal stability due to different subunit interactions. ► Pentameric (canonical) chlorite dismutase exhibits a high thermal stability and enzymatic activity at high temperatures. ► Presented thermodynamic data are representative for chlorite dismutases of two distinct phylogenetic lineages.