Simply surviving within terrestrial and marine environments alike can pose considerable challenges to microbial life. Nutrient scarcity and fierce intermicrobial competition often place severe restrictions on growth and necessitate a transition to a state of dormancy until conditions improve. While the cessation of growth and replication embody the most obvious characteristics of dormancy, minimal metabolic activity is required to sustain cellular integrity and maintenance. Many members of the bacterial genus Mycobacterium leverage their metabolic flexibility during dormancy to prolong survival when confronted with resource deprivation. As organoheterotrophs, mycobacteria depend on organic carbon as electron donors to supply their respiratory chains during growth. During carbon starvation, the atmospheric trace gas carbon monoxide (CO) is one energetic lifeline available to otherwise electron donor deficient mycobacteria. In the soil dwelling Mycobacterium smegmatis, the multisubunit enzyme complex Carbon Monoxide DeHydrogenase (CODH) mediates the scavenging of atmospheric CO via oxidation and hydroxylation at a molybdenum-copper centre and subsequent shuttling of electrons to the respiratory chain through a relay of iron-sulfur clusters and a flavin cofactor. CO scavenging has been demonstrated to be upregulated and increase survival during carbon starvation. However, the biochemical characteristics that underpin the high affinity required to oxidise atmospheric concentrations of CO, and how CO-liberated electrons enter the respiratory chain, both remain to be understood. Here, we present current progress towards the biochemical and structural characterisation of CODH. CODH has been natively purified from M. smegmatis using a chromosomal strep-tag approach, and subject to structural analysis via Cryo-EM. Enzymatic assays with purified CODH are in progress to determine the kinetic parameters of CO oxidation and to identify the native electron acceptor.