Sara Kleindienst, Karuna Chourney, Gao Chen, Robert W. Murdoch, Steven A. Higgins, Ramsunderlyer, Shawn R. Campagna, E. Erin Mack, Edward S. Seger, Robert L. Hettich, Frank E. Löffler
Naturally produced and anthropogenically released DCM can reside in anoxic environments, yet little is known about the diversity of organisms, enzymes, and mechanisms involved in carbon-chlorine bond cleavage in the absence of oxygen. A proteogenomic approach identified two RDases and four corrinoid-dependent methyltransferases expressed by the DCM degrader “ Candidatus Dichloromethanomonas elyunquensis” strain RM, suggesting that reductive dechlorination and methyl group transfer play roles in anaerobic DCM degradation. These findings suggest that the characterized DCM-degrading bacterium Dehalobacterium formicoaceticum and “ Candidatus Dichloromethanomonas elyunquensis” strain RM utilize distinct strategies for carbon-chlorine bond cleavage, indicating that multiple pathways evolved for anaerobic DCM metabolism. The specific proteins (e.g., RDases and methyltransferases) identified in strain RM may have value as biomarkers for monitoring anaerobic DCM degradation in natural and contaminated environments.
Kleindienst S, Chourey K, Chen G, Murdoch RW, Higgins SA, Iyer R, Campagna SR, Mack EE, Seger ES, Hettich RL, Löffler FE. 2019. Proteogenomics reveals novel reductive dehalogenases and methyltransferases expressed during anaerobic dichloromethane metabolism. Applied and Environmental Microbiology 85:e02768-18.