Methane is the second most abundant greenhouse gas after CO2, which accounts for 14% of global greenhouse gas emissions, and it is by far the largest constituent of natural gas deposits. Methyl-coenzyme M Reductase (MCR) is a key enzyme in the biological conversion of methane. MCR catalyzes the reaction of methyl-coenzyme M (CH3-SCoM) with coenzyme B (HSCoB) in methanogenic archaea to form methane and the heterodisulfide, CoMSSCoB using the Ni-based cofactor F430. Recently, we established that the MCR substrates bind to the active Ni(I) state of MCR through their sulfonate rather than the S atom of the thioether moiety as previously postulated. This finding required a revision of the canonical enzymatic mechanism. Here, we explore the mechanistic details of the methane production and utilization by computationally probing two possible binding mechanisms of the substrates at the active site. Specifically, a variety of computational approaches is employed to interpret spectroscopic measurements and investigate the role of residues suggested to be important for substrate binding/product release and in interactions with the F430 cofactor.

Computational mechanistic studies of methyl-coenzyme M reductase enzyme

Fall 2022 abstracts, posters, and presentations will launch in mid-September.

ACS Fall 2022

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.