Skip to main content

Computational Mechanistic Studies of Methyl-coenzyme M Reductase Enzyme


EMSL Project ID
60322

Abstract

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 the key enzyme in the methane biological conversion by microbial communities containing sulfate- or nitrate-reducing bacteria. 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 a Ni-based cofactor F430. MCR also catalyzes the reverse reaction in methane oxidizing archaea. We postulate that “methanotrophic” and “methanogenic” MCRs achieve a catalytic bias toward utilizing or producing methane though changes in protein confinement of substrates both at the active site and along the substrate channel. We will use advanced computational approaches to explore the specific contribution of the protein environment to the reactivity in this important system.

Project Details

Project type
Large-Scale EMSL Research
Start Date
2022-10-01
End Date
N/A
Status
Active

Team

Principal Investigator

Bojana Ginovska
Institution
Pacific Northwest National Laboratory

Co-Investigator(s)

Simone Raugei
Institution
Pacific Northwest National Laboratory

Team Members

Maureen Kitheka
Institution
Pacific Northwest National Laboratory

Nathan Wong
Institution
Duke University

Busra Dereli Caglayan
Institution
Pacific Northwest National Laboratory

Suman Samantray
Institution
Pacific Northwest National Laboratory

Jack Fuller
Institution
Pacific Northwest National Laboratory

Hoshin Kim
Institution
Pacific Northwest National Laboratory

Samantha JI Johnson
Institution
Pacific Northwest National Laboratory

Stephen Ragsdale
Institution
University of Michigan