Methyl-coenzyme M reductase (MCR) is the key rate-determining enzyme of methanogenesis and anaerobic methane oxidation, the essential energy metabolisms of methanogenic archaea and anaerobic methanotrophs (ANME), respectively. Given the role of methane as both a potent greenhouse gas as well as a valuable energy source, understanding its production and consumption in nature is becoming increasingly important. Although methanogenic MCR has been extensively studied, revealing key biochemical and mechanistic insights, the enzymatic properties of ANME MCR have never been reported. This is primarily due the difficulty in culturing these organisms which have extremely slow growth rates. MCR is a heterohexamer and requires coenzyme F430 for proper assembly and enzymatic activity, making it difficult to obtain an effective heterologous expression system for this complex enzyme. Here we report our progress in the development of such a system for expressing recombinant ANME MCR in the model methanogen, <i>Methanococcus maripaludis</i>. This work lays the foundation for future biochemical and mechanistic studies of anaerobic C-H bond activation catalyzed by ANME MCR.

Recombinant expression and assembly of methyl-coenzyme M reductase from anaerobic methanotrophs

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

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