In vitro methanol production from methyl coenzyme M using the Methanosarcina barkeri MtaABC protein complex. (12th June 2017)

• Record Type: Journal Article
• Authors: Dong, Ming; Gonzalez, Tara D.; Klems, Meghan M.; Steinberg, Lisa M.; Chen, Wilfred; Papoutsakis, Eleftherios T.; Bahnson, Brian J.
• Is Part Of: Biotechnology progress. Volume 33:Number 5(2017)
• Page Start: 1243
• Page End: 1249
• Publication Date: 2017-06-12
• Subjects: anaerobic methane oxidation -- methanol from methane -- methanogens -- CoM -- Zn enzyme -- corrinoid; Biotechnology -- Periodicals; Food industry and trade -- Periodicals; Bioengineering -- Periodicals; 660.6
• DOI: 10.1002/btpr.2503
• Languages: English
• ISSNs: 8756-7938

Abstract

Abstract : Methanol:coenzyme M methyltransferase is an enzyme complex composed of three subunits, MtaA, MtaB, and MtaC, found in methanogenic archaea and is needed for their growth on methanol ultimately producing methane. MtaABC catalyzes the energetically favorable methyl transfer from methanol to coenzyme M to form methyl coenzyme M. Here we demonstrate that this important reaction for possible production of methanol from the anaerobic oxidation of methane can be reversed in vitro. To this effect, we have expressed and purified the Methanosarcina barkeri MtaABC enzyme, and developed an in vitro functional assay that demonstrates MtaABC can catalyze the energetically unfavorable (Δ G ° = 27 kJ/mol) reverse reaction starting from methyl coenzyme M and generating methanol as a product. Demonstration of an in vitro ability of MtaABC to produce methanol may ultimately enable the anaerobic oxidation of methane to produce methanol and from methanol alternative fuel or fuel‐precursor molecules. © 2017 American Institute of Chemical Engineers Biotechnol. Prog., 33:1243–1249, 2017