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In vitro methanol production from methyl coenzyme M using the Methanosarcina barkeri MtaABC protein complex
Author(s) -
Dong Ming,
Gonzalez Tara D.,
Klems Meghan M.,
Steinberg Lisa M.,
Chen Wilfred,
Papoutsakis Eleftherios T.,
Bahnson Brian J.
Publication year - 2017
Publication title -
biotechnology progress
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 129
eISSN - 1520-6033
pISSN - 8756-7938
DOI - 10.1002/btpr.2503
Subject(s) - methanosarcina barkeri , methanol , chemistry , methanosarcina , cofactor , methanomicrobiales , biochemistry , methanogenesis , methane , archaea , biosynthesis , enzyme , organic chemistry , gene
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