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Title: In vitro methanol production from methyl coenzyme M using the Methanosarcina barkeri MtaABC protein complex

Journal Article · · Biotechnology Progress
DOI:https://doi.org/10.1002/btpr.2503· OSTI ID:1533125

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

Research Organization:
Univ. of Delaware, Newark, DE (United States)
Sponsoring Organization:
USDOE Advanced Research Projects Agency - Energy (ARPA-E)
Grant/Contract Number:
AR0000432; DE‐AR0000432
OSTI ID:
1533125
Alternate ID(s):
OSTI ID: 1399795
Journal Information:
Biotechnology Progress, Vol. 33, Issue 5; ISSN 8756-7938
Publisher:
Society for Biological EngineeringCopyright Statement
Country of Publication:
United States
Language:
English
Citation Metrics:
Cited by: 7 works
Citation information provided by
Web of Science

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Cited By (1)

Co-occurring genomic capacity for anaerobic methane and dissimilatory sulfur metabolisms discovered in the Korarchaeota journal March 2019