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

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

Authors:
 [1];  [1];  [1];  [1]; ORCiD logo [1];  [1];  [1]
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  1. Univ. of Delaware, Newark, DE (United States)
Publication Date:
Research Org.:
Univ. of Delaware, Newark, DE (United States)
Sponsoring Org.:
USDOE Advanced Research Projects Agency - Energy (ARPA-E)
OSTI Identifier:
1533125
Alternate Identifier(s):
OSTI ID: 1399795
Grant/Contract Number:  
AR0000432; DE‐AR0000432
Resource Type:
Accepted Manuscript
Journal Name:
Biotechnology Progress
Additional Journal Information:
Journal Volume: 33; Journal Issue: 5; Journal ID: ISSN 8756-7938
Publisher:
Society for Biological Engineering
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; biotechnology & applied microbiology; food science & technology; anaerobic methane oxidation; methanol from methane; methanogens; CoM; Zn enzyme; corrinoid

Citation Formats

Dong, Ming, Gonzalez, Tara D., Klems, Meghan M., Steinberg, Lisa M., Chen, Wilfred, Papoutsakis, Eleftherios T., and Bahnson, Brian J. In vitro methanol production from methyl coenzyme M using the Methanosarcina barkeri MtaABC protein complex. United States: N. p., 2017. Web. doi:10.1002/btpr.2503.
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Dong, Ming, Gonzalez, Tara D., Klems, Meghan M., Steinberg, Lisa M., Chen, Wilfred, Papoutsakis, Eleftherios T., & Bahnson, Brian J. In vitro methanol production from methyl coenzyme M using the Methanosarcina barkeri MtaABC protein complex. United States. https://doi.org/10.1002/btpr.2503
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Dong, Ming, Gonzalez, Tara D., Klems, Meghan M., Steinberg, Lisa M., Chen, Wilfred, Papoutsakis, Eleftherios T., and Bahnson, Brian J. Sat . "In vitro methanol production from methyl coenzyme M using the Methanosarcina barkeri MtaABC protein complex". United States. https://doi.org/10.1002/btpr.2503. https://www.osti.gov/servlets/purl/1533125.
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@article{osti_1533125,
title = {In vitro methanol production from methyl coenzyme M using the Methanosarcina barkeri MtaABC protein complex},
author = {Dong, Ming and Gonzalez, Tara D. and Klems, Meghan M. and Steinberg, Lisa M. and Chen, Wilfred and Papoutsakis, Eleftherios T. and Bahnson, Brian J.},
abstractNote = {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},
doi = {10.1002/btpr.2503},
journal = {Biotechnology Progress},
number = 5,
volume = 33,
place = {United States},
year = {Sat May 27 00:00:00 EDT 2017},
month = {Sat May 27 00:00:00 EDT 2017}
}
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https://doi.org/10.1002/btpr.2503
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Works referenced in this record:

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journal, December 2005

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    Works referencing / citing this record:

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