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The key nickel enzyme of methanogenesis catalyses the anaerobic oxidation of methane

Nature volume 465, pages 606–608 (2010)Cite this article

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Abstract

Large amounts (estimates range from 70 Tg per year to 300 Tg per year) of the potent greenhouse gas methane are oxidized to carbon dioxide in marine sediments by communities of methanotrophic archaea and sulphate-reducing bacteria1,2,3, and thus are prevented from escaping into the atmosphere. Indirect evidence indicates that the anaerobic oxidation of methane might proceed as the reverse of archaeal methanogenesis from carbon dioxide with the nickel-containing methyl-coenzyme M reductase (MCR) as the methane-activating enzyme4,5. However, experiments showing that MCR can catalyse the endergonic back reaction have been lacking. Here we report that purified MCR from Methanothermobacter marburgensis converts methane into methyl-coenzyme M under equilibrium conditions with apparent Vmax (maximum rate) and Km (Michaelis constant) values consistent with the observed in vivo kinetics of the anaerobic oxidation of methane with sulphate6,7,8. This result supports the hypothesis of ‘reverse methanogenesis’4,9 and is paramount to understanding the still-unknown mechanism of the last step of methanogenesis. The ability of MCR to cleave the particularly strong C–H bond of methane without the involvement of highly reactive oxygen-derived intermediates is directly relevant to catalytic C–H activation, currently an area of great interest in chemistry10,11,12,13.

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Figure 1: Reverse methanogenesis.
Figure 2: Incorporation of 13 C from 13 CH 4 into the methyl group of CH 3 -S-CoM as catalysed by purified MCR-I from M. marburgensis at 60 °C.
Figure 3: Formation of 13 CH 3 -S-CoM (in μmol) after 30 min at 60 °C.

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Acknowledgements

We thank the Swiss National Science Foundation (S.S. and B.J.; grant 200020-119752) and the Max Planck Society and the Fonds der Chemischen Industrie (M.G., R.B. and R.K.T.) for financial support.

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Authors and Affiliations

  1. Laboratory of Organic Chemistry, ETH Zurich, Wolfgang-Pauli-Str. 10, 8093 Zurich, Switzerland ,

    Silvan Scheller & Bernhard Jaun

  2. Max Planck Institute for Terrestrial Microbiology, Karl-von-Frisch-Str. 10, 35043 Marburg, Germany ,

    Meike Goenrich, Reinhard Boecher & Rudolf K. Thauer

Authors
  1. Silvan Scheller
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  2. Meike Goenrich
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  3. Reinhard Boecher
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  4. Rudolf K. Thauer
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  5. Bernhard Jaun
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Contributions

B.J., R.K.T. and S.S. conceived and planned the experiments. S.S. carried out the synthesis of substrates, the NMR measurements and data analysis. M.G. and R.B. purified the enzyme, and S.S., M.G. and R.B. carried out the assays for the reverse reaction. B.J., R.K.T. and S.S. wrote the manuscript. All authors discussed and edited the manuscript.

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Correspondence to Bernhard Jaun.

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The authors declare no competing financial interests.

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This file contains Supplementary Figures S1-S5 with legends, Supplementary Tables 1-3, Supplementary Notes, a Supplementary Discussion and References. (PDF 926 kb)

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Scheller, S., Goenrich, M., Boecher, R. et al. The key nickel enzyme of methanogenesis catalyses the anaerobic oxidation of methane. Nature 465, 606–608 (2010). https://doi.org/10.1038/nature09015

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