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

Silvan Scheller, Meike Goenrich, Reinhard Boecher, Rudolf K. Thauer, Bernhard Jaun*

*Corresponding author for this work

Research output: Contribution to journalArticle

204 Citations (Scopus)

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 bacteria1-3, 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 sulphate6-8. This result supports the hypothesis of reverse methanogenesis4,9 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 chemistry10-13.

Original languageEnglish
Pages (from-to)606-608
Number of pages3
JournalNature
Volume465
Issue number7298
DOIs
Publication statusPublished - 3 Jun 2010
MoE publication typeA1 Journal article-refereed

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