Intermediates in the catalytic cycle of methyl coenzyme M reductase: Isotope exchange is consistent with formation of a σ-Alkane-Nickel Complex

Silvan Scheller*, Meike Goenrich, Stefan Mayr, Rudolf K. Thauer, Bernhard Jaun

*Corresponding author for this work

Research output: Contribution to journalArticleScientificpeer-review

36 Citations (Scopus)

Abstract

The key nickel enzyme for methanogenesis (MCR) catalyzes the formation of CH3D and CH2D2 in a deuterated medium. CH 2D2 is formed by an exchange of deuterium into the S-methyl group of the substrate. Deuterium is incorporated at both carbon atoms of the S-ethyl group of ethyl coenzyme M, and a 13C label is rapidly scrambled within the ethyl group (see scheme). Thus, at least one intermediate is formed and the isotope exchange pattern is consistent with formation of a σ-alkane-nickel complex.

Original languageEnglish
Pages (from-to)8112-8115
Number of pages4
JournalAngewandte Chemie
Volume49
Issue number44
DOIs
Publication statusPublished - 25 Oct 2010
MoE publication typeA1 Journal article-refereed

Keywords

  • σ-alkane ligands
  • C-H activation
  • Isotope exchange
  • Methyl coenzyme M reductase
  • Nickel enzymes

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