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 language | English |
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Pages (from-to) | 8112-8115 |
Number of pages | 4 |
Journal | Angewandte Chemie |
Volume | 49 |
Issue number | 44 |
DOIs | |
Publication status | Published - 25 Oct 2010 |
MoE publication type | A1 Journal article-refereed |
Keywords
- σ-alkane ligands
- C-H activation
- Isotope exchange
- Methyl coenzyme M reductase
- Nickel enzymes