A nickel hydride complex in the active site of methyl-coenzyme M reductase: implications for the catalytic cycle

Harmer, Jeffrey, Finazzo, Cinzia, Piskorski, Rafal, Ebner, Sieglinde, Duin, Evert C., Goenrich, Meike, Thauer, Rudolf K., Reiher, Markus, Schweiger, Arthur, Hinderberger, Dariush and Jaun, Bernhard (2008) A nickel hydride complex in the active site of methyl-coenzyme M reductase: implications for the catalytic cycle. Journal of the American Chemical Society, 130 33: 10907-10920. doi:10.1021/ja710949e


Author Harmer, Jeffrey
Finazzo, Cinzia
Piskorski, Rafal
Ebner, Sieglinde
Duin, Evert C.
Goenrich, Meike
Thauer, Rudolf K.
Reiher, Markus
Schweiger, Arthur
Hinderberger, Dariush
Jaun, Bernhard
Title A nickel hydride complex in the active site of methyl-coenzyme M reductase: implications for the catalytic cycle
Journal name Journal of the American Chemical Society   Check publisher's open access policy
ISSN 0002-7863
1520-5126
Publication date 2008-08
Sub-type Article (original research)
DOI 10.1021/ja710949e
Volume 130
Issue 33
Start page 10907
End page 10920
Total pages 14
Place of publication Washington, United State
Publisher American Chemical Society
Language eng
Formatted abstract
Methanogenic archaea utilize a specific pathway in their metabolism, converting C1 substrates (i.e., CO2) or acetate to methane and thereby providing energy for the cell. Methyl-coenzyme M reductase (MCR) catalyzes the key step in the process, namely methyl-coenzyme M (CH3-S-CoM) plus coenzyme B (HS-CoB) to methane and CoM-S-S-CoB. The active site of MCR contains the nickel porphinoid F430. We report here on the coordinated ligands of the two paramagnetic MCRred2 states, induced when HS-CoM (a reversible competitive inhibitor) and the second substrate HS-CoB or its analogue CH3-S-CoB are added to the enzyme in the active MCRred1 state (NiΙF430). Continuous wave and pulse EPR spectroscopy are used to show that the MCRred2a state exhibits a very large proton hyperfine interaction with principal values A(1H) = [−43,−42,−5] MHz and thus represents formally a NiΙΙΙF430 hydride complex formed by oxidative addition to NiΙ. In view of the known ability of nickel hydrides to activate methane, and the growing body of evidence for the involvement of MCR in “reverse” methanogenesis (anaerobic oxidation of methane), we believe that the nickel hydride complex reported here could play a key role in helping to understand both the mechanism of “reverse” and “forward” methanogenesis.
Keyword Catalyzing methane formation
X-Ray absorption
Ni-N bond
Methanobacterium thermoautotrophicum
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collection: Centre for Advanced Imaging Publications
 
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