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

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 MCR red2 states, induced when HS-CoM ...

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Publication status:
Published

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Publisher copy:
10.1021/ja710949e

Authors


Finazzo, C More by this author
Piskorski, R More by this author
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Journal:
Journal of the American Chemical Society
Volume:
130
Issue:
33
Pages:
10907-10920
Publication date:
2008-08-05
DOI:
EISSN:
1520-5126
ISSN:
0002-7863
URN:
uuid:0c7a486d-72e1-4f74-9937-23eea2665d3a
Source identifiers:
254678
Local pid:
pubs:254678

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