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Two sub-states of the red2 state of methyl-coenzyme M reductase revealed by high-field EPR spectroscopy.

Abstract:

Methyl-coenzyme M reductase (MCR) catalyzes the formation of methane from methyl-coenzyme M and coenzyme B in methanogenic archaea. The enzyme has two structurally interlinked active sites embedded in an alpha(2)beta(2)gamma(2) subunit structure. Each active site has the nickel porphyrinoid F(430) as a prosthetic group. In the active state, F(430) contains the transition metal in the Ni(I) oxidation state. The active enzyme exhibits an axial Ni(I)-based continuous wave (CW) electron paramagne...

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Publication status:
Published

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Publisher copy:
10.1007/s00775-007-0281-3

Authors


Goenrich, M More by this author
Thauer, RK More by this author
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Journal:
Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry
Volume:
12
Issue:
8
Pages:
1097-1105
Publication date:
2007-11-05
DOI:
EISSN:
1432-1327
ISSN:
0949-8257
URN:
uuid:f22a349b-9dc1-42f9-b609-59ba6ef2b0f2
Source identifiers:
326043
Local pid:
pubs:326043

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