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Coordination and binding geometry of methyl-coenzyme M in the red1m state of methyl-coenzyme M reductase

Abstract:

Methane formation in methanogenic Archaea is catalyzed by methyl-coenzyme M reductase (MCR) and takes place via the reduction of methyl-coenzyme M (CH₃-S-CoM) with coenzyme B (HS-CoB) to methane and the heterodisulfide CoM-S-S-CoB. MCR harbors the nickel porphyrinoid conenzyme F⠄₃₀ as a prosthetic group, which has to be in the Ni(I) oxidation state for the enzyme to be active. To date no intermediates in the catalytic cycle of MCRred1 (red for reduced Ni) have been identified. Here...

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Publication status:
Published
Peer review status:
Peer reviewed

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Institution:
Max-Planck-Institut für Polymerforschung, Mainz, Germany
Role:
Author
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Institution:
ETH Zürich
Role:
Author
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Institution:
ETH Zürich
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Author
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Institution:
ETH Zürich
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Author
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Institution:
ETH Zürich
Role:
Author
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Name:
Deutsche Forschungsgemeinschaft
Funding agency for:
Hinderberger, D
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Name:
Engineering and Physical Sciences Research Council
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Name:
Biotechnology and Biological Sciences Research Council
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Name:
Fonds der Chemischen Industrie
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Name:
Swiss National Science Foundation
Publisher:
Springer
Journal:
Journal of Biological Inorganic Chemistry More from this journal
Volume:
13
Issue:
8
Pages:
1275-1289
Publication date:
2008-11-01
DOI:
EISSN:
1432-1327
ISSN:
0949-8257
Language:
English
Subjects:
UUID:
uuid:06e4e9e4-38d0-41ac-b967-3138dc8281c0
Local pid:
ora:4172
Deposit date:
2010-09-16

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