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Characterization of the MCRred2 form of methyl-coenzyme M reductase: a pulse EPR and ENDOR study.

Abstract:

Methyl-coenzyme M reductase (MCR), which catalyses the reduction of methyl-coenzyme M (CH(3)-S-CoM) with coenzyme B (H-S-CoB) to CH(4) and CoM-S-S-CoB, contains the nickel porphinoid F430 as prosthetic group. The active enzyme exhibits the Ni(I)-derived axial EPR signal MCR(red1) both in the absence and presence of the substrates. When the enzyme is competitively inhibited by coenzyme M (HS-CoM) the MCR(red1) signal is partially converted into the rhombic EPR signal MCR(red2). To obtain deepe...

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Publication status:
Published

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Publisher copy:
10.1007/s00775-003-0450-y

Authors


Finazzo, C More by this author
Mahlert, F 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:
8
Issue:
5
Pages:
586-593
Publication date:
2003-05-05
DOI:
EISSN:
1432-1327
ISSN:
0949-8257
URN:
uuid:c4398c08-a536-4d31-b37e-341083406bce
Source identifiers:
326034
Local pid:
pubs:326034

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