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PMID: 7410369 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Role of component C in the methylreductase system of Methanobacterium.

The Journal of biological chemistry ·Vol. 255 ·No. 18 ·1980-09-25 ·Pages 8388-9

Ellefson WL, Wolfe RS

Abstract

A major simplification of the methyl coenzyme M methylreductase system of Methanobacterium has been effected. The 500,000-dalton hydrogenase complex has been replaced by an NADPH-coenzyme F420 oxidoreductase. By use of this electron-generating reaction, the methylreductase was found to be localized in component C, an acidic protein fraction. In the presence of the oxidoreductase and the methylreductase, formation of methane under a nitrogen atmosphere was dependent upon the addition of NADPH, coenzyme F420, component B (a new cofactor of unknown structure), ATP, Mg2+, and methyl coenzyme M.

MeSH Terms
Euryarchaeota/enzymology Hydrogen Kinetics Macromolecular Substances Molecular Weight NADP Oxidation-Reduction Oxidoreductases/metabolism
Chemicals
Macromolecular Substances NADP Hydrogen Oxidoreductases methyl coenzyme M methylreductase
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Ellefson W L
Wolfe R S
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
1980-09-25
Pages
8388-9
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
Grants
NIAID NIH HHS · AI 12277 · United States
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