Document Detail


A methyl-CoM methylreductase system from methanogenic bacterium strain Gö 1 not requiring ATP for activity.
MedLine Citation:
PMID:  3197839     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Crude inside-out vesicles from the methanogenic strain Gö1 were prepared via protoplasts. These vesicles catalyzed methane formation from methyl-CoM and H2 at a maximal rate of 35 nmol/min.mg protein. Methane formation by the vesicles did not depend on the addition of ATP. This was in contrast to conventionally prepared crude extracts from the same organism or from Methanosarcina barkeri which exhibited strict ATP dependence of methanogenesis. ATP analogues inhibited methanogenesis by extracts to a much higher extent than that by vesicles. Both, particulate and soluble components prepared from the crude vesicles by ultracentrifugation were necessary for ATP-independent methane formation from methyl-CoM and H2. Hydrogenase activity was mainly associated with the particulate fraction whereas methyl-CoM methylreductase could be assigned to the soluble fraction. The detergent sulfobetaine inhibited methane formation from methyl-CoM without affecting hydrogenase or titanium citrate-dependent methylreductase activities, indicating that an additional membraneous component is involved in methanogenesis for methyl-CoM and H2.
Authors:
U Deppenmeier; M Blaut; A Jussofie; G Gottschalk
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  FEBS letters     Volume:  241     ISSN:  0014-5793     ISO Abbreviation:  FEBS Lett.     Publication Date:  1988 Dec 
Date Detail:
Created Date:  1989-01-25     Completed Date:  1989-01-25     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0155157     Medline TA:  FEBS Lett     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  60-4     Citation Subset:  IM    
Affiliation:
Institut für Mikrobiologie, Göttingen, FRG.
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MeSH Terms
Descriptor/Qualifier:
Adenosine Triphosphate / metabolism
Cell Membrane / enzymology
Cytoplasm / enzymology
Euryarchaeota / enzymology*
Kinetics
Multienzyme Complexes / metabolism*
Oxidoreductases / metabolism*
Chemical
Reg. No./Substance:
0/Multienzyme Complexes; 56-65-5/Adenosine Triphosphate; EC 1.-/Oxidoreductases; EC 1.-/methyl coenzyme M methylreductase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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