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Methanogenic archaea: ecologically relevant differences in energy conservation
In methanogens with cytochromes, the first and last steps in methanogenesis from CO2 are coupled chemiosmotically, whereas in methenogens without cyto Chromes, these steps are energetically coupled by a cytoplasmic enzyme complex that mediates flavin-based electron bifurcation.
Biochemistry of methanogenesis: a tribute to Marjory Stephenson. 1998 Marjory Stephenson Prize Lecture.
  • R. Thauer
  • Biology
  • 1 September 1998
In 1933, Stephenson & Stickland published that they had isolated from river mud, by the single cell technique, a methanogenic organism capable of growth in an inorganic medium with formate as the sole carbon source.
Energy conservation in chemotrophic anaerobic bacteria.
This article corrects the article on p. 100 in vol.
A conspicuous nickel protein in microbial mats that oxidize methane anaerobically
The abundance of the nickel protein (7% of extracted proteins) in the mat suggests an important role in AOM, and similarities to methyl-coenzyme M reductase from methanogenic archaea are revealed.
Coupling of ferredoxin and heterodisulfide reduction via electron bifurcation in hydrogenotrophic methanogenic archaea
It is reported here that the purified complex from Methanothermobacter marburgensis catalyzes the CoM-S- S-CoB-dependent reduction of ferredoxin with H2, indicating an electron bifurcation coupling mechanism.
The genome of Clostridium kluyveri, a strict anaerobe with unique metabolic features
The genome sequence of C. kluyveri was reported, which revealed new insights into the metabolic capabilities of this well studied organism and suggested that the two enzymes, which are isolated together in a macromolecular complex, form a carboxysome-like structure.
Coupled Ferredoxin and Crotonyl Coenzyme A (CoA) Reduction with NADH Catalyzed by the Butyryl-CoA Dehydrogenase/Etf Complex from Clostridium kluyveri
Fredoxin reduction with NADH in cell extracts from Clostridium kluyveri is catalyzed by the butyryl-CoA dehydrogenase/Etf complex and the implications of this finding for the energy metabolism of butyrate-forming anaerobes are discussed in the accompanying paper.
Crystal structure of methyl-coenzyme M reductase: the key enzyme of biological methane formation.
Together with a second structurally characterized enzyme state (MCRsilent) containing the heterodisulfide of coenzymes M and B, a reaction mechanism is proposed that uses a radical intermediate and a nickel organic compound.