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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.
A 3-Hydroxypropionate/4-Hydroxybutyrate Autotrophic Carbon Dioxide Assimilation Pathway in Archaea
The Global Ocean Sampling database contains half as many 4-hydroxybutyryl-CoA dehydratase sequences as compared with those found for another key photosynthetic CO2-fixing enzyme, ribulose-1,5-bisphosphate carboxylase-oxygenase, indicating the importance of this enzyme in global carbon cycling.
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.
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.
Energy Conservation via Electron-Transferring Flavoprotein in Anaerobic Bacteria
Energy conservation in chemotrophic organisms is generally coupled to redox reactions in catabolic pathways. In the oxidative part or branch, “energy-rich” compounds are formed, from which ATP is
Flavin-Based Electron Bifurcation, A New Mechanism of Biological Energy Coupling.
The crystal structures and electron transport of EtfAB-butyryl-CoA dehydrogenase and NfnAB are compared with those of complex III of the respiratory chain (cytochrome bc1), whereby unexpected common features have become apparent.
Propionate oxidation in Escherichia coli: evidence for operation of a methylcitrate cycle in bacteria
The results indicate that E. coli oxidises propionate to pyruvate via the methylcitrate cycle known from yeast.
On the mechanism of action of the antifungal agent propionate.
  • M. Brock, W. Buckel
  • Biology, Computer Science
    European journal of biochemistry
  • 1 August 2004
Data are presented that correlate inhibition of fungal polyketide synthesis by propionyl-CoA with the accumulation of this CoA-derivative, and a possible toxicity of propionate for humans in diseases such as propionic acidaemia and methylmalonic aciduria is discussed.
2-Methylisocitrate lyases from the bacterium Escherichia coli and the filamentous fungus Aspergillus nidulans: characterization and comparison of both enzymes.
In Escherichia coli and Aspergillus nidulans, propionate is oxidized to pyruvate via the methylcitrate cycle, the last step of which is catalysed by 2-methylisocitrate lyase, a native homotetrameric structure as identified by size-exclusion chromatography.