Coupled Ferredoxin and Crotonyl Coenzyme A (CoA) Reduction with NADH Catalyzed by the Butyryl-CoA Dehydrogenase/Etf Complex from Clostridium kluyveri
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Cell extracts of butyrate-forming clostridia have been shown to catalyze acetyl-coenzyme A (acetyl-CoA)- and ferredoxin-dependent formation of H 2 from NADH. It has been proposed that these bacteria contain an NADH:ferredoxin oxidoreductase which is allosterically regulated by acetyl-CoA. We report here that ferredoxin reduction with NADH in cell extracts from Clostridium kluyveri is catalyzed by the butyryl-CoA dehydrogenase/Etf complex and that the acetyl-CoA dependence previously observed is due to the fact that the cell extracts catalyze the reduction of acetyl-CoA with NADH via crotonyl-CoA to butyryl-CoA. The cytoplasmic butyryl-CoA dehydrogenase complex was purified and is shown to couple the endergonic reduction of ferredoxin (E 0 ′ = −410 mV) with NADH (E 0 ′ = −320 mV) to the exergonic reduction of crotonyl-CoA to butyryl-CoA (E 0 ′ = −10 mV) with NADH. The stoichiometry of the fully coupled reaction is extrapolated to be as follows: 2 NADH + 1 oxidized ferredoxin + 1 crotonyl-CoA = 2 NAD + + 1 ferredoxin reduced by two electrons + 1 butyryl-CoA. The implications of this finding for the energy metabolism of butyrate-forming anaerobes are discussed in the accompanying paper.
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Chemolithoautotrophs perform flavin-based electron bifurcation to reduce CO2 with electrons from H2.
“The answer, which only recently became apparent and is an exciting development in energetics, is that they perform a reaction called flavin-based electron bifurcation [143,158].”
From Early bioenergetic evolution (2013) · cites this paper as [158]
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- Authors
- Li, F., Hinderberger, J., Seedorf, H., Zhang, J., Buckel, W., & Thauer, R. K.
- Affiliations
- Max Planck Institute for Terrestrial Microbiology (DE)
- Philipps University of Marburg (DE)
- Venue
- Journal of Bacteriology
- Publisher
- American Society for Microbiology
- Published
- 2008-02
- Volume
- 190
- Issue
- 3
- Pages
- 843-850
- ISSN
- 0021-9193 (ISSN-L)
- 1098-5530
- PMC
- PMC2223550
- OpenAlex
- W2100769504
- Cited by
- 420
- References
- 2
- Citations by year
- 2026: 18 · 2025: 13 · 2024: 12 · 2023: 24 · 2022: 24 · 2021: 30 · 2020: 26 · 2019: 27 · 2018: 25 · 2017: 20 · 2016: 32 · 2015: 23 · 2014: 25 · 2013: 28 · 2012: 20
- FWCI
- 10.34
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Journal of Bacteriology (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Max-Planck-Gesellschaft
- Topics
- Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › Metalloenzymes and iron-sulfur proteins
- Physical Sciences › Engineering › Building and Construction › Anaerobic Digestion and Biogas Production
- Physical Sciences › Environmental Science › Environmental Engineering › Microbial Fuel Cells and Bioremediation
- Keywords
- butyryl-CoA dehydrogenase, electron transfer flavoprotein, ferredoxin reduction, NADH, crotonyl-CoA, acetyl-CoA, Clostridium kluyveri, energy metabolism
- MeSH terms
- Acyl Coenzyme A, Catalysis, Ferredoxins, Hydrogen, NAD, Oxidation-Reduction, Butyryl-CoA Dehydrogenase, Electron-Transferring Flavoproteins, Clostridium kluyveri
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