NADP + Reduction with Reduced Ferredoxin and NADP + Reduction with NADH Are Coupled via an Electron-Bifurcating Enzyme Complex in Clostridium kluyveri
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It was recently found that the cytoplasmic butyryl-coenzyme A (butyryl-CoA) dehydrogenase-EtfAB complex from Clostridium kluyveri couples the exergonic reduction of crotonyl-CoA to butyryl-CoA with NADH and the endergonic reduction of ferredoxin with NADH via flavin-based electron bifurcation. We report here on a second cytoplasmic enzyme complex in C. kluyveri capable of energetic coupling via this novel mechanism. It was found that the purified iron-sulfur flavoprotein complex NfnAB couples the exergonic reduction of NADP + with reduced ferredoxin (Fd red ) and the endergonic reduction of NADP + with NADH in a reversible reaction: Fd red 2− + NADH + 2 NADP + + H + = Fd ox + NAD + + 2 NADPH. The role of this energy-converting enzyme complex in the ethanol-acetate fermentation of C. kluyveri is discussed.
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Soluble confurcation processes have already been described, such as those involving multimeric hydrogenases and the NfnAB transhydrogenase.
“Soluble confurcation processes have already been described, such as those involving multimeric hydrogenases (NADH and Fdred as electron donors for H2 production) [196] and the NfnAB transhydrogenase (NADH and Fdred as electron donors for NADP+ reduction) [89,198].”
From Early bioenergetic evolution (2013) · cites this paper as [198]
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- Authors
- Wang, S., Huang, H., Moll, J., & Thauer, R. K.
- Affiliations
- Max Planck Institute for Terrestrial Microbiology (DE)
- Venue
- Journal of Bacteriology
- Publisher
- American Society for Microbiology
- Published
- 2010-10
- Volume
- 192
- Issue
- 19
- Pages
- 5115-5123
- ISSN
- 0021-9193 (ISSN-L)
- 1098-5530
- PMC
- PMC2944534
- OpenAlex
- W1970604668
- Cited by
- 230
- References
- 2
- Citations by year
- 2026: 8 · 2025: 9 · 2024: 8 · 2023: 13 · 2022: 17 · 2021: 18 · 2020: 17 · 2019: 6 · 2018: 16 · 2017: 14 · 2016: 26 · 2015: 19 · 2014: 15 · 2013: 16 · 2012: 18
- FWCI
- 6.60
- Type
- journal article
- Language
- en
- Update notices
- correction (2015-01-21)
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Journal of Bacteriology (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Max Planck Institute for Plasma Physics (submittedVersion)
- MPG.PuRe (Max Planck Society) (submittedVersion)
- Funders
- Max-Planck-Gesellschaft
- Topics
- Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › Metalloenzymes and iron-sulfur proteins
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Microbial metabolism and enzyme function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Microbial Metabolic Engineering and Bioproduction
- Keywords
- NADP+ reduction, NADP+ reductase, electron bifurcation, ferredoxin, NADH, energy coupling, iron-sulfur flavoprotein, Clostridium kluyveri
- MeSH terms
- Acyl Coenzyme A, Bacterial Proteins, Ferredoxins, NAD, NADP, Oxidation-Reduction, Clostridium kluyveri
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