Bacterial Na + -translocating ferredoxin:NAD + oxidoreductase
Open accessAbstract
The anaerobic acetogenic bacterium Acetobacterium woodii carries out a unique type of Na + -motive, anaerobic respiration with caffeate as electron acceptor, termed “caffeate respiration.” Central, and so far the only identified membrane-bound reaction in this respiration pathway, is a ferredoxin:NAD + oxidoreductase (Fno) activity. Here we show that inverted membrane vesicles of A. woodii couple electron transfer from reduced ferredoxin to NAD + with the transport of Na + from the outside into the lumen of the vesicles. Na + transport was electrogenic, and accumulation was inhibited by sodium ionophores but not protonophores, demonstrating a direct coupling of Fno activity to Na + transport. Results from inhibitor studies are consistent with the hypothesis that Fno activity coupled to Na + translocation is catalyzed by the Rnf complex, a membrane-bound, iron–sulfur and flavin-containing electron transport complex encoded by many bacterial and some archaeal genomes. Fno is a unique type of primary Na + pump and represents an early evolutionary mechanism of energy conservation that expands the redox range known to support life. In addition, it explains the lifestyle of many anaerobic bacteria and gives a mechanistic explanation for the enigma of the energetic driving force for the endergonic reduction of ferredoxin with NADH plus H + as reductant in a number of aerobic bacteria.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Fdred is the substrate for a membrane-bound protein called Rnf that generates NADH and pumps about one Na+ ion per electron transferred, thus generating the ion gradient harnessed by the ATPase, which requires about 4 Na+ ions per ATP.
“Fdred is the substrate for a membrane-bound protein called Rnf [147] that generates NADH and pumps, in the process, about one Na+ ion per electron transferred, thus generating the ion gradient that is harnessed by the ATPase, which requires about 4 Na+ ions per ATP.”
From Early bioenergetic evolution (2013) · cites this paper as [147]
Oxidation of Fdred by a pumping complex such as Rnf or the Ech hydrogenase couples the electron bifurcation mechanism to chemiosmotic energy conservation.
“Oxidation of Fdred by a pumping complex such as Rnf [147] or the Ech hydrogenase [159] couples the electron bifurcation mechanism to chemiosmotic energy conservation (figure 4).”
From Early bioenergetic evolution (2013) · cites this paper as [147]
Electron transfer from ferredoxin to NAD+ drives the extrusion of Na+ via Rnf.
“Electron transfer from ferredoxin to NAD+ drives the extrusion of Na+ via Rnf [147].”
From Early bioenergetic evolution (2013) · cites this paper as [147]
Cites
Energy conservation in chemotrophic anaerobic bacteria
Thauer, R. K., Jungermann, K., & Decker, K. (1977) · Bacteriological Reviews · doi:10.1128/br.41.1.100-180.1977 · Cited by 4,146 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Ecological Aspects of the Distribution of Different Autotrophic CO <sub>2</sub> Fixation Pathways
Berg, I. A. (2011) · Applied and Environmental Microbiology · doi:10.1128/aem.02473-10 · Cited by 821 · see citing works
Buckel, W., & Thauer, R. K. (2013) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2012.07.002 · Cited by 797 · see citing works
Alternative Pathways of Carbon Dioxide Fixation: Insights into the Early Evolution of Life?
Fuchs, G. (2011) · Annual Review of Microbiology · doi:10.1146/annurev-micro-090110-102801 · Cited by 726 · see citing works
Liew, F., Martin, M. E., Tappel, R. C., Heijstra, B. D., Mihalcea, C., & Köpke, M. (2016) · Frontiers in Microbiology · doi:10.3389/fmicb.2016.00694 · Cited by 485 · see citing works
Commercial Biomass Syngas Fermentation.
Daniell, J., Köpke, M., & Simpson, S. (2012) · Energies · doi:10.3390/en5125372 · Cited by 444 · see citing works
Chen, L., Zhernakova, D. V., Kurilshikov, A., Andreu-Sánchez, S., Wang, D., Augustijn, H. E., Vich Vila, A., Study, L. C., Weersma, R. K., Medema, M. H., et al. (2022) · Nature Medicine · doi:10.1038/s41591-022-02014-8 · Cited by 327 · see citing works
Sousa, F. L., Thiergart, T., Landan, G., Nelson-Sathi, S., Pereira, I. A. C., Allen, J. F., Lane, N., & Martin, W. F. (2013) · Philosophical Transactions of the Royal Society B: Biological Sciences · doi:10.1098/rstb.2013.0088 · Cited by 286 · see citing works
Poehlein, A., Schmidt, S., Kaster, A.-K., Goenrich, M., Vollmers, J., Thürmer, A., Bertsch, J., Schuchmann, K., Voigt, B., Hecker, M., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0033439 · Cited by 274 · see citing works
Self-citationA Bacterial Electron-bifurcating Hydrogenase
Schuchmann, K., & Müller, V. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.395038 · Cited by 218 · see citing works
Self-citationLatif, H., Zeidan, A. A., Nielsen, A. T., & Zengler, K. (2014) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2013.12.001 · Cited by 199 · see citing works
Huang, H., Wang, S., Moll, J., & Thauer, R. K. (2012) · Journal of Bacteriology · doi:10.1128/jb.00385-12 · Cited by 177 · see citing works
Electron bifurcation: A long-hidden energy-coupling mechanism
Müller, V., Chowdhury, N. P., & Basen, M. (2018) · Annual Review of Microbiology · doi:10.1146/annurev-micro-090816-093440 · Cited by 159 · see citing works
Self-citationMarcellin, E., Behrendorff, J. B., Nagaraju, S., DeTissera, S., Segovia, S., Palfreyman, R. W., Daniell, J., Licona-Cassani, C., Quek, L.-E., Speight, R., et al. (2016) · Green Chemistry · doi:10.1039/c5gc02708j · Cited by 159 · see citing works
Callaghan, A. V., Morris, B. E. L., Pereira, I. A. C., McInerney, M. J., Austin, R. N., Groves, J. T., Kukor, J. J., Suflita, J. M., Young, L. Y., Zylstra, G. J., et al. (2012) · Environmental Microbiology · doi:10.1111/j.1462-2920.2011.02516.x · Cited by 159 · see citing works
Schönheit, P., Buckel, W., & Martin, W. F. (2016) · Trends in Microbiology · doi:10.1016/j.tim.2015.10.003 · Cited by 156 · see citing works
Wang, S., Huang, H., Kahnt, J., & Thauer, R. K. (2013) · Journal of Bacteriology · doi:10.1128/jb.02158-12 · Cited by 140 · see citing works
Early Microbial Evolution: The Age of Anaerobes
Martin, W. F., & Sousa, F. L. (2016) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a018127 · Cited by 129 · see citing works
Martin, W. F. (2012) · FEBS Letters · doi:10.1016/j.febslet.2011.09.031 · Cited by 108 · see citing works
Sousa, F. L., & Martin, W. F. (2014) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2014.02.001 · Cited by 100 · see citing works
Poehlein, A., Cebulla, M., Ilg, M. M., Bengelsdorf, F. R., Schiel-Bengelsdorf, B., Whited, G., Andreesen, J. R., Gottschalk, G., Daniel, R., & Dürre, P. (2015) · mBio · doi:10.1128/mbio.01168-15 · Cited by 80 · see citing works
Iron Regulation in Clostridioides difficile
Berges, M., Michel, A.-M., Lassek, C., Nuss, A. M., Beckstette, M., Dersch, P., Riedel, K., Sievers, S., Becher, D., Otto, A., et al. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.03183 · Cited by 63 · see citing works
- Authors
- Biegel, E., & Müller, V.
- Affiliations
- Goethe University Frankfurt (DE)
- Corresponding author
- Müller, Volker
- ORCID
- Müller, Volker
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2010-10-04
- Volume
- 107
- Issue
- 42
- Pages
- 18138-18142
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC2964206
- OpenAlex
- W2035252706
- Cited by
- 262
- References
- 1
- Citations by year
- 2026: 7 · 2025: 7 · 2024: 7 · 2023: 15 · 2022: 18 · 2021: 14 · 2020: 19 · 2019: 21 · 2018: 14 · 2017: 10 · 2016: 28 · 2015: 25 · 2014: 21 · 2013: 20 · 2012: 17
- FWCI
- 17.22
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Deutsche Forschungsgemeinschaft
- Topics
- Physical Sciences › Environmental Science › Environmental Engineering › Microbial Fuel Cells and Bioremediation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › Metalloenzymes and iron-sulfur proteins
- Keywords
- Acetobacterium woodii, anaerobic respiration, sodium transport, electrogenic transport, inverted membrane vesicles, Rnf complex, iron-sulfur flavoprotein, electron transfer, energy conservation, anaerobic bacteria
- MeSH terms
- Biological Evolution, Ferredoxins, NADH Dehydrogenase, Sodium, Ion Transport, Acetobacterium
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review