The DOI matches its Crossref record; 74 of the 74 references it cites were found in a registry or an index.
Electron Bifurcation Involved in the Energy Metabolism of the Acetogenic Bacterium Moorella thermoacetica Growing on Glucose or H 2 plus CO 2
Open accessAbstract
Moorella thermoacetica ferments glucose to three acetic acids. In the oxidative part of the fermentation, the hexose is converted to 2 acetic acids and 2 CO 2 molecules with the formation of 2 NADH and 2 reduced ferredoxin (Fd red 2− ) molecules. In the reductive part, 2 CO 2 molecules are reduced to acetic acid, consuming the 8 reducing equivalents generated in the oxidative part. An open question is how the two parts are electronically connected, since two of the four oxidoreductases involved in acetogenesis from CO 2 are NADP specific rather than NAD specific. We report here that the 2 NADPH molecules required for CO 2 reduction to acetic acid are generated by the reduction of 2 NADP + molecules with 1 NADH and 1 Fd red 2− catalyzed by the electron-bifurcating NADH-dependent reduced ferredoxin:NADP + oxidoreductase (NfnAB). The cytoplasmic iron-sulfur flavoprotein was heterologously produced in Escherichia coli , purified, and characterized. The purified enzyme was composed of 30-kDa (NfnA) and 50-kDa (NfnB) subunits in a 1-to-1 stoichiometry. NfnA harbors a [2Fe2S] cluster and flavin adenine dinucleotide (FAD), and NfnB harbors two [4Fe4S] clusters and FAD. M. thermoacetica contains a second electron-bifurcating enzyme. Cell extracts catalyzed the coupled reduction of NAD + and Fd with 2 H 2 molecules. The specific activity of this cytoplasmic enzyme was 3-fold higher in H 2 -CO 2 -grown cells than in glucose-grown cells. The function of this electron-bifurcating hydrogenase is not yet clear, since H 2 -CO 2 -grown cells additionally contain high specific activities of an NADP + -dependent hydrogenase that catalyzes the reduction of NADP + with H 2 . This activity is hardly detectable in glucose-grown cells.
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“Of energetic consequence, the formation of the formyl pterin formyl-H4F is endergonic, requiring ATP hydrolysis, while the 5,10-methylene-H4F reductase step is highly exergonic (–57 kJ mol−1) [73] and is suspected to be a site of energy conservation in some acetogen species [89].”
From Early bioenergetic evolution (2013) · cites this paper as [89]
In the citing paper
“The cytochrome-containing acetogens such as Moorella, in particular, come to mind in this respect, because they contain menaquinone, but there is yet no obvious role for it in core metabolism [89].”
From Early bioenergetic evolution (2013) · cites this paper as [89]
In the citing paper
“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 [89]
In the citing paper
“Homologues of HdrABC are found in other organisms, including at least one cytochrome-containing acetogen, Moorella thermoacetica [89], and many proteobacterial and clostridial sulfate reducers [172].”
From Early bioenergetic evolution (2013) · cites this paper as [89]
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Self-citation
Research works printed but not linked: 1
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Frontiers, Opportunities, and Challenges in Biochemical and Chemical Catalysis of CO 2 Fixation
Appel, A. M., Bercaw, J. E., Bocarsly, A. B., Dobbek, H., DuBois, D. L., Dupuis, M., Ferry, J. G., Fujita, E., Hille, R., Kenis, P. J. A., et al. (2013) · Chemical Reviews · doi:10.1021/cr300463y · Cited by 2,193
Self-citationSchuchmann, K., & Müller, V. (2014) · Nature Reviews Microbiology · doi:10.1038/nrmicro3365 · Cited by 845
Buckel, W., & Thauer, R. K. (2013) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2012.07.002 · Cited by 797
Self-citationKracke, F., Vassilev, I., & Krömer, J. O. (2015) · Frontiers in Microbiology · doi:10.3389/fmicb.2015.00575 · Cited by 748
How to make a living from anaerobic ammonium oxidation
Kartal, B., de Almeida, N. M., Maalcke, W. J., den Camp, H. J. M. O., Jetten, M. S. M., & Keltjens, J. T. (2012) · FEMS Microbiology Reviews · doi:10.1111/1574-6976.12014 · Cited by 602
Metadata
- Authors
- Huang, H., Wang, S., Moll, J., & Thauer, R. K.
- Affiliations
- Max Planck Institute for Terrestrial Microbiology (DE)
- Shandong University (CN)
- Venue
- Journal of Bacteriology
- Publisher
- American Society for Microbiology
- Published
- 2012-07-15
- Volume
- 194
- Issue
- 14
- Pages
- 3689-3699
- ISSN
- 0021-9193 (ISSN-L)
- 1098-5530
- PMC
- PMC3393501
- OpenAlex
- W2117142868
- Cited by
- 177
- References
- 74
- Citations by year
- 2026: 12 · 2025: 6 · 2024: 12 · 2023: 9 · 2022: 8 · 2021: 13 · 2020: 6 · 2019: 13 · 2018: 15 · 2017: 15 · 2016: 16 · 2015: 18 · 2014: 15 · 2013: 12 · 2012: 7
- FWCI
- 6.38
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Bacteriology (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Max Planck Institute for Plasma Physics (submittedVersion)
- MPG.PuRe (Max Planck Society) (submittedVersion)
- Funders
- Max-Planck-Gesellschaft
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Metalloenzymes and iron-sulfur proteins
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Microbial metabolism and enzyme function
- Physical Sciences › Environmental Science › Environmental Engineering › Microbial Fuel Cells and Bioremediation
- Keywords
- electron bifurcation, Moorella thermoacetica, acetogenesis, hydrogenase, NADPH production, ferredoxin, iron-sulfur flavoprotein, glucose fermentation, energy metabolism, NADH oxidation
- MeSH terms
- Carbon Dioxide, Electrons, Energy Metabolism, Glucose, Hydrogen, Molecular Sequence Data, Oxidoreductases, Gene Expression Regulation, Bacterial, Gene Expression Regulation, Enzymologic, Moorella
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