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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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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