Evidence map›Paper›PMID 25002540›Full record

ArticleJournal of bacteriology2014

Evidence for a hexaheteromeric methylenetetrahydrofolate reductase in Moorella thermoacetica.

Johanna Mock, Shuning Wang, Haiyan Huang, Jörg Kahnt, Rudolf K Thauer

Open access · bronzeAbstract read
In one paragraph

Article in Journal of bacteriology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
5.6field-weighted citation impact, top 3% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

54 citing papers in PubMed, 101 citations in OpenAlex.

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  13. Deep-branching acetogens in serpentinized subsurface fluids of Oman.Proceedings of the National Academy of Sciences of the United States of America · 2022
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  16. Systems Biology on Acetogenic Bacteria for Utilizing C1 Feedstocks.Advances in biochemical engineering/biotechnology · 2022
    Article
  17. Is reduced ferredoxin the physiological electron donor for MetVF-type methylenetetrahydrofolate reductases in acetogenesis? A hypothesis.International microbiology : the official journal of the Spanish Society for Microbiology · 2022
    Article
  18. Review
  19. Review
  20. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 2 countries.

Johanna MockMax Planck Institute for Terrestrial Microbiology, Marburg, Germany.
Shuning WangMax Planck Institute for Terrestrial Microbiology, Marburg, Germany State Key Laboratory of Microbial Technology, Shandong University, Jinan, People's Republic of China.
Haiyan HuangMax Planck Institute for Terrestrial Microbiology, Marburg, Germany Institute of Basic Medicine, Shandong Academy of Medical Science, Jinan, People's Republic of China.
Jörg KahntMax Planck Institute for Terrestrial Microbiology, Marburg, Germany.
Rudolf K ThauerMax Planck Institute for Terrestrial Microbiology, Marburg, Germany thauer@mpi-marburg.mpg.de.
Max Planck Institute for Terrestrial Microbiology · DEShandong University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Moorella thermoacetica can grow with H₂ and CO₂, forming acetic acid from 2 CO₂ via the Wood-Ljungdahl pathway. All enzymes involved in this pathway have been characterized to date, except for methylenetetrahydrofolate reductase (MetF). We report here that the M. thermoacetica gene that putatively encodes this enzyme, metF, is part of a transcription unit also containing the genes hdrCBA, mvhD, and metV. MetF copurified with the other five proteins encoded in the unit in a hexaheteromeric complex with an apparent molecular mass in the 320-kDa range. The 40-fold-enriched preparation contained per mg protein 3.1 nmol flavin adenine dinucleotide (FAD), 3.4 nmol flavin mononucleotide (FMN), and 110 nmol iron, almost as predicted from the primary structure of the six subunits. It catalyzed the reduction of methylenetetrahydrofolate with reduced benzyl viologen but not with NAD(P)H in either the absence or presence of oxidized ferredoxin. It also catalyzed the reversible reduction of benzyl viologen with NADH (diaphorase activity). Heterologous expression of the metF gene in Escherichia coli revealed that the subunit MetF contains one FMN rather than FAD. MetF exhibited 70-fold-higher methylenetetrahydrofolate reductase activity with benzyl viologen when produced together with MetV, which in part shows sequence similarity to MetF. Heterologously produced HdrA contained 2 FADs and had NAD-specific diaphorase activity. Our results suggested that the physiological electron donor for methylenetetrahydrofolate reduction in M. thermoacetica is NADH and that the exergonic reduction of methylenetetrahydrofolate with NADH is coupled via flavin-based electron bifurcation with the endergonic reduction of an electron acceptor, whose identity remains unknown.

Indexed as

Bacterial ProteinsGene Expression Regulation, BacterialGene Expression Regulation, EnzymologicMethylenetetrahydrofolate Reductase (NADPH2)MoorellaBacterial ProteinsMethylenetetrahydrofolate Reductase (NADPH2)

Identifiers

PMID25002540
PMCPMC4135698
OpenAlexW2161914201

What OpenQuestion holds

Textmetadata
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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.