Evidence map›Paper›PMID 22557999›Full record

ArticleFrontiers in microbiology2012

Mutational Analyses of the Enzymes Involved in the Metabolism of Hydrogen by the Hyperthermophilic Archaeon Pyrococcus furiosus.

Gerrit J Schut, William J Nixon, Gina L Lipscomb, Robert A Scott, Michael W W Adams

Open access · goldAbstract read
In one paragraph

Article in Frontiers in microbiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

30 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Manipulating Fermentation Pathways in the Hyperthermophilic ArchaeonApplied and environmental microbiology · 2023
    Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. The Piezo-Hyperthermophilic ArchaeonFrontiers in microbiology · 2021
    Article
  13. Article
  14. Review
  15. Article
  16. Biotechnology of extremely thermophilic archaea.FEMS microbiology reviews · 2018
    Review
  17. Two functionally distinct NADPThe Journal of biological chemistry · 2017
    Article
  18. Radiation resistance in thermophiles: mechanisms and applications.World journal of microbiology & biotechnology · 2017
    Review
  19. Article
  20. Article
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 1 institution in 1 country.

Gerrit J SchutDepartment of Biochemistry and Molecular Biology, University of Georgia Athens, GA, USA.
William J Nixon
Gina L Lipscomb
Robert A Scott
Michael W W Adams
University of Georgia · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Pyrococcus furiosus grows optimally near 100°C by fermenting carbohydrates to produce hydrogen (H(2)) or, if elemental sulfur (S(0)) is present, hydrogen sulfide instead. It contains two cytoplasmic hydrogenases, SHI and SHII, that use NADP(H) as an electron carrier and a membrane-bound hydrogenase (MBH) that utilizes the redox protein ferredoxin. We previously constructed deletion strains lacking SHI and/or SHII and showed that they exhibited no obvious phenotype. This study has now been extended to include biochemical analyses and growth studies using the ΔSHI and ΔSHII deletion strains together with strains lacking a functional MBH (ΔmbhL). Hydrogenase activity in cytoplasmic extracts of various strains demonstrate that SHI is responsible for most of the cytoplasmic hydrogenase activity. The ΔmbhL strain showed no growth in the absence of S(0), confirming the hypothesis that, in the absence of S(0), MBH is the only enzyme that can dispose of reductant (in the form of H(2)) generated during sugar oxidation. Under conditions of limiting sulfur, a small but significant amount of H(2) was produced by the ΔmbhL strain, showing that SHI can produce H(2) from NADPH in vivo, although this does not enable growth of ΔmbhL in the absence of S(0). We propose that the physiological function of SHI is to recycle H(2) and provide a link between external H(2) and the intracellular pool of NADPH needed for biosynthesis. This likely has a distinct energetic advantage in the environment, but it is clearly not required for growth of the organism under the usual laboratory conditions. The function of SHII, however, remains unknown.

Indexed as

anaerobeenergy metabolismferredoxinhydrogenasePyrococcus furiosussulfurthermophile

Identifiers

PMID22557999
PMCPMC3341082
OpenAlexW1993943840

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
Read underepoch 390

Registered trials

None linked

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.