Evidence map›Paper›PMID 20463892›Full record

ArticlePloS one2010

Heterologous expression and maturation of an NADP-dependent [NiFe]-hydrogenase: a key enzyme in biofuel production.

Junsong Sun, Robert C Hopkins, Francis E Jenney, Patrick M McTernan, Michael W W Adams

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
5.2field-weighted citation impact, top 5% 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

24 citing papers in PubMed, 93 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Protein Engineering of the Soluble Metal-dependent Formate Dehydrogenase from Escherichia coli.Analytical sciences : the international journal of the Japan Society for Analytical Chemistry · 2021
    Article
  6. Review
  7. Article
  8. Article
  9. The multifaceted benefits of protein co-expression in Escherichia coli.Journal of visualized experiments : JoVE · 2015
    Article
  10. Review
  11. NADPH-generating systems in bacteria and archaea.Frontiers in microbiology · 2015
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Extreme Thermophiles: Moving beyond single-enzyme biocatalysis.Current opinion in chemical engineering · 2012
    Article
  18. 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.

Junsong SunDepartment of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia, United States of America.
Robert C Hopkins
Francis E Jenney
Patrick M McTernan
Michael W W Adams
University of Georgia · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Hydrogen gas is a major biofuel and is metabolized by a wide range of microorganisms. Microbial hydrogen production is catalyzed by hydrogenase, an extremely complex, air-sensitive enzyme that utilizes a binuclear nickel-iron [NiFe] catalytic site. Production and engineering of recombinant [NiFe]-hydrogenases in a genetically-tractable organism, as with metalloprotein complexes in general, has met with limited success due to the elaborate maturation process that is required, primarily in the absence of oxygen, to assemble the catalytic center and functional enzyme. We report here the successful production in Escherichia coli of the recombinant form of a cytoplasmic, NADP-dependent hydrogenase from Pyrococcus furiosus, an anaerobic hyperthermophile. This was achieved using novel expression vectors for the co-expression of thirteen P. furiosus genes (four structural genes encoding the hydrogenase and nine encoding maturation proteins). Remarkably, the native E. coli maturation machinery will also generate a functional hydrogenase when provided with only the genes encoding the hydrogenase subunits and a single protease from P. furiosus. Another novel feature is that their expression was induced by anaerobic conditions, whereby E. coli was grown aerobically and production of recombinant hydrogenase was achieved by simply changing the gas feed from air to an inert gas (N2). The recombinant enzyme was purified and shown to be functionally similar to the native enzyme purified from P. furiosus. The methodology to generate this key hydrogen-producing enzyme has dramatic implications for the production of hydrogen and NADPH as vehicles for energy storage and transport, for engineering hydrogenase to optimize production and catalysis, as well as for the general production of complex, oxygen-sensitive metalloproteins.

Indexed as

BiofuelsAmino Acid SequenceBase Sequencebeta-GalactosidaseEscherichia coliHydrogenaseMolecular Sequence DataNADPPlasmidsPromoter Regions, GeneticPyrococcus furiosusRecombinant Proteinsbeta-GalactosidaseBiofuelsHydrogenaseNADPnickel-iron hydrogenaseRecombinant Proteins

Identifiers

PMID20463892
PMCPMC2865534
OpenAlexW1999299765

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.