Evidence map›Paper›PMID 29545812›Full record

ArticleFrontiers in plant science2018

Directions for Optimization of Photosynthetic Carbon Fixation: RuBisCO's Efficiency May Not Be So Constrained After All.

Peter L Cummins, Babu Kannappan, Jill E Gready

Abstract read
In one paragraph

Article in Frontiers in plant science, 2018. 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
–field-weighted citation impact
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.

  1. Article
  2. Review
  3. bioRxiv : the preprint server for biology · 2026
    Article
  4. Review
  5. Review
  6. Review
  7. Light-emitting plants development by inoculating of Vibrio campbellii RMT1 on the rhizospheric zone of Aglaonema cochinchinense.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2024
    Article
  8. Rubisco is evolving for improved catalytic efficiency and COProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  9. Engineering Rubisco to enhance COSynthetic and systems biotechnology · 2024
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. A computational walk to the hidden peaks of protein performance.Synthetic biology (Oxford, England) · 2021
    Article
  16. Review
  17. Article
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  19. Review
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors.

Peter L CumminsGready Group, Department of Genome Science, John Curtin School of Medical Research, Australian National University, Canberra, ACT, Australia.
Babu KannappanGready Group, Department of Genome Science, John Curtin School of Medical Research, Australian National University, Canberra, ACT, Australia.
Jill E GreadyGready Group, Department of Genome Science, John Curtin School of Medical Research, Australian National University, Canberra, ACT, Australia.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The ubiquitous enzyme Ribulose 1,5-bisphosphate carboxylase-oxygenase (RuBisCO) fixes atmospheric carbon dioxide within the Calvin-Benson cycle that is utilized by most photosynthetic organisms. Despite this central role, RuBisCO's efficiency surprisingly struggles, with both a very slow turnover rate to products and also impaired substrate specificity, features that have long been an enigma as it would be assumed that its efficiency was under strong evolutionary pressure. RuBisCO's substrate specificity is compromised as it catalyzes a side-fixation reaction with atmospheric oxygen; empirical kinetic results show a trend to tradeoff between relative specificity and low catalytic turnover rate. Although the dominant hypothesis has been that the active-site chemistry constrains the enzyme's evolution, a more recent study on RuBisCO stability and adaptability has implicated competing selection pressures. Elucidating these constraints is crucial for directing future research on improving photosynthesis, as the current literature casts doubt on the potential effectiveness of site-directed mutagenesis to improve RuBisCO's efficiency. Here we use regression analysis to quantify the relationships between kinetic parameters obtained from empirical data sets spanning a wide evolutionary range of RuBisCOs. Most significantly we found that the rate constant for dissociation of CO

Indexed as

carbon fixationenzyme-complex stabilityenzyme kinetics and specificityevolutionary constraintsgas-substrate bindingphotosynthesisprotein evolutionRuBisCO

Identifiers

PMID29545812
PMCPMC5838012

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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.