Evidence map›Paper›PMID 27122573›Full record

ArticleJournal of experimental botany2016

Improved analysis of C4 and C3 photosynthesis via refined in vitro assays of their carbon fixation biochemistry.

Robert E Sharwood, Balasaheb V Sonawane, Oula Ghannoum, Spencer M Whitney

Open access · hybridAbstract read
In one paragraph

Article in Journal of experimental botany, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
6.1field-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

38 citing papers in PubMed, 99 citations in OpenAlex.

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  17. Distinct CPlant direct · 2021
    Article
  18. Sucrose Utilization for Improved Crop Yields: A Review Article.International journal of molecular sciences · 2021
    Review
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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

4 authors at 3 institutions in 1 country.

Robert E SharwoodARC Centre of Excellence for Translational Photosynthesis, Research School of Biology, Australian National University, Canberra ACT 2601, Australia robert.sharwood@anu.edu.au.
Balasaheb V SonawaneARC Centre of Excellence for Translational Photosynthesis, Hawkesbury Institute for the Environment, Western Sydney University, Richmond NSW 2753, Australia.
Oula GhannoumARC Centre of Excellence for Translational Photosynthesis, Hawkesbury Institute for the Environment, Western Sydney University, Richmond NSW 2753, Australia.
Spencer M WhitneyARC Centre of Excellence for Translational Photosynthesis, Research School of Biology, Australian National University, Canberra ACT 2601, Australia.
Western Sydney University · AUARC Centre of Excellence for Transformative Meta-Optical Systems · AUAustralian National University · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Plants operating C3 and C4 photosynthetic pathways exhibit differences in leaf anatomy and photosynthetic carbon fixation biochemistry. Fully understanding this underpinning biochemical variation is requisite to identifying solutions for improving photosynthetic efficiency and growth. Here we refine assay methods for accurately measuring the carboxylase and decarboxylase activities in C3 and C4 plant soluble protein. We show that differences in plant extract preparation and assay conditions are required to measure NADP-malic enzyme and phosphoenolpyruvate carboxylase (pH 8, Mg(2+), 22 °C) and phosphoenolpyruvate carboxykinase (pH 7, >2mM Mn(2+), no Mg(2+)) maximal activities accurately. We validate how the omission of MgCl2 during leaf protein extraction, lengthy (>1min) centrifugation times, and the use of non-pure ribulose-1,5-bisphosphate (RuBP) significantly underestimate Rubisco activation status. We show how Rubisco activation status varies with leaf ontogeny and is generally lower in mature C4 monocot leaves (45-60% activation) relative to C3 monocots (55-90% activation). Consistent with their >3-fold lower Rubisco contents, full Rubisco activation in soluble protein from C4 leaves (<5min) was faster than in C3 plant samples (<10min), with addition of Rubisco activase not required for full activation. We conclude that Rubisco inactivation in illuminated leaves primarily stems from RuBP binding to non-carbamylated enzyme, a state readily reversible by dilution during cellular protein extraction.

Indexed as

Carbon DioxideIn Vitro TechniquesMalate Dehydrogenase (NADP+)NicotianaPanicumPhosphoenolpyruvate Carboxykinase (ATP)PhotosynthesisPlant LeavesPoaceaeRibulose-Bisphosphate CarboxylaseTriticumZea maysCarbon DioxideMalate Dehydrogenase (NADP+)Phosphoenolpyruvate Carboxykinase (ATP)Ribulose-Bisphosphate CarboxylaseCarbamylationcarbon fixationCO2-concentrating mechanismphotosynthesisRubiscoRubisco activase.

Identifiers

PMID27122573
PMCPMC4867899
OpenAlexW2343690410

What OpenQuestion holds

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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.