Evidence map›Paper›PMID 21828292›Full record

ArticleThe Plant cell2011

Cyanobacterial lactate oxidases serve as essential partners in N2 fixation and evolved into photorespiratory glycolate oxidases in plants.

Claudia Hackenberg, Ramona Kern, Jan Hüge, Lucas J Stal, Yoshinori Tsuji, Joachim Kopka, Yoshihiro Shiraiwa, Hermann Bauwe, Martin Hagemann

Open access · bronzeAbstract read
In one paragraph

Article in The Plant cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.1field-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

22 citing papers in PubMed, 53 citations in OpenAlex.

  1. Review
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  9. TheFrontiers in plant science · 2018
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  11. Diverse COFrontiers in microbiology · 2017
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  17. 2-Hydroxy Acids in Plant Metabolism.The arabidopsis book · 2015
    Article
  18. Article
  19. Review
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 4 institutions in 3 countries.

Claudia HackenbergUniversity of Rostock, Plant Physiology Department, 18051 Rostock, Germany.
Ramona Kern
Jan Hüge
Lucas J Stal
Yoshinori Tsuji
Joachim Kopka
Yoshihiro Shiraiwa
Hermann Bauwe
Martin Hagemann
University of Rostock · DEMax Planck Institute of Molecular Plant Physiology · DEUniversity of Tsukuba · JPNetherlands Institute of Ecology · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glycolate oxidase (GOX) is an essential enzyme involved in photorespiratory metabolism in plants. In cyanobacteria and green algae, the corresponding reaction is catalyzed by glycolate dehydrogenases (GlcD). The genomes of N(2)-fixing cyanobacteria, such as Nostoc PCC 7120 and green algae, appear to harbor genes for both GlcD and GOX proteins. The GOX-like proteins from Nostoc (No-LOX) and from Chlamydomonas reinhardtii showed high L-lactate oxidase (LOX) and low GOX activities, whereas glycolate was the preferred substrate of the phylogenetically related At-GOX2 from Arabidopsis thaliana. Changing the active site of No-LOX to that of At-GOX2 by site-specific mutagenesis reversed the LOX/GOX activity ratio of No-LOX. Despite its low GOX activity, No-LOX overexpression decreased the accumulation of toxic glycolate in a cyanobacterial photorespiratory mutant and restored its ability to grow in air. A LOX-deficient Nostoc mutant grew normally in nitrate-containing medium but died under N(2)-fixing conditions. Cultivation under low oxygen rescued this lethal phenotype, indicating that N(2) fixation was more sensitive to O(2) in the Δlox Nostoc mutant than in the wild type. We propose that LOX primarily serves as an O(2)-scavenging enzyme to protect nitrogenase in extant N(2)-fixing cyanobacteria, whereas in plants it has evolved into GOX, responsible for glycolate oxidation during photorespiration.

Indexed as

Alcohol OxidoreductasesAmino Acid SequenceArabidopsisBacterial ProteinsCell RespirationChlamydomonas reinhardtiiCyanobacteriaGlycolatesMixed Function OxygenasesMolecular Sequence DataMutationNitrogenaseNitrogen FixationNostocOxidation-ReductionOxygenAlcohol OxidoreductasesBacterial ProteinsGlycolatesglycollate oxidaselactate 2-monooxygenaseMixed Function OxygenasesNitrogenaseOxygenPlant Proteins

Identifiers

PMID21828292
PMCPMC3180805
OpenAlexW2099189524

What OpenQuestion holds

Textmetadata
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.