Evidence map›Paper›PMID 16228425›Full record

ArticlePhotosynthesis research2000

The IdiA protein of Synechococcus sp. PCC 7942 functions in protecting the acceptor side of Photosystem II under oxidative stress.

P Exss-Sonne, J Tölle, K P Bader, E K Pistorius, K P Michel

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Article in Photosynthesis research, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

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0cells of the map it votes in
12citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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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

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3 · Its place in the literature

Who cites it

12 citing papers in PubMed.

  1. A redox switch allows binding of Fe(II) and Fe(III) ions in the cyanobacterial iron-binding protein FutA fromProceedings of the National Academy of Sciences of the United States of America · 2024
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4 · The record

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5 · Who and what money

Authors and funding

5 authors.

P Exss-SonneBiologie VIII: Zellphysiologie, Universität Bielefeld, 33501, Bielefeld, Germany.
J Tölle
K P Bader
E K Pistorius
K P Michel

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Synechococcus sp. strains PCC 7942 and PCC 6301 contain a 35 kDa protein called IdiA (Iron deficiency induced protein A) that is expressed in elevated amounts under Fe deficiency and to a smaller extent also under Mn deficiency. Absence of this protein was shown to mainly damage Photosystem II. To decide whether IdiA has a function in optimizing and/or protecting preferentially either the donor or acceptor side reaction of Photosystem II, a comparative analysis was performed of Synechococcus sp. PCC 7942 wild-type, the IdiA-free mutant, the previously constructed PsbO-free Synechococcus PCC 7942 mutant and a newly constructed Synechococcus PCC 7942 double mutant lacking both PsbO and IdiA. Measurements of the chlorophyll fluorescence and determinations of Photosystem II activity using a variety of electron acceptors gave evidence that IdiA has its main function in protecting the acceptor side of Photosystem II. Especially, the use of dichlorobenzoquinone, preferentially accepting electrons from Q(A), gave a decreased O(2) evolving activity in the IdiA-free mutant. Investigations of the influence of hydrogen peroxide treatment on cells revealed that this treatment caused a significantly higher damage of Photosystem II in the IdiA-free mutant than in wild-type. These results suggest that although the IdiA protein is not absolutely required for Photosystem II activity in Synechococcus PCC 7942, it does play an important role in protecting the acceptor side against oxidative damage.

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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.