Evidence map›Paper›PMID 26887804›Full record

ArticleScientific reports2016

The N-terminal sequence of the extrinsic PsbP protein modulates the redox potential of Cyt b559 in photosystem II.

Taishi Nishimura, Ryo Nagao, Takumi Noguchi, Jon Nield, Fumihiko Sato, Kentaro Ifuku

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

16 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Review
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  13. Antimycin A inhibits cytochrome bPhotosynthesis research · 2019
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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

6 authors at 3 institutions in 2 countries.

Taishi NishimuraGraduate School of Biostudies, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan.
Ryo NagaoGraduate School of Science, Nagoya University, Aichi 464-8602, Japan.
Takumi NoguchiGraduate School of Science, Nagoya University, Aichi 464-8602, Japan.
Jon NieldSchool of Biological and Chemical Sciences, Queen Mary University of London, London E1 4NS, United Kingdom.
Fumihiko SatoGraduate School of Biostudies, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan.
Kentaro IfukuGraduate School of Biostudies, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan.
Kyoto University · JPNagoya University · JPQueen Mary University of London · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The PsbP protein, an extrinsic subunit of photosystem II (PSII) in green plants, is known to induce a conformational change around the catalytic Mn4CaO5 cluster securing the binding of Ca(2+) and Cl(-) in PSII. PsbP has multiple interactions with the membrane subunits of PSII, but how these affect the structure and function of PSII requires clarification. Here, we focus on the interactions between the N-terminal residues of PsbP and the α subunit of Cytochrome (Cyt) b559 (PsbE). A key observation was that a peptide fragment formed of the first N-terminal 15 residues of PsbP, 'pN15', was able to convert Cyt b559 into its HP form. Interestingly, addition of pN15 to NaCl-washed PSII membranes decreased PSII's oxygen-evolving activity, even in the presence of saturating Ca(2+) and Cl(-) ions. In fact, pN15 reversibly inhibited the S1 to S2 transition of the OEC in PSII. These data suggest that pN15 can modulate the redox property of Cyt b559 involved in the side-electron pathway in PSII. This potential change of Cyt b559, in the absence of the C-terminal domain of PsbP, however, would interfere with any electron donation from the Mn4CaO5 cluster, leading to the possibility that multiple interactions of PsbP, binding to PSII, have distinct roles in regulating electron transfer within PSII.

Indexed as

Cytochrome b GroupOxidation-ReductionPhotosystem II Protein ComplexProtein DomainsSpinacia oleraceacytochrome b559Cytochrome b GroupPhotosystem II Protein Complex

Identifiers

PMID26887804
PMCPMC4757834
OpenAlexW2280774878

What OpenQuestion holds

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LicenceCC BY
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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.