Evidence map›Paper›PMID 33168889›Full record

ArticleScientific reports2020

In situ formation of photoactive B-ring reduced chlorophyll isomer in photosynthetic protein LH2.

Yoshitaka Saga, Yuji Otsuka, Daichi Funakoshi, Yuto Masaoka, Yu Kihara, Tsubasa Hidaka, Hiroka Hatano, Hitoshi Asakawa, Yutaka Nagasawa, Hitoshi Tamiaki

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.7field-weighted citation impact, top 32% 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

4 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
  2. Article
  3. Cryo-EM structures of light-harvesting 2 complexes fromProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  4. Article
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

10 authors at 3 institutions in 1 country.

Yoshitaka SagaDepartment of Chemistry, Faculty of Science and Engineering, Kindai University, Higashi-Osaka, Osaka, 577-8502, Japan. saga@chem.kindai.ac.jp.
Yuji OtsukaDepartment of Chemistry, Faculty of Science and Engineering, Kindai University, Higashi-Osaka, Osaka, 577-8502, Japan.
Daichi FunakoshiGraduate School of Life Sciences, Ritsumeikan University, Kusatsu, Shiga, 525-8577, Japan.
Yuto MasaokaGraduate School of Life Sciences, Ritsumeikan University, Kusatsu, Shiga, 525-8577, Japan.
Yu KiharaGraduate School of Life Sciences, Ritsumeikan University, Kusatsu, Shiga, 525-8577, Japan.
Tsubasa HidakaGraduate School of Life Sciences, Ritsumeikan University, Kusatsu, Shiga, 525-8577, Japan.
Hiroka HatanoGraduate School of Natural Science and Technology, Kanazawa University, Kanazawa, 920-1192, Japan.
Hitoshi AsakawaGraduate School of Natural Science and Technology, Kanazawa University, Kanazawa, 920-1192, Japan.
Yutaka NagasawaGraduate School of Life Sciences, Ritsumeikan University, Kusatsu, Shiga, 525-8577, Japan.
Hitoshi TamiakiGraduate School of Life Sciences, Ritsumeikan University, Kusatsu, Shiga, 525-8577, Japan.
Ritsumeikan University · JPKanazawa University · JPKindai University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Natural chlorophylls have a D-ring reduced chlorin π-system; however, no naturally occurring photosynthetically active B-ring reduced chlorins have been reported. Here we report a B-ring reduced chlorin, 17,18-didehydro-bacteriochlorophyll (BChl) a, produced by in situ oxidation of B800 bacteriochlorophyll (BChl) a in a light-harvesting protein LH2 from a purple photosynthetic bacterium Phaeospirillum molischianum. The regioselective oxidation of the B-ring of B800 BChl a is rationalized by its molecular orientation in the protein matrix. The formation of 17,18-didehydro-BChl a produced no change in the local structures and circular arrangement of the LH2 protein. The B-ring reduced 17,18-didehydro-BChl a functions as an energy donor in the LH2 protein. The photoactive B-ring reduced Chl isomer in LH2 will be helpful for understanding the photofunction and evolution of photosynthetic cyclic tetrapyrrole pigments.

Indexed as

Bacterial ProteinsBacteriochlorophyll ALight-Harvesting Protein ComplexesRhodobacter sphaeroidesRhodospirillaceaeBacterial ProteinsBacteriochlorophyll ALight-Harvesting Protein Complexes

Identifiers

PMID33168889
PMCPMC7652862
OpenAlexW3102784175

What OpenQuestion holds

Textmetadata
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.