Evidence map›Paper›PMID 25978726›Full record

ArticleScientific reports2015

Rhodobacter sphaeroides mutants overexpressing chlorophyllide a oxidoreductase of Blastochloris viridis elucidate functions of enzymes in late bacteriochlorophyll biosynthetic pathways.

Yusuke Tsukatani, Jiro Harada, Jiro Nomata, Haruki Yamamoto, Yuichi Fujita, Tadashi Mizoguchi, Hitoshi Tamiaki

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

7 citing papers in PubMed, 20 citations in OpenAlex.

  1. Review
  2. Review
  3. ChlorophyllBiology · 2023
    Article
  4. Article
  5. Article
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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

7 authors at 3 institutions in 1 country.

Yusuke Tsukatani1] Graduate School of Life Sciences, Ritsumeikan University, Shiga 525-8577, Japan [2] PRESTO, Japan Science and Technology Agency, Saitama 332-0012, Japan [3] Earth-Life Science Institute, Tokyo Institute of Technology, Tokyo 152-8550, Japan.
Jiro HaradaDepartment of Medical Biochemistry, Kurume University School of Medicine, Fukuoka 830-0011, Japan.
Jiro NomataGraduate School of Bioagricultural Sciences, Nagoya University, Nagoya 464-8601, Japan.
Haruki YamamotoGraduate School of Bioagricultural Sciences, Nagoya University, Nagoya 464-8601, Japan.
Yuichi FujitaGraduate School of Bioagricultural Sciences, Nagoya University, Nagoya 464-8601, Japan.
Tadashi MizoguchiGraduate School of Life Sciences, Ritsumeikan University, Shiga 525-8577, Japan.
Hitoshi TamiakiGraduate School of Life Sciences, Ritsumeikan University, Shiga 525-8577, Japan.
Nagoya University · JPRitsumeikan University · JPKurume University Medical Center · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In previous studies we have demonstrated that chlorophyllide a oxidoreductases (CORs) from bacteriochlorophyll (BChl) a-producing Rhodobacter species and BChl b-producing Blastochloris viridis show distinct substrate recognition and different catalytic hydrogenation reactions, and that these two types of CORs therefore cause committed steps for BChls a and b biosynthesis. In this study, COR genes from B. viridis were incorporated and overexpressed in a series of Rhodobacter sphaeroides mutants. We found that the following two factors are essential in making R. sphaeroides produce BChl b: the loss of functions of both intrinsic COR and 8-vinyl reductase (BciA) in the host R. sphaeroides strain; and expression of the BchYZ catalytic components of COR from B. viridis, not the complete set of COR (BchXYZ), in the host strain. In addition, we incorporated bchYZ of B. viridis into the R. sphaeroides mutant lacking BchJ and BciA, resulting in the strain accumulating both BChl a and BChl b. This is the first example of an anoxygenic photosynthetic bacterium producing BChls a and b together. The results suggest that BchJ enhances activity of the intrinsic COR. The physiological significance of BchJ in pigment biosynthetic pathways will be discussed.

Indexed as

Biosynthetic PathwaysMutationBacteriochlorophyllsChromatography, High Pressure LiquidEnzyme ActivationGene ExpressionOxygenasesPigments, BiologicalRhodobacter sphaeroidesBacteriochlorophyllschlorophyll a oxygenaseOxygenasesPigments, Biological

Identifiers

PMID25978726
PMCPMC4432870
OpenAlexW1546006919

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Registered trials

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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.