Evidence map›Paper›PMID 32210238›Full record

ArticleNature communications2020

Polychromatic solar energy conversion in pigment-protein chimeras that unite the two kingdoms of (bacterio)chlorophyll-based photosynthesis.

Juntai Liu, Vincent M Friebe, Raoul N Frese, Michael R Jones

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

15 citing papers in PubMed, 41 citations in OpenAlex.

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  10. A bound iron porphyrin is redox active in hybrid bacterial reaction centers modified to possess a four-helix bundle domain.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2022
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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

4 authors at 1 institution in 1 country.

Juntai LiuSchool of Biochemistry, Faculty of Life Sciences, Biomedical Sciences Building, University of Bristol, University Walk, Bristol, BS8 1TD, UK.ORCID http://orcid.org/0000-0003-2692-7093
Vincent M FriebeDepartment of Physics and Astronomy, LaserLaB Amsterdam, VU University Amsterdam, De Boelelaan 1081, Amsterdam, 1081 HV, The Netherlands.ORCID http://orcid.org/0000-0002-4277-8473
Raoul N FreseDepartment of Physics and Astronomy, LaserLaB Amsterdam, VU University Amsterdam, De Boelelaan 1081, Amsterdam, 1081 HV, The Netherlands.
Michael R JonesSchool of Biochemistry, Faculty of Life Sciences, Biomedical Sciences Building, University of Bristol, University Walk, Bristol, BS8 1TD, UK. m.r.jones@bristol.ac.uk.ORCID http://orcid.org/0000-0002-8063-0744
University of Bristol · GB

Funding

Biotechnology and Biological Sciences Research Council BB/L01386X/1
6 · The paper itself

Abstract

Natural photosynthesis can be divided between the chlorophyll-containing plants, algae and cyanobacteria that make up the oxygenic phototrophs and a diversity of bacteriochlorophyll-containing bacteria that make up the anoxygenic phototrophs. Photosynthetic light harvesting and reaction centre proteins from both kingdoms have been exploited for solar energy conversion, solar fuel synthesis and sensing technologies, but the energy harvesting abilities of these devices are limited by each protein's individual palette of pigments. In this work we demonstrate a range of genetically-encoded, self-assembling photosystems in which recombinant plant light harvesting complexes are covalently locked with reaction centres from a purple photosynthetic bacterium, producing macromolecular chimeras that display mechanisms of polychromatic solar energy harvesting and conversion. Our findings illustrate the power of a synthetic biology approach in which bottom-up construction of photosystems using naturally diverse but mechanistically complementary components can be achieved in a predictable fashion through the encoding of adaptable, plug-and-play covalent interfaces.

Indexed as

Solar EnergyArabidopsis ProteinsBacterial ProteinsBacteriochlorophyllsCarotenoidsLight-Harvesting Protein ComplexesRecombinant Fusion ProteinsRhodobacter sphaeroidesSunlightSynthetic BiologyArabidopsis ProteinsBacterial ProteinsBacteriochlorophyllsCAB2 protein, ArabidopsisCarotenoidsLight-Harvesting Protein ComplexesRecombinant Fusion Proteins

Identifiers

PMID32210238
PMCPMC7093453
OpenAlexW3013871991

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.