Evidence map›Paper›PMID 29603081›Full record

ArticlePhotosynthesis research2018

Evolution of photosynthetic reaction centers: insights from the structure of the heliobacterial reaction center.

Gregory S Orf, Christopher Gisriel, Kevin E Redding

Open access · greenAbstract read
PubMed Publisher
In one paragraph

Article in Photosynthesis research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
3.6field-weighted citation impact, top 6% 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

35 citing papers in PubMed, 78 citations in OpenAlex.

  1. Review
  2. Synthesis of bacteriochlorophyllChemical science · 2026
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  9. Illuminating the coevolution of photosynthesis and Bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2024
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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

3 authors at 1 institution in 1 country.

Gregory S OrfSchool of Molecular Sciences, Arizona State University, Tempe, AZ, 85287, USA.ORCID http://orcid.org/0000-0002-4853-8518
Christopher GisrielSchool of Molecular Sciences, Arizona State University, Tempe, AZ, 85287, USA.ORCID http://orcid.org/0000-0002-8011-0052
Kevin E ReddingSchool of Molecular Sciences, Arizona State University, Tempe, AZ, 85287, USA. kevin.redding@asu.edu.ORCID http://orcid.org/0000-0003-2819-4022
Arizona State University · US

Funding

U.S. Department of Energy DE-SC0010575
6 · The paper itself

Abstract

The proliferation of phototrophy within early-branching prokaryotes represented a significant step forward in metabolic evolution. All available evidence supports the hypothesis that the photosynthetic reaction center (RC)-the pigment-protein complex in which electromagnetic energy (i.e., photons of visible or near-infrared light) is converted to chemical energy usable by an organism-arose once in Earth's history. This event took place over 3 billion years ago and the basic architecture of the RC has diversified into the distinct versions that now exist. Using our recent 2.2-Å X-ray crystal structure of the homodimeric photosynthetic RC from heliobacteria, we have performed a robust comparison of all known RC types with available structural data. These comparisons have allowed us to generate hypotheses about structural and functional aspects of the common ancestors of extant RCs and to expand upon existing evolutionary schemes. Since the heliobacterial RC is homodimeric and loosely binds (and reduces) quinones, we support the view that it retains more ancestral features than its homologs from other groups. In the evolutionary scenario we propose, the ancestral RC predating the division between Type I and Type II RCs was homodimeric, loosely bound two mobile quinones, and performed an inefficient disproportionation reaction to reduce quinone to quinol. The changes leading to the diversification into Type I and Type II RCs were separate responses to the need to optimize this reaction: the Type I lineage added a [4Fe-4S] cluster to facilitate double reduction of a quinone, while the Type II lineage heterodimerized and specialized the two cofactor branches, fixing the quinone in the Q

Indexed as

Evolution, MolecularPhylogenyBacterial ProteinsCell MembraneCoenzymesCrystallography, X-RayEubacterialesModels, MolecularPhotosynthesisPhotosystem II Protein ComplexPhotosystem I Protein ComplexProtein MultimerizationQuinonesBacterial ProteinsCoenzymesPhotosystem II Protein ComplexPhotosystem I Protein ComplexQuinonesEvolution of photosynthesisHeliobacteriaPhotosynthesisReaction centerSequence alignmentsStructural alignments

Identifiers

PMID29603081
OpenAlexW2795223240

What OpenQuestion holds

Textmetadata
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.