Evidence map›Paper›PMID 30710189›Full record

ArticlePhotosynthesis research2019

Energy transfer from chlorophyll f to the trapping center in naturally occurring and engineered Photosystem I complexes.

Vasily Kurashov, Ming-Yang Ho, Gaozhong Shen, Karla Piedl, Tatiana N Laremore, Donald A Bryant, John H Golbeck

Abstract read
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In one paragraph

Article in Photosynthesis research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
3.2field-weighted citation impact, top 7% 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

25 citing papers in PubMed, 57 citations in OpenAlex.

  1. Structure and evolution of photosystem I in the early-branching cyanobacteriumProceedings of the National Academy of Sciences of the United States of America · 2025
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  5. Adaptation processes inFrontiers in plant science · 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

7 authors at 1 institution in 1 country.

Vasily KurashovDepartment of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA, 16802, USA.
Ming-Yang HoDepartment of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA, 16802, USA.
Gaozhong ShenDepartment of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA, 16802, USA.
Karla PiedlDepartment of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA, 16802, USA.
Tatiana N LaremoreProteomics and Mass Spectrometry Core Facility, The Huck Institutes for the Life Sciences, The Pennsylvania State University, University Park, PA, 16802, USA.
Donald A BryantDepartment of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA, 16802, USA.
John H GolbeckDepartment of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA, 16802, USA. jhg5@psu.edu.
Pennsylvania State University · US

Funding

Division of Molecular and Cellular Biosciences MCB-1613022
6 · The paper itself

Abstract

Certain cyanobacteria can thrive in environments enriched in far-red light (700-800 nm) due to an acclimation process known as far-red light photoacclimation (FaRLiP). During FaRLiP, about 8% of the Chl a molecules in the photosystems are replaced by Chl f and a very small amount of Chl d. We investigated the spectroscopic properties of Photosystem I (PSI) complexes isolated from wild-type (WT) Synechococcus sp. PCC 7335 and a chlF mutant strain (lacking Chl f synthase) grown in white and far-red light (WL-PSI and FRL-PSI, respectively). WT-FRL-PSI complexes contain Chl f and Chl a but not Chl d. The light-minus dark difference spectrum of the trapping center at high spectral resolution indicates that the special pair in WT-FRL-PSI consists of Chl a molecules with maximum bleaching at 703-704 nm. The action spectrum for photobleaching of the special pair showed that Chl f molecules absorbing at wavelengths up to 800 nm efficiently transfer energy to the trapping center in FRL-PSI complexes to produce a charge-separated state. This is ~ 50 nm further into the near IR than WL-PSI; Chl f has a quantum yield equivalent to that of Chl a in the antenna, i.e., ~ 1.0. PSI complexes from Synechococcus 7002 carrying 3.8 Chl f molecules could promote photobleaching of the special pair by energy transfer at wavelengths longer than WT PSI complexes. Results from these latter studies are directly relevant to the issue of whether introduction of Chl f synthase into plants could expand the wavelength range available for oxygenic photosynthesis in crop plants.

Indexed as

Energy TransferAcclimatizationChlorophyllLightPhotosynthesisPhotosystem I Protein ComplexSynechococcusChlorophyllchlorophyll fPhotosystem I Protein ComplexAction spectrumChlorophyllChlorophyll f synthaseCyanobacteriaFaRLiPFar-red light photoacclimationPhotosynthesisPhotosystem IQuantum yieldSynechococcus sp. PCC 7002Synechococcus sp. PCC 7335

Identifiers

PMID30710189
OpenAlexW2914273510

What OpenQuestion holds

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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.